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Volumn 77, Issue 2, 2013, Pages 277-321

Acyltransferases in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ACYLTRANSFERASE ATFA; BACTERIAL ENZYME; CHLORAMPHENICOL ACETYLTRANSFERASE; ESTER; GLYCEROL 3 PHOSPHATE ACYLTRANSFERASE; HISTIDINE; LEUKOTOXIN; LIPID A; LYSOPHOSPHATIDIC ACID; PHA SYNTHASE; POLYESTER; POLYKETIDE; RHAMNOLIPID; RTXC ACYLTRANSFERASE; SYNTHETASE; THIOESTER; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; WAX ESTER;

EID: 84878215672     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00010-13     Document Type: Review
Times cited : (129)

References (312)
  • 1
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • DOI 10.1146/annurev.biochem.74.082803.133524
    • White SW, Zheng J, Zhang YM, Rock CO. 2005. The structural biology of the type II fatty acid biosynthesis. Annu. Rev. Biochem. 74:791-831. (Pubitemid 40995524)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.-M.3    Rock, C.O.4
  • 2
    • 0141566277 scopus 로고    scopus 로고
    • Transmembrane movement of exogenous long-chain fatty acids: Proteins, enzymes, and vectorial esterification
    • DOI 10.1128/MMBR.67.3.454-472.2003
    • Black PN, DiRusso CC. 2003. Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification. Microbiol. Mol. Biol. Rev. 67:454-472. (Pubitemid 37122529)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.3 , pp. 454-472
    • Black, P.N.1    DiRusso, C.C.2
  • 3
    • 77955481009 scopus 로고    scopus 로고
    • Current understanding of fatty acid biosynthesis and the acyl carrier protein
    • Chan DI, Vogel HJ. 2010. Current understanding of fatty acid biosynthesis and the acyl carrier protein. Biochem. J. 430:1-19.
    • (2010) Biochem. J. , vol.430 , pp. 1-19
    • Chan, D.I.1    Vogel, H.J.2
  • 4
    • 0027751310 scopus 로고
    • Structure, function and biogenesis of storage lipid bodies and oleosins in plants
    • DOI 10.1016/0163-7827(93)90009-L
    • Murphy DJ. 1993. Structure, function and biogenesis of storage lipid bodies and oleosins in plants. Prog. Lipid Res. 32:247-280. (Pubitemid 24020883)
    • (1993) Progress in Lipid Research , vol.32 , Issue.3 , pp. 247-280
    • Murphy, D.J.1
  • 5
    • 18944391677 scopus 로고    scopus 로고
    • Neutral lipid bodies in prokaryotes: Recent insights into structure, formation, and relationship to eukaryotic lipid depots
    • Wältermann M, Steinbüchel A. 2005. Neutral lipid bodies in prokaryotes: recent insights into structure, formation, and relationship to eukaryotic lipid depots. J. Bacteriol. 187:3607-3619.
    • (2005) J. Bacteriol. , vol.187 , pp. 3607-3619
    • Wältermann, M.1    Steinbüchel, A.2
  • 6
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • Anderson AJ, Dawes EA. 1990. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol. Rev. 54:450-472. (Pubitemid 120004382)
    • (1990) Microbiological Reviews , vol.54 , Issue.4 , pp. 450-472
    • Anderson, A.J.1    Dawes, E.A.2
  • 7
    • 4444272576 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis: II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family
    • DOI 10.1074/jbc.M406226200
    • Cheng JB, Russell DW. 2004. Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase gene family. J. Biol. Chem. 279:37798-37807. (Pubitemid 39195494)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37798-37807
    • Cheng, J.B.1    Russell, D.W.2
  • 8
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • DOI 10.1016/S0163-7827(01)00013-3, PII S0163782701000133
    • Murphy DJ. 2001. The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40:325-438. (Pubitemid 32727212)
    • (2001) Progress in Lipid Research , vol.40 , Issue.5 , pp. 325-438
    • Murphy, D.J.1
  • 9
    • 43049180903 scopus 로고    scopus 로고
    • Sealing plant surfaces: Cuticular wax formation by epidermal cells
    • DOI 10.1146/annurev.arplant.59.103006.093219
    • Samuels L, Kunst L, Jetter R. 2008. Sealing plant surfaces: cuticular wax formation by epidermal cells. Annu. Rev. Plant Biol. 59:683-707. (Pubitemid 351813047)
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 683-707
    • Samuels, L.1    Kunst, L.2    Jetter, R.3
  • 10
    • 0012046831 scopus 로고
    • Lipids and membranes
    • Voet D, Voet JG (ed), Wiley, New York, NY
    • Voet D, Voet JG. 1990. Lipids and membranes, p 271-314. In Voet D, Voet JG (ed), Biochemistry. Wiley, New York, NY.
    • (1990) Biochemistry , pp. 271-314
    • Voet, D.1    Voet, J.G.2
  • 13
    • 55549115700 scopus 로고    scopus 로고
    • Identification of the wax ester synthase/acyl-coenzyme a:diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis
    • DOI 10.1104/pp.108.123471
    • Li F, Wu X, Lam P, Bird D, Zheng H, Samuels L, Jetter R, Kunst L. 2008. Identification of the wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase WSD1 required for stem wax ester biosynthesis in Arabidopsis. Plant Physiol. 148:97-107. (Pubitemid 352847579)
    • (2008) Plant Physiology , vol.148 , Issue.1 , pp. 97-107
    • Li, F.1    Wu, X.2    Lam, P.3    Bird, D.4    Zheng, H.5    Samuels, L.6    Jetter, R.7    Kunst, L.8
  • 14
    • 0000959782 scopus 로고
    • Biosynthesis of wax in the honeybee, Apis mellifera L
    • Blomquist GJ, Chu AJ, Remaley S. 1980. Biosynthesis of wax in the honeybee, Apis mellifera L. Insect Biochem. 10:313-321.
    • (1980) Insect Biochem. , vol.10 , pp. 313-321
    • Blomquist, G.J.1    Chu, A.J.2    Remaley, S.3
  • 15
    • 0000967012 scopus 로고
    • Beeswax: Structure of the esters and their component hydroxy acids and diols
    • Tulloch AP. 1971. Beeswax: structure of the esters and their component hydroxy acids and diols. Chem. Phys. Lipids. 6:235-265.
    • (1971) Chem. Phys. Lipids. , vol.6 , pp. 235-265
    • Tulloch, A.P.1
  • 16
    • 0001389261 scopus 로고
    • Function of the spermaceti organ of the sperm whale
    • Clarke MR. 1970. Function of the spermaceti organ of the sperm whale. Nature 228:873-874.
    • (1970) Nature , vol.228 , pp. 873-874
    • Clarke, M.R.1
  • 17
    • 0033765914 scopus 로고    scopus 로고
    • Purification of a Jojoba embryo wax synthase, cloning of its cDNA, and production of high levels of wax in seeds of transgenic Arabidopsis
    • Lardizabal KD, Metz JG, Sakamoto T, Hutton WC, Pollard MR, Lassner MW. 2000. Purification of a Jojoba embryo wax synthase, cloning of its cDNA, and production of high levels of wax in seeds of transgenic Arabidopsis. Plant Physiol. 122:645-655.
    • (2000) Plant Physiol. , vol.122 , pp. 645-655
    • Lardizabal, K.D.1    Metz, J.G.2    Sakamoto, T.3    Hutton, W.C.4    Pollard, M.R.5    Lassner, M.W.6
  • 18
    • 0030163048 scopus 로고    scopus 로고
    • Formation of intracytoplasmic lipid inclusions by Rhodococcus opacus strain PD630
    • Alvarez HM, Mayer F, Fabritius D, Steinbüchel A. 1996. Formation of intracytoplasmic lipid inclusions by Rhodococcus opacus strain PD630. Arch. Microbiol. 165:377-386. (Pubitemid 126423390)
    • (1996) Archives of Microbiology , vol.165 , Issue.6 , pp. 377-386
    • Alvarez, H.M.1    Mayer, F.2    Fabritius, D.3    Steinbuchel, A.4
  • 19
    • 0017056496 scopus 로고
    • Solubilization of diglyceride acyltransferase from the membrane of Mycobacterium smegmatis
    • Akao T, Kusaka T. 1976. Solubilization of diglyceride acyltransferase from membrane of Mycobacterium smegmatis. J. Biochem. 80:723-728. (Pubitemid 8014820)
    • (1976) Journal of Biochemistry , vol.80 , Issue.4 , pp. 723-728
    • Akao, T.1    Kusaka, T.2
  • 20
    • 0000210119 scopus 로고    scopus 로고
    • Accumulation of storage lipids in species of Rhodococcus and Nocardia and effects of inhibitors and polyethylene glycol
    • Alvarez HM, Kalscheuer R, Steinbüchel A. 1997. Accumulation of storage lipids in species of Rhodococcus and Nocardia and effects of inhibitors and polyethylene glycol. Fett/Lipid. 99:239-246.
    • (1997) Fett/Lipid. , vol.99 , pp. 239-246
    • Alvarez, H.M.1    Kalscheuer, R.2    Steinbüchel, A.3
  • 23
    • 0005164230 scopus 로고
    • Lipid biosynthesis by actinomycetes cultivated on different media
    • Koval'schuk LP, Donets AP, Razumovskii PN. 1973. Lipid biosynthesis by actinomycetes cultivated on different media. Mikrobiol. Int. 42:567-571.
    • (1973) Mikrobiol. Int. , vol.42 , pp. 567-571
    • Koval'schuk, L.P.1    Donets, A.P.2    Razumovskii, P.N.3
  • 24
    • 0039585100 scopus 로고
    • Bacterial production of fats and oils
    • Ratledge C, Dawson P, Rattray J. (ed), American Oil Chemists Society, Champaign, IL
    • Wayman M, Jenkins AD, Kormendy AG. 1984. Bacterial production of fats and oils, p 129-143. In Ratledge C, Dawson P, Rattray J. (ed), Biotechnology for the oils and fat industry. American Oil Chemists Society, Champaign, IL.
    • (1984) Biotechnology for the Oils and Fat Industry , pp. 129-143
    • Wayman, M.1    Jenkins, A.D.2    Kormendy, A.G.3
  • 25
    • 0022977499 scopus 로고
    • Structure, distribution and function of wax esters in Acinetobacter calcoaceticus
    • Fixter LM, Nagi MN, McCormack JG, Fewson CA. 1986. Structure, distribution and function of wax esters in Acinetobacter calcoaceticus. J. Gen. Microbiol. 132:3147-3157. (Pubitemid 17185861)
    • (1986) Journal of General Microbiology , vol.132 , Issue.11 , pp. 3147-3157
    • Fixter, L.M.1    Nagi, M.N.2    McCormack, J.G.3    Fewson, C.A.4
  • 27
    • 0016436552 scopus 로고
    • Comparative analysis of lipids of Acinetobacter species grown on hexadecane
    • Makula RA, Lockwood PJ, Finnerty WR. 1975. Comparative analysis of lipids of Acinetobacter species grown on hexadecane. J. Bacteriol. 121:303-312.
    • (1975) J. Bacteriol. , vol.121 , pp. 303-312
    • Makula, R.A.1    Lockwood, P.J.2    Finnerty, W.R.3
  • 29
    • 1642482765 scopus 로고    scopus 로고
    • Submersed culture production of extracellular wax esters by the marine bacterium Fundibacter jadensis
    • Bredemeier R, Hulsch R, Metzger JO, Berthe-Corti L. 2003. Submersed culture production of extracellular wax esters by the marine bacterium Fundibacter jadensis. Mar. Biotechnol. 5:579-588.
    • (2003) Mar. Biotechnol. , vol.5 , pp. 579-588
    • Bredemeier, R.1    Hulsch, R.2    Metzger, J.O.3    Berthe-Corti, L.4
  • 30
  • 31
    • 0015130119 scopus 로고
    • Occurrence of waxes in Acinetobacter
    • Gallagher IHC. 1971. Occurrence of waxes in Acinetobacter. J. Gen. Microbiol. 68:245-247.
    • (1971) J. Gen. Microbiol. , vol.68 , pp. 245-247
    • Gallagher, I.H.C.1
  • 32
    • 34248384746 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoid wax ester in Marinobacter hydrocarbonoclasticus DSM 8798: Identification and characterization of isoprenoid coenzyme a synthetase and wax ester syethases
    • DOI 10.1128/JB.01932-06
    • Holtzapple E, Schmidt-Dannert C. 2007. Biosynthesis of isoprenoid wax ester in Marinobacter hydrocarbonoclasticus DSM 8798: identification and characterization of isoprenoid coenzyme A synthetase and wax ester synthases. J. Bacteriol. 189:3804-3812. (Pubitemid 46740178)
    • (2007) Journal of Bacteriology , vol.189 , Issue.10 , pp. 3804-3812
    • Holtzapple, E.1    Schmidt-Dannert, C.2
  • 33
    • 0018971654 scopus 로고
    • The effect of growth temperature on wax ester composition in the psychrophilic bacterium Micrococcus cryophilus ATCC 15174
    • Russell NJ, Volkman JK. 1980. The effect of growth temperature and wax ester composition in the psychrophilic bacterium Micrococcus cryophilus ATCC 15174. J. Gen. Microbiol. 118:131-141. (Pubitemid 10013774)
    • (1980) Journal of General Microbiology , vol.118 , Issue.1 , pp. 131-141
    • Russell, N.J.1    Volkman, J.K.2
  • 34
    • 0016177564 scopus 로고
    • Identification of n-decane oxidation products in Corynebacterium cultures by combined gas chromatography mass spectrometry
    • Bacchin P, Robertiello A, Viglia A. 1974. Identification of n-decane oxidation products in Corynebacterium cultures by combined gas chromatography mass spectrometry. Appl. Microbiol. 28:737-741.
    • (1974) Appl. Microbiol. , vol.28 , pp. 737-741
    • Bacchin, P.1    Robertiello, A.2    Viglia, A.3
  • 35
    • 70449312593 scopus 로고
    • n-Alkane utilization and lipid formation by a Nocardia
    • Raymond RL, Davies JB. 1960. n-Alkane utilization and lipid formation by a Nocardia. Appl. Microbiol. 8:329-334.
    • (1960) Appl. Microbiol. , vol.8 , pp. 329-334
    • Raymond, R.L.1    Davies, J.B.2
  • 36
    • 70349591123 scopus 로고    scopus 로고
    • The application of biotechnological methods for the synthesis of biodiesel
    • Adamczak M, Bornscheuer UT, Bednarski W. 2009. The application of biotechnological methods for the synthesis of biodiesel. Eur. J. Lipid Sci. Technol. 111:808-813.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 808-813
    • Adamczak, M.1    Bornscheuer, U.T.2    Bednarski, W.3
  • 37
    • 66349139329 scopus 로고    scopus 로고
    • New microbial fuels: A biotech perspective
    • Rude MA, Schirmer A. 2009. New microbial fuels: a biotech perspective. Curr. Opin. Microbiol. 12:274-281.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 274-281
    • Rude, M.A.1    Schirmer, A.2
  • 38
    • 80052720279 scopus 로고    scopus 로고
    • Production of wax esters by bacteria
    • Timmis KN (ed), Springer-Verlag, Berlin, Germany
    • Rontani JF. 2010. Production of wax esters by bacteria, p 460-470. In Timmis KN (ed), Handbook of hydrocarbon and lipid microbiology. Springer-Verlag, Berlin, Germany.
    • (2010) Handbook of Hydrocarbon and Lipid Microbiology , pp. 460-470
    • Rontani, J.F.1
  • 39
    • 0242298277 scopus 로고    scopus 로고
    • Industrial use of lipases to produce fatty acid esters
    • DOI 10.1002/ejlt.200300853
    • Hills G. 2003. Industrial use of lipases to produce fatty acid esters. Eur. J. Lipid Sci. Technol. 105:601-607. (Pubitemid 37363266)
    • (2003) European Journal of Lipid Science and Technology , vol.105 , Issue.10 , pp. 601-607
    • Hills, G.1
  • 41
    • 45549087079 scopus 로고    scopus 로고
    • Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels
    • Stöveken T, Steinbüchel A. 2008. Bacterial acyltransferases as an alternative for lipase-catalyzed acylation for the production of oleochemicals and fuels. Angew Chem. Int. Ed. Engl. 47:3688-3694.
    • (2008) Angew Chem. Int. Ed. Engl. , vol.47 , pp. 3688-3694
    • Stöveken, T.1    Steinbüchel, A.2
  • 42
    • 33748762752 scopus 로고    scopus 로고
    • Microdiesel: Escherichia coli engineered for fuel production
    • Kalscheuer R, Stölting T, Steinbüchel A. 2006. Microdiesel: Escherichia coli engineered for fuel production. Microbiology 152:2529-2536.
    • (2006) Microbiology , vol.152 , pp. 2529-2536
    • Kalscheuer, R.1    Stölting, T.2    Steinbüchel, A.3
  • 44
  • 45
    • 0018846846 scopus 로고
    • Enzymes of glycerolipid synthesis in eukaryotes
    • Bell RM, Coleman RA. 1980. Enzymes of glycerolipid synthesis in eukaryotes. Annu. Rev. Biochem. 49:459-487.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 459-487
    • Bell, R.M.1    Coleman, R.A.2
  • 49
    • 84863478799 scopus 로고    scopus 로고
    • Multifunctional acyltransferases from Tetrahymena thermophila
    • Biester EM, Hellenbrand J, Frentzen M. 2012. Multifunctional acyltransferases from Tetrahymena thermophila. Lipids 47:371-381.
    • (2012) Lipids , vol.47 , pp. 371-381
    • Biester, E.M.1    Hellenbrand, J.2    Frentzen, M.3
  • 51
    • 0037424538 scopus 로고    scopus 로고
    • A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase mediates wax ester and triacylglycerol biosynthesis in Acinetobacter calcoaceticus ADP1
    • Kalscheuer R, Steinbüchel A. 2003. A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase mediates wax ester and triacylglycerol biosynthesis in Acinetobacter calcoaceticus ADP1. J. Biol. Chem. 278:8075-8082.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8075-8082
    • Kalscheuer, R.1    Steinbüchel, A.2
  • 52
    • 77949875486 scopus 로고    scopus 로고
    • Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters
    • Teerawanichpan P, Qiu X. 2010. Fatty acyl-CoA reductase and wax synthase from Euglena gracilis in the biosynthesis of medium-chain wax esters. Lipids 45:263-273.
    • (2010) Lipids , vol.45 , pp. 263-273
    • Teerawanichpan, P.1    Qiu, X.2
  • 53
    • 34250025178 scopus 로고    scopus 로고
    • Cuticular wax biosynthesis in petunia petals: Cloning and characterization of an alcohol-acyltransferase that synthesizes wax-esters
    • DOI 10.1007/s00425-007-0489-z
    • King A, Nam JW, Han J, Hilliard J, Jaworski JG. 2007. Cuticular wax biosynthesis in petunia petals: cloning and characterization of an alcohol-acyltransferase that synthesizes wax-esters. Planta 226:381-394. (Pubitemid 46889517)
    • (2007) Planta , vol.226 , Issue.2 , pp. 381-394
    • King, A.1    Nam, J.-W.2    Han, J.3    Hilliard, J.4    Jaworski, J.G.5
  • 54
    • 14544268951 scopus 로고    scopus 로고
    • The wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1: Characterization of a novel type of acyltransferase
    • Stöveken T, Kalscheuer R, Malkus U, Reichelt R, Steinbüchel A. 2005. The wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1: characterization of a novel type of acyltransferase. J. Bacteriol. 187:1369-1376.
    • (2005) J. Bacteriol. , vol.187 , pp. 1369-1376
    • Stöveken, T.1    Kalscheuer, R.2    Malkus, U.3    Reichelt, R.4    Steinbüchel, A.5
  • 55
    • 0037482236 scopus 로고
    • Substrate-dependent and growth temperature dependent changes in the wax ester compositions produced by Acinetobacter sp. HO1-N
    • Ratledge C, Dawson P, Rattray L (ed), American Oil Chemists Society, Champaign, IL
    • Ervin JL, Geigert J, Neidleman SL, Wadsworth J. 1984. Substrate-dependent and growth temperature dependent changes in the wax ester compositions produced by Acinetobacter sp. HO1-N, p 217-222. In Ratledge C, Dawson P, Rattray L (ed), Biotechnology of the oil and fats industry. American Oil Chemists Society, Champaign, IL.
    • (1984) Biotechnology of the Oil and Fats Industry , pp. 217-222
    • Ervin, J.L.1    Geigert, J.2    Neidleman, S.L.3    Wadsworth, J.4
  • 56
    • 0242329840 scopus 로고    scopus 로고
    • In vitro and in vivo biosynthesis of wax diesters by an unspecific bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter calcoaceticus ADP1
    • DOI 10.1002/ejlt.200300840
    • Kalscheuer R, Uthoff S, Luftmann H, Steinbüchel A. 2003. In vitro and in vivo biosynthesis of wax diesters by an unspecific bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase from Acinetobacter calcoaceticus ADP1. Eur. J. Lipid Sci. Technol. 105:578-584. (Pubitemid 37363263)
    • (2003) European Journal of Lipid Science and Technology , vol.105 , Issue.10 , pp. 578-584
    • Kaischeuer, R.1    Uthoff, S.2    Luftmann, H.3    Steinbuchel, A.4
  • 57
    • 13544266225 scopus 로고    scopus 로고
    • Thio wax ester biosynthesis utilizing the unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase of Acinetobacter sp. strain ADP1
    • Uthoff S, Stöveken T, Weber N, Vosmann K, Klein E, Kalscheuer R, Steinbüchel A. 2005. Thio wax ester biosynthesis utilizing the unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase of Acinetobacter sp. strain ADP1. Appl. Environ. Microbiol. 71:790-796.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 790-796
    • Uthoff, S.1    Stöveken, T.2    Weber, N.3    Vosmann, K.4    Klein, E.5    Kalscheuer, R.6    Steinbüchel, A.7
  • 58
    • 76949095510 scopus 로고    scopus 로고
    • Biotransformation of glycidol by the unspecific wax ester synthase/acyl-CoA:diacylglycerol acyltransferase of Acinetobacter baylyi ADP1
    • Kim OB, Luftmann H, Steinbüchel A. 2009. Biotransformation of glycidol by the unspecific wax ester synthase/acyl-CoA:diacylglycerol acyltransferase of Acinetobacter baylyi ADP1. Eur. J. Lipid Sci. Technol. 111:972-978.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 972-978
    • Kim, O.B.1    Luftmann, H.2    Steinbüchel, A.3
  • 59
    • 68349111234 scopus 로고    scopus 로고
    • Both histidine residues of the conserved HHXXXDG motif are essential for wax ester synthase/acyl-CoA:diacylglycerol acyl-transferase catalysis
    • Stöveken T, Kalscheuer R, Steinbüchel A. 2009. Both histidine residues of the conserved HHXXXDG motif are essential for wax ester synthase/acyl-CoA:diacylglycerol acyl-transferase catalysis. Eur. J. Lipid Sci. Technol. 111:112-119.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 112-119
    • Stöveken, T.1    Kalscheuer, R.2    Steinbüchel, A.3
  • 60
    • 33846477310 scopus 로고    scopus 로고
    • Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA: Diacylglycerol acyltransferases
    • Wältermann M, Stöveken T, Steinbüchel A. 2007. Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: properties, function and occurrence of wax ester synthases/acyl-CoA: diacylglycerol acyltransferases. Biochimie 89:230-242.
    • (2007) Biochimie , vol.89 , pp. 230-242
    • Wältermann, M.1    Stöveken, T.2    Steinbüchel, A.3
  • 61
    • 0022855997 scopus 로고
    • Catalytic mechanism of chloramphenicol acetyltransferase investigated by site-directed mutagenesis
    • Murray IA, Lewendon A, Kleanthous C, Shaw WV. 1986. Catalytic mechanism of chloramphenicol acetyltransferase investigated by site-directed mutagenesis. Biochem. Soc. Trans. 14:1227-1228. (Pubitemid 17221103)
    • (1986) Biochemical Society Transactions , vol.14 , Issue.6 , pp. 1227-1228
    • Murray, I.A.1    Lewendon, A.2    Kleanthous, C.3    Shaw, W.V.4
  • 63
    • 34447282028 scopus 로고    scopus 로고
    • Structural and Functional Insights into a Peptide Bond-Forming Bidomain from a Nonribosomal Peptide Synthetase
    • DOI 10.1016/j.str.2007.05.008, PII S0969212607001888
    • Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO. 2007. Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase. Structure 15:781-792. (Pubitemid 47042430)
    • (2007) Structure , vol.15 , Issue.7 , pp. 781-792
    • Samel, S.A.1    Schoenafinger, G.2    Knappe, T.A.3    Marahiel, M.A.4    Essen, L.-O.5
  • 64
    • 49749152413 scopus 로고    scopus 로고
    • Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis
    • Six DA, Carty SM, Guan Z, Raetz CRH. 2008. Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis. Biochemistry 47:8623-8637.
    • (2008) Biochemistry , vol.47 , pp. 8623-8637
    • Six, D.A.1    Carty, S.M.2    Guan, Z.3    Raetz, C.R.H.4
  • 66
    • 53149087861 scopus 로고    scopus 로고
    • Acyltransferases in bacterial glycerophospholipid synthesis
    • Zhang YM, Rock CO. 2008. Acyltransferases in bacterial glycerophospholipid synthesis. J. Lipid Res. 49:1867-1874.
    • (2008) J. Lipid Res. , vol.49 , pp. 1867-1874
    • Zhang, Y.M.1    Rock, C.O.2
  • 68
    • 51249184965 scopus 로고
    • Studies on biosynthesis of waxes by developing jojoba seed. II. The demonstration of wax biosynthesis by cell-free homogenates
    • Pollard MR, McKeon T, Gupta LM, Stumpf PK. 1979. Studies on biosynthesis of waxes by developing jojoba seed. II. The demonstration of wax biosynthesis by cell-free homogenates. Lipids 14:651-662.
    • (1979) Lipids , vol.14 , pp. 651-662
    • Pollard, M.R.1    McKeon, T.2    Gupta, L.M.3    Stumpf, P.K.4
  • 69
    • 77954267973 scopus 로고    scopus 로고
    • Pilot-scale production of fatty acid ethyl esters by an engineered Escherichia coli strain harboring the p(Microdiesel) plasmid
    • Elbahloul Y, Steinbüchel A. 2010. Pilot-scale production of fatty acid ethyl esters by an engineered Escherichia coli strain harboring the p(Microdiesel) plasmid. Appl. Environ. Microbiol. 76:4560-4565.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4560-4565
    • Elbahloul, Y.1    Steinbüchel, A.2
  • 70
    • 10444228204 scopus 로고    scopus 로고
    • Synthesis of novel lipids in Saccharomyces cerevisiae by heterologous expression of an unspecific bacterial acyltransferase
    • Kalscheuer R, Luftmann H, Steinbüchel A. 2004. Synthesis of novel lipids in Saccharomyces cerevisiae by heterologous expression of an unspecific bacterial acyltransferase. Appl. Environ. Microbiol. 70:7112-7125.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 7112-7125
    • Kalscheuer, R.1    Luftmann, H.2    Steinbüchel, A.3
  • 71
    • 81455143861 scopus 로고    scopus 로고
    • Synthesis of FAEEs from glycerol in engineered Saccharomyces cerevisiae using endogenously produced ethanol by heterologous expression of an unspecific bacterial acyltransferase
    • Yu KO, Jung J, Kim SW, Park CH, Han SO. 2012. Synthesis of FAEEs from glycerol in engineered Saccharomyces cerevisiae using endogenously produced ethanol by heterologous expression of an unspecific bacterial acyltransferase. Biotechnol. Bioeng. 109:110-115.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 110-115
    • Yu, K.O.1    Jung, J.2    Kim, S.W.3    Park, C.H.4    Han, S.O.5
  • 72
    • 84857243863 scopus 로고    scopus 로고
    • Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production
    • Shi S, Valle-Rodríguez JO, Khoomrung S, Siewers V, Nielsen J. 2012. Functional expression and characterization of five wax ester synthases in Saccharomyces cerevisiae and their utility for biodiesel production. Biotechnol. Biofuels 5:7-16.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 7-16
    • Shi, S.1    Valle-Rodríguez, J.O.2    Khoomrung, S.3    Siewers, V.4    Nielsen, J.5
  • 73
    • 3242750587 scopus 로고    scopus 로고
    • Induction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture
    • DOI 10.1128/JB.186.15.5017-5030.2004
    • Daniel J, Deb C, Dubey VS, Sirakova TD, Abomoelak B, Morbidoni HR, Kolattukudy PE. 2004. Introduction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture. J. Bacteriol. 186:5017-5030. (Pubitemid 38970829)
    • (2004) Journal of Bacteriology , vol.186 , Issue.15 , pp. 5017-5030
    • Daniel, J.1    Deb, C.2    Dubey, V.S.3    Sirakova, T.D.4    Abomoelak, B.5    Morbidoni, H.R.6    Kolattukudy, P.E.7
  • 74
    • 51149089101 scopus 로고    scopus 로고
    • Cloning and characterization of a gene involved in triacylglycerol biosynthesis and identification of additional homologous genes in the oleaginous bacterium Rhodococcus opacus PD630
    • Alvarez AF, Alvarez HM, Kalscheuer R, Wältermann M, Steinbüchel A. 2008. Cloning and characterization of a gene involved in triacylglycerol biosynthesis and identification of additional homologous genes in the oleaginous bacterium Rhodococcus opacus PD630. Microbiology 154:2327-2335.
    • (2008) Microbiology , vol.154 , pp. 2327-2335
    • Alvarez, A.F.1    Alvarez, H.M.2    Kalscheuer, R.3    Wältermann, M.4    Steinbüchel, A.5
  • 76
    • 68349093972 scopus 로고    scopus 로고
    • Analysis of neutral lipid biosynthesis in Streptomyces avermitilis MA-4680 and characterization of an acyltransferase involved herein
    • Kaddor C, Biermann K, Kalscheuer R, Steinbüchel A. 2009. Analysis of neutral lipid biosynthesis in Streptomyces avermitilis MA-4680 and characterization of an acyltransferase involved herein. Appl. Microbiol. Biotechnol. 84:143-155.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 143-155
    • Kaddor, C.1    Biermann, K.2    Kalscheuer, R.3    Steinbüchel, A.4
  • 77
    • 0038784717 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis pathogenesis and molecular determinants of virulence
    • DOI 10.1128/CMR.16.3.463-496.2003
    • Smith I. 2003. Mycobacterium tuberculosis pathogenesis and molecular determinants of virulence. Clin. Microbiol. Rev. 16:463-496. (Pubitemid 36871317)
    • (2003) Clinical Microbiology Reviews , vol.16 , Issue.3 , pp. 463-496
    • Smith, I.1
  • 78
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • DOI 10.1146/annurev.micro.55.1.139
    • Wayne LG, Sohaskey CD. 2001. Nonreplicating persistence of Mycobacterium tuberculosis. Annu. Rev. Microbiol. 55:139-163. (Pubitemid 32978103)
    • (2001) Annual Review of Microbiology , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 79
    • 0036774641 scopus 로고    scopus 로고
    • Intracellular lipophilic inclusions of mycobacteria in vitro and in sputum
    • Garton NJ, Christensen H, Minnikin DE, Adegbola RA, Barer MR. 2002. Intracellular lipophilic inclusions of mycobacteria in vitro and in sputum. Microbiology 148:2951-2958. (Pubitemid 35243694)
    • (2002) Microbiology , vol.148 , Issue.10 , pp. 2951-2958
    • Garton, N.J.1    Christensen, H.2    Minnikin, D.E.3    Adegbola, R.A.4    Barer, M.R.5
  • 80
    • 0043192504 scopus 로고    scopus 로고
    • Phagosomes, fatty acids and tuberculosis
    • DOI 10.1038/ncb0903-776
    • Russell DG. 2003. Phagosomes, fatty acids and tuberculosis. Nat. Cell Biol. 5:776-778. (Pubitemid 37087163)
    • (2003) Nature Cell Biology , vol.5 , Issue.9 , pp. 776-778
    • Russell, D.G.1
  • 81
    • 33748769518 scopus 로고    scopus 로고
    • Identification of a diacylglycerol acyltransferase gene involved in accumulation of triacylglycerol in Mycobacterium tuberculosis under stress
    • DOI 10.1099/mic.0.28993-0
    • Sirakova TD, Dubey VS, Deb C, Daniel J, Korotkova TA, Abomoelak B, Kolattukudy PE. 2006. Identification of a diacylglycerol acyltransferase gene involved in accumulation of triacylglycerol in Mycobacterium tuberculosis under stress. Microbiology 152:2717-2725. (Pubitemid 44405096)
    • (2006) Microbiology , vol.152 , Issue.9 , pp. 2717-2725
    • Sirakova, T.D.1    Dubey, V.S.2    Deb, C.3    Daniel, J.4    Korotkova, T.A.5    Abomoelak, B.6    Kolattukudy, P.E.7
  • 82
    • 0033779946 scopus 로고    scopus 로고
    • Microbial degradation of the multiply branched alkane 2,6,10,15,19,23-hexamethyltetracosane (squalane) by Mycobacterium fortuitum and Mycobacterium ratisbonense
    • Berekaa MM, Steinbüchel A. 2000. Microbial degradation of the multiply branched alkane 2,6,10,15,19,23-hexamethyltetracosane (squalane) by Mycobacterium fortuitum and Mycobacterium ratisbonense. Appl. Environ. Microbiol. 66:4462-4467.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4462-4467
    • Berekaa, M.M.1    Steinbüchel, A.2
  • 83
    • 34447520453 scopus 로고    scopus 로고
    • Biodegradation of phytane (2,6,10,14-tetramethylhexadecane) and accumulation of related isoprenoid wax esters by Mycobacterium ratisbonense strain SD4 under nitrogen-starved conditions
    • DOI 10.1111/j.1574-6968.2007.00770.x
    • Silva RA, Grossi V, Alvarez HM. 2007. Biodegradation of phytane (2,6,10,14-tetramethylhexadecane) and accumulation of related isoprenoid wax esters by Mycobacterium ratisbonense strain SD4 under nitrogen-starvation conditions. FEMS Microbiol. Lett. 272:220-228. (Pubitemid 47074615)
    • (2007) FEMS Microbiology Letters , vol.272 , Issue.2 , pp. 220-228
    • Silva, R.A.1    Grossi, V.2    Alvarez, H.M.3
  • 85
    • 39749201900 scopus 로고    scopus 로고
    • Cytoplasmic wax ester accumulation during biofilm-driven substrate assimilation at the alkane-water interface by Marinobacter hydrocarbonoclasticus SP17
    • Klein B, Grossi V, Bouriat P, Goulas P, Grimaud R. 2008. Cytoplasmic wax ester accumulation during biofilm-driven substrate assimilation at the alkane-water interface by Marinobacter hydrocarbonoclasticus SP17. Res. Microbiol. 159:137-144.
    • (2008) Res. Microbiol. , vol.159 , pp. 137-144
    • Klein, B.1    Grossi, V.2    Bouriat, P.3    Goulas, P.4    Grimaud, R.5
  • 86
    • 0032960487 scopus 로고    scopus 로고
    • Production of wax esters during aerobic growth of marine bacteria on isoprenoid compounds
    • Rontani JF, Bonin P, Volkman JK. 1999. Production of wax esters during aerobic growth of marine bacteria on isoprenoid compounds. Appl. Environ. Microbiol. 65:221-230. (Pubitemid 29029642)
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.1 , pp. 221-230
    • Rontani, J.-F.1    Bonin, P.C.2    Volkman, J.K.3
  • 87
    • 0038492676 scopus 로고    scopus 로고
    • Production of a polyunsaturated isoprenoid wax ester during aerobic metabolism of squalene by Marinobacter squalenivorans sp. nov.
    • DOI 10.1128/AEM.69.7.4167-4176.2003
    • Rontani JF, Mouzdahir A, Michotey V, Caumette P, Bonin P. 2003. Production of a polyunsaturated isoprenoid wax ester during aerobic metabolism of squalene by Marinobacter squalenivorans sp. nov. Appl. Environ. Microbiol. 69:4167-4176. (Pubitemid 36870078)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.7 , pp. 4167-4176
    • Rontani, J.-F.1    Mouzdahir, A.2    Michotey, V.3    Caumette, P.4    Bonin, P.5
  • 88
    • 19544375814 scopus 로고    scopus 로고
    • Marinobacter hydrocarbonoclasticus Gauthier et al. 1992 and Marinobacter aquaeolei Nguyen et al. 1999 are heterotypic synonyms
    • Márquez MC, Ventosa A. 2005. Marinobacter hydrocarbonoclasticus Gauthier et al. 1992 and Marinobacter aquaeolei Nguyen et al. 1999 are heterotypic synonyms. Int. J. Syst. Evol. Microbiol. 55:1349-1351.
    • (2005) Int. J. Syst. Evol. Microbiol. , vol.55 , pp. 1349-1351
    • Márquez, M.C.1    Ventosa, A.2
  • 89
    • 84871904714 scopus 로고    scopus 로고
    • Identification of a residue affecting fatty alcohol selectivity in wax ester synthase
    • 19 October doi:10.1128/AEM.02523-12
    • Barney BM, Mann RL, Ohlert JM. 19 October 2012. Identification of a residue affecting fatty alcohol selectivity in wax ester synthase. Appl. Environ. Microbiol. doi:10.1128/AEM.02523-12.
    • (2012) Appl. Environ. Microbiol.
    • Barney, B.M.1    Mann, R.L.2    Ohlert, J.M.3
  • 93
    • 0036263683 scopus 로고    scopus 로고
    • Identification of phenyldecanoic acid as a constituent of triacylglycerols and wax ester produced by Rhodococcus opacus PD630
    • Alvarez HM, Luftmann H, Silva RA, Cesari AC, Viale A, Wältermann M, Steinbüchel A. 2002. Identification of phenyldecanoic acid as a constituent of triacylglycerols and wax ester produced by Rhodococcus opacus PD630. Microbiology 148:1407-1412. (Pubitemid 34567217)
    • (2002) Microbiology , vol.148 , Issue.5 , pp. 1407-1412
    • Alvarez, H.M.1    Luftmann, H.2    Silva, R.A.3    Cesari, A.C.4    Viale, A.5    Waltermann, M.6    Steinbuchel, A.7
  • 94
    • 0028349583 scopus 로고
    • Importance of stored triacylglycerols in Streptomyces: Possible carbon source for antibiotics
    • Olukoshi ER, Packter NM. 1994. Importance of stored triacylglycerols in Streptomyces: possible carbon source for antibiotics. Microbiology 140:931-943. (Pubitemid 24124667)
    • (1994) Microbiology , vol.140 , Issue.4 , pp. 931-943
    • Olukoshi, E.R.1    Packter, N.M.2
  • 96
    • 0027412424 scopus 로고
    • Triacylglycerol synthesis by an sn-1,2(2,3)-diacylglycerol transacylase from rat intestinal microsomes
    • Lehner R, Kuksis A. 1993. Triacylglycerol synthesis by an sn-1,2(2,3)-diacylglycerol transacylase from rat intestinal microsomes. J. Biol. Chem. 268:8781-8786. (Pubitemid 23118667)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.12 , pp. 8781-8786
    • Lehner, R.1    Kuksis, A.2
  • 97
    • 0030802803 scopus 로고    scopus 로고
    • Triacylglycerols are synthesised and utilized by transacylation reactions in microsomal preparations of developing safflower (Carthamus tinctorius L.) seeds
    • DOI 10.1007/s004250050165
    • Stobart K, Mancha M, Lenman M, Dahlqvist A, Stymne S. 1997. Triacylglycerols are synthesized and utilized by transacylation reactions in microsomal preparations of developing safflower (Carthamus tinctorius L.) seeds. Planta 203:58-66. (Pubitemid 27378193)
    • (1997) Planta , vol.203 , Issue.1 , pp. 58-66
    • Stobart, K.1    Mancha, M.2    Lenman, M.3    Dahlqvist, A.4    Stymne, S.5
  • 99
    • 0034612345 scopus 로고    scopus 로고
    • Phospholipid:diacylglycerol acyltransferase: An enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
    • Dahlqvist A, Ståhl U, Lenman M, Banas A, Lee M, Sandager L, Ronne H, Stymne S. 2000. Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc. Natl. Acad. Sci. U. S. A. 97:6487-6492.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6487-6492
    • Dahlqvist, A.1    Ståhl, U.2    Lenman, M.3    Banas, A.4    Lee, M.5    Sandager, L.6    Ronne, H.7    Stymne, S.8
  • 101
    • 0030175841 scopus 로고    scopus 로고
    • Biosynthesis of triacylglycerols
    • DOI 10.1016/0163-7827(96)00005-7
    • Lehner R, Kuksis A. 1996. Biosynthesis of triacylglycerols. Prog. Lipid Res. 35:169-201. (Pubitemid 26366398)
    • (1996) Progress in Lipid Research , vol.35 , Issue.2 , pp. 169-201
    • Lehner, R.1    Kuksis, A.2
  • 103
    • 0025131925 scopus 로고
    • Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity
    • Coleman J. 1990. Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. J. Biol. Chem. 265:17215-17221.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17215-17221
    • Coleman, J.1
  • 104
    • 0031941001 scopus 로고    scopus 로고
    • A conserved histidine is essential for glycerolipid acyltransferase catalysis
    • Heath RJ, Rock CO. 1998. A conserved histidine is essential for glycerolipid acyltransferase catalysis. J. Bacteriol. 180:1425-1430. (Pubitemid 28125725)
    • (1998) Journal of Bacteriology , vol.180 , Issue.6 , pp. 1425-1430
    • Heath, R.J.1    Rock, C.O.2
  • 105
    • 0033522379 scopus 로고    scopus 로고
    • Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction
    • Lewin TM, Wang P, Coleman RA. 1999. Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction. Biochemistry 38:5764-5771.
    • (1999) Biochemistry , vol.38 , pp. 5764-5771
    • Lewin, T.M.1    Wang, P.2    Coleman, R.A.3
  • 107
    • 0026548077 scopus 로고
    • Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3- phosphate acyltransferase (plsC)
    • Coleman J. 1992. Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC). Mol. Gen. Genet. 232:295-303.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 295-303
    • Coleman, J.1
  • 108
    • 0019784527 scopus 로고
    • Membrane phospholipid synthesis in Escherichia coli. Purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase
    • Green PR, Merrill AH, Bell RM Jr. 1981. Membrane phospholipid synthesis in Escherichia coli: purification, reconstitution, and characterization of sn-glycerol-3-phosphate acyltransferase. J. Biol. Chem. 256:11151-11159. (Pubitemid 12181595)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.21 , pp. 11151-11159
    • Green, P.R.1    Merrill Jr., A.H.2    Bell, R.M.3
  • 109
    • 0019431621 scopus 로고
    • Phospholipid synthesis in Escherichia coli. Characteristics of fatty acid transfer from acyl-acyl carrier protein to sn-glycerol 3-phosphate
    • Rock CO, Goelz SE, Cronan JE, Jr. 1981. Phospholipid synthesis in Escherichia coli. Characteristics of fatty acid transfer from acyl-acyl carrier protein to sn-glycerol-3-phosphate. J. Biol. Chem. 256:736-742. (Pubitemid 11151446)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.2 , pp. 736-742
    • Rock, C.O.1    Goelz, S.E.2    Cronan Jr., J.E.3
  • 110
    • 0018189560 scopus 로고
    • An estimate of the minimum amount of fluid lipid required for the growth of Escherichia coli
    • Jackson MB, Cronan, JE Jr. 1978. An estimate of the minimum amount of fluid lipid required for the growth of Escherichia coli. Biochim. Biophys. Acta 512:472-479. (Pubitemid 9019423)
    • (1978) Biochimica et Biophysica Acta , vol.512 , Issue.3 , pp. 472-479
    • Jackson, M.B.1    Cronan Jr., J.E.2
  • 112
    • 0029153622 scopus 로고
    • A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant
    • Hanke C, Wolter FP, Coleman J, Peterek G, Frentzen M. 1995. A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant. Eur. J. Biochem. 232:806-810.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 806-810
    • Hanke, C.1    Wolter, F.P.2    Coleman, J.3    Peterek, G.4    Frentzen, M.5
  • 113
    • 34249740681 scopus 로고    scopus 로고
    • Topology and active site of PlsY: The bacterial acylphosphate:glycerol-3- phosphate acyltransferase
    • DOI 10.1074/jbc.M700374200
    • Lu YJ, Zhang F, Grimes KD, Lee RE, Rock CO. 2007. Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. J. Biol. Chem. 282:11339-11346. (Pubitemid 47100780)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11339-11346
    • Lu, Y.-J.1    Zhang, F.2    Grimes, K.D.3    Lee, R.E.4    Rock, C.O.5
  • 114
    • 33747887074 scopus 로고    scopus 로고
    • Acyl-Phosphates Initiate Membrane Phospholipid Synthesis in Gram-Positive Pathogens
    • DOI 10.1016/j.molcel.2006.06.030, PII S1097276506004941
    • Lu YJ, Zhang YM, Grimes KD, Qi J, Lee RE, Rock CO. 2006. Acylphosphates initiate membrane phospholipid synthesis in Gram-negative pathogens. Mol. Cell 23:765-772. (Pubitemid 44292558)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 765-772
    • Lu, Y.-J.1    Zhang, Y.-M.2    Grimes, K.D.3    Qi, J.4    Lee, R.E.5    Rock, C.O.6
  • 115
    • 34547791319 scopus 로고    scopus 로고
    • Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis
    • DOI 10.1128/JB.00602-07
    • Paoletti L, Lu YL, Schujman GE, de Mendoza D, Rock CO. 2007. Coupling of fatty acid and phospholipid synthesis in Bacillus subtilis. J. Bacteriol. 189:5816-5824. (Pubitemid 47236134)
    • (2007) Journal of Bacteriology , vol.189 , Issue.16 , pp. 5816-5824
    • Paoletti, L.1    Lu, Y.-J.2    Schujman, G.E.3    De Mendoza, D.4    Rock, C.O.5
  • 116
  • 117
    • 0022964758 scopus 로고
    • Molecular genetics of membrane phospholipid synthesis
    • Raetz CRH. 1986. Molecular genetics of membrane phospholipid synthesis. Annu. Rev. Genet. 20:253-295.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 253-295
    • Raetz, C.R.H.1
  • 119
    • 11144290631 scopus 로고    scopus 로고
    • LPS, TLR4 and infectious disease diversity
    • DOI 10.1038/nrmicro1068
    • Miller SI, Ernst RK, Bader MW. 2005. LPS, TLR4 and infectious disease diversity. Nat. Rev. Microbiol. 3:36-46. (Pubitemid 40028467)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.1 , pp. 36-46
    • Miller, S.I.1    Ernst, R.K.2    Bader, M.W.3
  • 120
    • 2342542372 scopus 로고    scopus 로고
    • Biosynthesis, transport, and modification of lipid A
    • DOI 10.1139/o03-070
    • Trent MS. 2004. Biosynthesis, transport, and modification of lipid A. Biochem. Cell Biol. 82:71-86. (Pubitemid 38580875)
    • (2004) Biochemistry and Cell Biology , vol.82 , Issue.1 , pp. 71-86
    • Trent, M.S.1
  • 121
    • 0031910071 scopus 로고    scopus 로고
    • Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl- acyl carrier protein-dependent UDP-GlcNAc acyltransferase
    • Dotson GD, Kaltashov IA, Cotter RJ, Raetz CR. 1998. Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl-acyl carrier protein-dependent UDP-GlcNAc acyltransferase. J. Bacteriol. 180:330-337. (Pubitemid 28100298)
    • (1998) Journal of Bacteriology , vol.180 , Issue.2 , pp. 330-337
    • Dotson, G.D.1    Kaltashov, I.A.2    Cotter, R.J.3    Raetz, C.R.H.4
  • 123
    • 0025736972 scopus 로고
    • Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from Gram-negative bacteria: Relationship to lipid A structure
    • Williamson JM, Anderson MS, Raetz CR. 1991. Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from Gram-negative bacteria: relationship to lipid A structure. J. Bacteriol. 173:3591-3596.
    • (1991) J. Bacteriol. , vol.173 , pp. 3591-3596
    • Williamson, J.M.1    Anderson, M.S.2    Raetz, C.R.3
  • 125
    • 0023853819 scopus 로고
    • First committed step of lipid A biosynthesis in Escherichia coli: Sequence of lpxA gene
    • Coleman J, Raetz CR. 1988. First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene. J. Bacteriol. 170:1268-1274. (Pubitemid 18079066)
    • (1988) Journal of Bacteriology , vol.170 , Issue.3 , pp. 1268-1274
    • Coleman, J.1    Raetz, C.R.H.2
  • 126
    • 0025220127 scopus 로고
    • A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis
    • Galloway SM, Raetz CR. 1990. A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis. J. Biol. Chem. 265:6394-6402.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6394-6402
    • Galloway, S.M.1    Raetz, C.R.2
  • 127
    • 46049093975 scopus 로고    scopus 로고
    • Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis
    • DOI 10.1128/JB.00234-08
    • Bainbridge BW, Karimi-Naser L, Reife R, Blethen F, Ernst RK, Darveau RP. 2008. Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis. J. Bacteriol. 190:4549-4558. (Pubitemid 351898971)
    • (2008) Journal of Bacteriology , vol.190 , Issue.13 , pp. 4549-4558
    • Bainbridge, B.W.1    Karimi-Naser, L.2    Reife, R.3    Blethen, F.4    Ernst, R.K.5    Darveau, R.P.6
  • 128
    • 0242362183 scopus 로고    scopus 로고
    • Crystal Structure of UDP-N-Acetylglucosamine Acyltransferase from Helicobacter pylori
    • DOI 10.1002/prot.10436
    • Lee BI, Suh SW. 2003. Crystal structure of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori. Proteins 53:772-774. (Pubitemid 37352190)
    • (2003) Proteins: Structure, Function and Genetics , vol.53 , Issue.3 , pp. 772-774
    • Lee, B.I.1    Suh, S.W.2
  • 131
    • 0035378670 scopus 로고    scopus 로고
    • A Chlamydia trachomatis UDP-N-acetylglucosamine acyltransferase selective for myristoyl-acyl carrier protein. Expression in Escherichia coli and formation of hybrid lipid A species
    • Sweet CR, Lin S, Cotter RJ, Raetz CR. 2001. A Chlamydia trachomatis UDP-N-acetylglucosamine acyltransferase selective for myristoyl-acyl carrier protein. Expression in Escherichia coli and formation of hybrid lipid A species. J. Biol. Chem. 276:19565-19574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19565-19574
    • Sweet, C.R.1    Lin, S.2    Cotter, R.J.3    Raetz, C.R.4
  • 132
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz CRH, Roderick SL. 1995. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270:997-1000.
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 133
    • 0027121143 scopus 로고
    • Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme
    • Vaara M. 1992. Eight bacterial proteins, including UDP-N- acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme. FEMS Microbiol. Lett. 97:249-254.
    • (1992) FEMS Microbiol. Lett. , vol.97 , pp. 249-254
    • Vaara, M.1
  • 134
    • 0033578887 scopus 로고    scopus 로고
    • The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis
    • Wyckoff TJO, Raetz CRH. 1999. The active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis. J. Biol. Chem. 274:27047-27055.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27047-27055
    • Wyckoff, T.J.O.1    Raetz, C.R.H.2
  • 135
    • 67650022094 scopus 로고    scopus 로고
    • Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA
    • Robins LI, Williams AH, Raetz CRH. 2009. Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA. Biochemistry 48:6191-6201.
    • (2009) Biochemistry , vol.48 , pp. 6191-6201
    • Robins, L.I.1    Williams, A.H.2    Raetz, C.R.H.3
  • 136
    • 79960981349 scopus 로고    scopus 로고
    • Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that of Escherichia coli
    • Li C, Guan Z, Liu D, Raetz CRH. 2011. Pathway for lipid A biosynthesis in Arabidopsis thaliana resembling that of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 108:11387-11392.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 11387-11392
    • Li, C.1    Guan, Z.2    Liu, D.3    Raetz, C.R.H.4
  • 137
    • 84861629566 scopus 로고    scopus 로고
    • Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase
    • Joo SH, Chung HS, Raetz CRH, Garrett TA. 2012. Activity and crystal structure of Arabidopsis thaliana UDP-N-acetylglucosamine acyltransferase. Biochemistry 51:4322-4330.
    • (2012) Biochemistry , vol.51 , pp. 4322-4330
    • Joo, S.H.1    Chung, H.S.2    Raetz, C.R.H.3    Garrett, T.A.4
  • 138
    • 0027275541 scopus 로고
    • The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)- glucosamine N-acyltransferase. The third step of endotoxin biosynthesis
    • Kelly TM, Stachula SA, Raetz CRH, Anderson MS. 1993. The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis. J. Biol. Chem. 268:19866-19874. (Pubitemid 23270782)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19866-19874
    • Kelly, T.M.1    Stachula, S.A.2    Raetz, C.R.H.3    Anderson, M.S.4
  • 141
    • 70249134273 scopus 로고    scopus 로고
    • Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis
    • Bartling CM, Raetz CRH. 2009. Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 15:8672-8683.
    • (2009) Biochemistry , vol.15 , pp. 8672-8683
    • Bartling, C.M.1    Raetz, C.R.H.2
  • 142
    • 43249099873 scopus 로고    scopus 로고
    • Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis
    • DOI 10.1021/bi800240r
    • Bartling CM, Raetz CRH. 2008. Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis. Biochemistry 47:5290-5302. (Pubitemid 351656973)
    • (2008) Biochemistry , vol.47 , Issue.19 , pp. 5290-5302
    • Bartling, C.M.1    Raetz, C.R.H.2
  • 143
    • 0029974220 scopus 로고    scopus 로고
    • Function of the htrB high temperature requirement gene of Escherchia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate
    • Clementz T, Bednarski JJ, Raetz CRH. 1996. Function of the htrB high temperature requirement gene of Escherchia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate. J. Biol. Chem. 271:12095-12102.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12095-12102
    • Clementz, T.1    Bednarski, J.J.2    Raetz, C.R.H.3
  • 144
    • 0030888162 scopus 로고    scopus 로고
    • Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A
    • Clementz T, Zhou Z, Raetz CRH. 1997. Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. J. Biol. Chem. 272:13353-13360.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13353-13360
    • Clementz, T.1    Zhou, Z.2    Raetz, C.R.H.3
  • 145
    • 0033515574 scopus 로고    scopus 로고
    • Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction at 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein
    • Carty SM, Sreekumar KR, Raetz CRH. 1999. Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction at 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein. J. Biol. Chem. 274:9677-9685.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9677-9685
    • Carty, S.M.1    Sreekumar, K.R.2    Raetz, C.R.H.3
  • 146
    • 0037134515 scopus 로고    scopus 로고
    • A triple mutant of Escherichia coli lacking secondary acyl chains on lipid A
    • DOI 10.1074/jbc.M200409200
    • Vorachek-Warren MK, Ramirez S, Cotter RJ, Raetz CRH. 2002. A triple mutant of Escherichia coli lacking secondary acyl chains on lipid A. J. Biol. Chem. 277:14194-14205. (Pubitemid 34968032)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 14194-14205
    • Vorachek-Warren, M.K.1    Ramirez, S.2    Cotter, R.J.3    Raetz, C.R.H.4
  • 147
    • 0024997060 scopus 로고
    • Biosynthesis of lipid A in Escherichia coli. Acyl carrier protein-dependent incorporation of laurate and myristate
    • Brozek KA, Raetz CRH. 1990. Biosynthesis of lipid A in Escherichia coli. Acyl carrier protein-dependent incorporation of laurate and myristate. J. Biol. Chem. 265:15410-15417.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15410-15417
    • Brozek, K.A.1    Raetz, C.R.H.2
  • 148
    • 0023904302 scopus 로고
    • Lipid A precursor from Pseudomonas aeruginosa is completely acylated prior to addition of 3-deoxy-D-manno-octulosonate
    • Goldman RC, Doran CC, Kadam SK, Capobianco JO. 1988. Lipid A precursor from Pseudomonas aeruginosa is completely acylated prior to addition of 3-deoxy-D-manno-octulosonate. J. Biol. Chem. 263:5217-5223.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5217-5223
    • Goldman, R.C.1    Doran, C.C.2    Kadam, S.K.3    Capobianco, J.O.4
  • 149
    • 0028117726 scopus 로고
    • Endotoxin biosynthesis in Pseudomonas aeruginosa: Enzymatic incorporation of laurate before 3-deoxy-D-manno-octulosonate
    • Mohan S, Raetz CRH. 1994. Endotoxin biosynthesis in Pseudomonas aeruginosa: enzymatic incorporation of laurate before 3-deoxy-D-manno- octulosonate. J. Bacteriol. 176:6944-6951. (Pubitemid 24349434)
    • (1994) Journal of Bacteriology , vol.176 , Issue.22 , pp. 6944-6951
    • Mohan, S.1    Raetz, C.R.H.2
  • 150
    • 0036224087 scopus 로고    scopus 로고
    • Endotoxin of Neisseria meningitidis composed only of intact lipid A: Inactivation of the meningococcal 3-deoxy-D-manno-octulosonic acid transferase
    • DOI 10.1128/JB.184.9.2379-2388.2002
    • Tzeng YL, Datta A, Kolli VK, Carlson RW, Stephens DS. 2002. Endotoxin of Neisseria meningitidis composed only of intact lipid A: inactivation of the meningococcal 3-deoxy-D-manno-octulosonic acid transferase. J. Bacteriol. 184:2379-2388. (Pubitemid 34311129)
    • (2002) Journal of Bacteriology , vol.184 , Issue.9 , pp. 2379-2388
    • Tzeng, Y.-L.1    Datta, A.2    Kumar, K.V.3    Carlson, R.W.4    Stephens, D.S.5
  • 151
    • 0034596969 scopus 로고    scopus 로고
    • Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria
    • Bishop RE, Gibbons HS, Guina T, Trent MS, Miller SI, Raetz CRH. 2000. Transfer of palmitate from phospholipids to lipid A in outer membranes of Gram-negative bacteria. EMBO J. 19:5071-5080.
    • (2000) EMBO J. , vol.19 , pp. 5071-5080
    • Bishop, R.E.1    Gibbons, H.S.2    Guina, T.3    Trent, M.S.4    Miller, S.I.5    Raetz, C.R.H.6
  • 152
    • 0023654461 scopus 로고
    • Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X
    • Brozek KA, Bulawa CE, Raetz CRH. 1987. Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X. J. Biol. Chem. 262:5170-5179.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5170-5179
    • Brozek, K.A.1    Bulawa, C.E.2    Raetz, C.R.H.3
  • 154
    • 0035846935 scopus 로고    scopus 로고
    • 2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli. A novel membrane enzyme dependent upon phosphatidylethanolamine
    • DOI 10.1074/jbc.M009019200
    • Kanipes MI, Lin S, Cotter RJ, Raetz CR. 2001. Ca2+-induced phosphoethanolamine transfer to the outer 3-deoxy-D-manno-octulosonic acid moiety of Escherichia coli lipopolysaccharide. A novel membrane enzyme dependent upon phosphatidylethanolamine. J. Biol. Chem. 12:1156-1163. (Pubitemid 32096542)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 1156-1163
    • Kanipes, M.I.1    Lin, S.2    Cotter, R.J.3    Raetz, C.R.H.4
  • 156
    • 33745670602 scopus 로고    scopus 로고
    • Topology of an outer-membrane enzyme: Measuring oxygen and water contacts in solution NMR studies of PagP
    • DOI 10.1021/ja0610075
    • Evanics F, Hwang PM, Cheng Y, Kay LE, Prosser RS. 2006. Topology of an outer-membrane enzyme: measuring oxygen and water contacts in solution NMR studies of PagP. J. Am. Chem. Soc. 128:8256-8264. (Pubitemid 43967770)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.25 , pp. 8256-8264
    • Evanics, F.1    Hwang, P.M.2    Cheng, Y.3    Kay, L.E.4    Prosser, R.S.5
  • 158
    • 23744436588 scopus 로고    scopus 로고
    • The lipid A palmitoyltransferase PagP: Molecular mechanisms and role in bacterial pathogenesis
    • DOI 10.1111/j.1365-2958.2005.04711.x
    • Bishop RE. 2005. The lipid A palmitoyltransferase PagP: molecular mechanisms and role in bacterial pathogenesis. Mol. Microbiol. 57:900-912. (Pubitemid 41139855)
    • (2005) Molecular Microbiology , vol.57 , Issue.4 , pp. 900-912
    • Bishop, R.E.1
  • 159
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • DOI 10.1039/a909079g
    • Staunton J, Weissman KJ. 2001. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18:380-416. (Pubitemid 32773840)
    • (2001) Natural Product Reports , vol.18 , Issue.4 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 160
    • 64049113564 scopus 로고    scopus 로고
    • Polyketide versatility in the biosynthesis of complex mycobacterial cell wall lipids
    • Chopra T, Gokhale RS. 2009. Polyketide versatility in the biosynthesis of complex mycobacterial cell wall lipids. Methods Enzymol. 459:259-294.
    • (2009) Methods Enzymol. , vol.459 , pp. 259-294
    • Chopra, T.1    Gokhale, R.S.2
  • 162
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • Daffé M, Draper P. 1998. The envelope layers of mycobacteria with reference to their pathogenicity. Adv. Microb. Physiol. 39:131-203.
    • (1998) Adv. Microb. Physiol. , vol.39 , pp. 131-203
    • Daffé, M.1    Draper, P.2
  • 166
    • 26444488572 scopus 로고    scopus 로고
    • The dimycocerosate ester polyketide virulence factors of mycobacteria
    • DOI 10.1016/j.plipres.2005.07.001, PII S0163782705000299
    • Onwueme KC, Vos CJ, Zurita J, Ferreras JA, Quadri LEN. 2005. The dimycocerosate ester polyketide virulence factors of mycobacteria. Prog. Lipid Res. 44:259-302. (Pubitemid 41429297)
    • (2005) Progress in Lipid Research , vol.44 , Issue.5 , pp. 259-302
    • Onwueme, K.C.1    Vos, C.J.2    Zurita, J.3    Ferreras, J.A.4    Quadri, L.E.N.5
  • 168
    • 21044443591 scopus 로고    scopus 로고
    • A homologue of the Mycobacterium tuberculosis PapA5 protein, Rif-Orf20, is an acetyltransferase involved in the biosynthesis of antitubercular drug rifamycin B by Amycolatopsis mediterranei S699
    • DOI 10.1002/cbic.200400387
    • Xiong Y, Wu X, Mahmud T. 2005. A homologoue of the Mycobacterium tuberculosis PapA5 protein, Rif-Orf20, is an acetyltransferase involved in the biosynthesis of antitubercular drug rifamycin B by Amycolatopsis mediterranei S699. Chembiochem. 6:834-837. (Pubitemid 40873743)
    • (2005) ChemBioChem , vol.6 , Issue.5 , pp. 834-837
    • Xiong, Y.1    Wu, X.2    Mahmud, T.3
  • 169
    • 3142776340 scopus 로고    scopus 로고
    • Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis
    • DOI 10.1074/jbc.M404011200
    • Buglino J, Onwueme KC, Ferreras JA, Quadri LE, Lima CD. 2004. Crystal structure of PapA5, a phthiocerol dimycocerosyl transferase from Mycobacterium tuberculosis. J. Biol. Chem. 279:30634-30642. (Pubitemid 38937995)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30634-30642
    • Buglino, J.1    Onwueme, K.C.2    Ferreras, J.A.3    Quadri, L.E.N.4    Lima, C.D.5
  • 170
    • 0037428082 scopus 로고    scopus 로고
    • Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport
    • DOI 10.1016/S0092-8674(02)01228-X
    • Jogl G, Tong L. 2003. Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. Cell 112:113-122. (Pubitemid 36106423)
    • (2003) Cell , vol.112 , Issue.1 , pp. 113-122
    • Jogl, G.1    Tong, L.2
  • 171
    • 0036295033 scopus 로고    scopus 로고
    • The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains
    • DOI 10.1038/nsb810
    • Keating TA, Marshall CG, Walsh CT, Keating AE. 2002. The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains. Nat. Struct. Biol. 9:522-526. (Pubitemid 34693807)
    • (2002) Nature Structural Biology , vol.9 , Issue.7 , pp. 522-526
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3    Keating, A.E.4
  • 172
    • 71749107774 scopus 로고    scopus 로고
    • Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis
    • Gupta M, Sajid A, Arora G, Tandon V, Singh Y. 2009. Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5, from substrates of serine/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis. J. Biol. Chem. 284:34723-34734.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34723-34734
    • Gupta, M.1    Sajid, A.2    Arora, G.3    Tandon, V.4    Singh, Y.5
  • 173
    • 33847218318 scopus 로고    scopus 로고
    • Two polyketide-synthase-associated acyltransferase are required for sulfolipid biosynthesis in Mycobacterium tuberculosis
    • Bhatt K, Gurcha SS, Bhatt A, Besra GS, Jacobs WR Jr. 2007. Two polyketide-synthase-associated acyltransferase are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153:513-520.
    • (2007) Microbiology , vol.153 , pp. 513-520
    • Bhatt, K.1    Gurcha, S.S.2    Bhatt, A.3    Besra, G.S.4    Jacobs Jr., W.R.5
  • 174
    • 68949090331 scopus 로고    scopus 로고
    • Mycobacterium marinum lipooligosaccharides are unique caryophyllose-containing cell wall glycolipids that inhibit tumor necrosis factor-alpha secretion in macrophages
    • Rombouts Y, Burguière A, Maes E, Coddeville B, Elass E, Guérardel Y, Kremer L. 2009. Mycobacterium marinum lipooligosaccharides are unique caryophyllose-containing cell wall glycolipids that inhibit tumor necrosis factor-alpha secretion in macrophages. J. Biol. Chem. 284:20975-20988.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20975-20988
    • Rombouts, Y.1    Burguière, A.2    Maes, E.3    Coddeville, B.4    Elass, E.5    Guérardel, Y.6    Kremer, L.7
  • 176
    • 14844356959 scopus 로고    scopus 로고
    • Rifamycin - Mode of action, resistance, and biosynthesis
    • DOI 10.1021/cr030112j
    • Floss HG, Yu TW. 2005. Rifamycin - mode of action, resistance, and biosynthesis. Chem. Rev. 105:621-632. (Pubitemid 40351636)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 621-632
    • Floss, H.G.1    Yu, T.-W.2
  • 178
    • 0031028172 scopus 로고    scopus 로고
    • O-Acetyltransferases for chloramphenicol and other natural products
    • Murray IA, Shaw WV. 1997. O-Acetyltransferases for chloramphenicol and other natural products. Antimicrob. Agents Chemother. 41:1-6. (Pubitemid 26428123)
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , Issue.1 , pp. 1-6
    • Murray, I.A.1    Shaw, W.V.2
  • 179
    • 6344291118 scopus 로고    scopus 로고
    • Molecular basis of bacterial resistance to chloramphenicol and florfenicol
    • DOI 10.1016/j.femsre.2004.04.001, PII S0168644504000336
    • Schwarz S, Kehrenberg C, Doublet B, Cloeckaert A. 2004. Molecular basis of bacterial resistance to chloramphenicol and florfenicol. FEMS Microbiol. Rev. 28:519-542. (Pubitemid 39469918)
    • (2004) FEMS Microbiology Reviews , vol.28 , Issue.5 , pp. 519-542
    • Schwarz, S.1    Kehrenberg, C.2    Doublet, B.3    Cloeckaert, A.4
  • 180
    • 0022373491 scopus 로고
    • 3-(Bromoacetyl)chloramphenicol, an active site directed inhibitor for chloramphenicol acetyltransferase
    • DOI 10.1021/bi00341a006
    • Kleanthous C, Cullis PM, Shaw WV. 1985. 3-(Bromoacetyl)chloramphenicol, an active site-directed inhibitor for chloramphenicol acetyltransferase. Biochemistry 24:5307-5313. (Pubitemid 16228804)
    • (1985) Biochemistry , vol.24 , Issue.20 , pp. 5307-5313
    • Kleanthous, C.1    Cullis, P.M.2    Shaw, W.V.3
  • 181
    • 0028300363 scopus 로고
    • Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: Evidence for a general base role for glutamate
    • Lewendon A, Murray IA, Shaw WV. 1994. Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate. Biochemistry 33:1944-1950. (Pubitemid 24089727)
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1944-1950
    • Lewendon, A.1    Murray, I.A.2    Shaw, W.V.3    Gibbs, M.R.4    Leslie, A.G.W.5
  • 182
    • 0021741915 scopus 로고
    • Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanism
    • Kleanthous C, Shaw WV. 1984. Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanism. Biochem. J. 223:211-220. (Pubitemid 15220363)
    • (1984) Biochemical Journal , vol.223 , Issue.1 , pp. 211-220
    • Kleanthous, C.1    Shaw, W.V.2
  • 183
    • 0024293240 scopus 로고
    • Substitutions in the active-site of chloramphenicol acetyltransferase- role of a conserved aspartate
    • Lewendon A, Murray IA, Klenthous C, CuIlis PM, Shaw WV. 1988. Substitutions in the active-site of chloramphenicol acetyltransferase-role of a conserved aspartate. Biochemistry 27:7385-7390.
    • (1988) Biochemistry , vol.27 , pp. 7385-7390
    • Lewendon, A.1    Murray, I.A.2    Klenthous, C.3    CuIlis, P.M.4    Shaw, W.V.5
  • 185
    • 0026657670 scopus 로고
    • Acetyl coenzyme A binding by chloramphenicol acetyltransferase
    • Day PJ, Shaw WV. 1992. Acetyl coenzyme A binding by chloramphenicol acetyltransferase. J. Biol. Chem. 267:5122-5127.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5122-5127
    • Day, P.J.1    Shaw, W.V.2
  • 186
    • 0025335792 scopus 로고
    • Refined crystal structure of Type III chloramphenicol acetyltransferase at 1.75 Å resolution
    • DOI 10.1016/S0022-2836(05)80129-9
    • Leslie AGW. 1990. Refined structure of type III chloramphenicol acetyltransferase at 1.75 Å resolution. J. Mol. Biol. 213:167-186. (Pubitemid 20171105)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.1 , pp. 167-186
    • Leslie, A.G.W.1
  • 187
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann U, Wu S, Flaherty KM, McKay DB. 1993. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12:3357-3364. (Pubitemid 23256422)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 188
    • 0034467679 scopus 로고    scopus 로고
    • RTX toxin structure and function: A story of numerous anomalies and few analogies in toxin biology
    • Welch RA. 2001. RTX toxin structure and function: a story of numerous anomalies and few analogies in toxin biology. Curr. Top. Microbiol. Immunol. 257:85-111. (Pubitemid 32230026)
    • (2000) Current Topics in Microbiology and Immunology , vol.257 , pp. 85-111
    • Welch, R.A.1
  • 189
    • 0027219645 scopus 로고
    • Repeat sequences in the Bordetella pertussis adenylate cyclase toxin can be recognized as alternative carboxyproximal secretion signals by the Escherichia coli α-haemolysin translocator
    • Šebo P, Ladant D. 1993. Repeat sequences in the Bordetella pertussis adenylate cyclase toxin can be recognized as alternative carboxyproximal secretion signals by the Escherichia coli α-haemolysin translocator. Mol. Microbiol. 9:999-1009.
    • (1993) Mol. Microbiol. , vol.9 , pp. 999-1009
    • Šebo, P.1    Ladant, D.2
  • 190
    • 0026009429 scopus 로고
    • Mutational analysis supports a role for multiple structural features in the C-terminal secretion signal of Escherichia coli haemolysin
    • Stanley P, Koronakis V, Hughes C. 1991. Mutational analysis supports a role for multiple structural features in the C terminal secretion signal of Escherichia coli haemolysin. Mol. Microbiol. 5:2391-2403. (Pubitemid 21895970)
    • (1991) Molecular Microbiology , vol.5 , Issue.10 , pp. 2391-2403
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 192
    • 0020415823 scopus 로고
    • Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli
    • Goebel W, Hedgepeth J. 1982. Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli. J. Bacteriol. 151:1290-1298. (Pubitemid 13243094)
    • (1982) Journal of Bacteriology , vol.151 , Issue.3 , pp. 1290-1298
    • Goebel, W.1    Hedgpeth, J.2
  • 193
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel JP, Koronakis V, Hughes C. 1991. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351:759-761. (Pubitemid 21896685)
    • (1991) Nature , vol.351 , Issue.6329 , pp. 759-761
    • Issartel, J.-P.1    Koronakis, V.2    Hughes, C.3
  • 194
    • 0028937570 scopus 로고
    • Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli O157:H7 strain EDL 933
    • Schmidt H, Beutin L, Karch H. 1995. Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli O157:H7 strain EDL 933. Infect. Immun. 63:1055-1061.
    • (1995) Infect. Immun. , vol.63 , pp. 1055-1061
    • Schmidt, H.1    Beutin, L.2    Karch, H.3
  • 195
    • 0023674373 scopus 로고
    • The calmodulin-sensitive adenylate cyclase of Bordetella pertussis: Cloning and expression in Escherichia coli
    • Glaser P, Ladant D, Sezer O, Pichot F, Ullmann A, Danchin A. 1988. The calmodulin-sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia coli. Mol. Microbiol. 2:19-30.
    • (1988) Mol. Microbiol. , vol.2 , pp. 19-30
    • Glaser, P.1    Ladant, D.2    Sezer, O.3    Pichot, F.4    Ullmann, A.5    Danchin, A.6
  • 196
    • 0035808430 scopus 로고    scopus 로고
    • Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC
    • DOI 10.1074/jbc.M006463200
    • Basar T, Havlicek V, Bezouskova S, Hackett M, Šebo P. 2001. Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC. J. Biol. Chem. 276:348-354. (Pubitemid 32050326)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 348-354
    • Basar, T.1    Havlicek, V.2    Bezouskova, S.3    Hackett, M.4    Sebo, P.5
  • 197
    • 0023231033 scopus 로고
    • Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica A1
    • Lo RY, Strathdee CA, Shewen PE. 1987. Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica A1. Infect. Immun. 55:1987-1996. (Pubitemid 17139272)
    • (1987) Infection and Immunity , vol.55 , Issue.9 , pp. 1987-1996
    • Lo, R.Y.C.1    Strathdee, C.A.2    Shewen, P.E.3
  • 198
    • 0033981139 scopus 로고    scopus 로고
    • Characterization of PaxA and its operon: A cohemolytic RTX toxin determinant from pathogenic Pasteurella aerogenes
    • Kuhnert P, Heyberger-Meyer B, Nicolet J, Frey J. 2000. Characterization of PaxA and its operon: a cohemolytic RTX toxin determinant from pathogenic Pasteurella aerogenes. Infect. Immun. 68:6-12. (Pubitemid 30016670)
    • (2000) Infection and Immunity , vol.68 , Issue.1 , pp. 6-12
    • Kuhnert, P.1    Heyberger-Meyer, B.2    Nicolet, J.3    Frey, J.4
  • 199
    • 0023269886 scopus 로고
    • Identification of two different hemolysin determinants in uropathogenic Proteus isolates
    • Welch RA. 1987. Identification of two different hemolysin determinants in uropathogenic Proteus isolates. Infect. Immun. 55:2183-2190. (Pubitemid 17139301)
    • (1987) Infection and Immunity , vol.55 , Issue.9 , pp. 2183-2190
    • Welch, R.A.1
  • 200
    • 0023238044 scopus 로고
    • The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the alpha-hemolysin of Escherichia coli
    • Koronakis V, Cross M, Senior B, Koronakis E, Hughes C. 1987. The secreted hemolysins of Proteus mirabilis, Proteus vulgaris, and Morganella morganii are genetically related to each other and to the α-hemolysin of Escherichia coli. J. Bacteriol. 169:1509-1515. (Pubitemid 17063477)
    • (1987) Journal of Bacteriology , vol.169 , Issue.4 , pp. 1509-1515
    • Koronakis, V.1    Cross, M.2    Senior, B.3
  • 202
    • 67449108344 scopus 로고    scopus 로고
    • Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin activity and initial interaction between toxin and host cells
    • Balashova NV, Shah C, Patel JK, Megalla S, Kachlany SC. 2009. Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin activity and initial interaction between toxin and host cells. Gene 443:42-47.
    • (2009) Gene , vol.443 , pp. 42-47
    • Balashova, N.V.1    Shah, C.2    Patel, J.K.3    Megalla, S.4    Kachlany, S.C.5
  • 203
    • 0025895554 scopus 로고
    • Nucleotide sequence of the hemolysin I gene from Actinobacillus pleuropneumoniae
    • Frey J, Meier R, Gygi D, Nicolet J. 1991. Nucleotide sequence of the hemolysin I gene from Actinobacillus pleuropneumoniae. Infect. Immun. 59:3026-3032.
    • (1991) Infect. Immun. , vol.59 , pp. 3026-3032
    • Frey, J.1    Meier, R.2    Gygi, D.3    Nicolet, J.4
  • 204
    • 34547447131 scopus 로고    scopus 로고
    • Construction and immunogencity of a ΔapxIC/ΔapxIIC double mutant of Actinobacillus pleuropneumoniae serovar 1
    • DOI 10.1111/j.1574-6968.2007.00813.x
    • Lin L, Bei W, Sha Y, Liu J, Guo Y, Liu W, Tu S, He Q, Chen H. 2007. Construction and immunogenicity of a ΔapxIC/ΔapxIIC double mutant of Actinobacillus pleuropneumoniae serovar 1. FEMS Microbiol. Lett. 274:55-62. (Pubitemid 47174307)
    • (2007) FEMS Microbiology Letters , vol.274 , Issue.1 , pp. 55-62
    • Lin, L.1    Bei, W.2    Sha, Y.3    Liu, J.4    Guo, Y.5    Liu, W.6    Tu, S.7    He, Q.8    Chen, H.9
  • 205
    • 0024452136 scopus 로고
    • Cloning and characterization of a hemolysin gene from Actinobacillus (Haemophilus) pleuropneumoniae
    • Chang YF, Young R, Struck DK. 1989. Cloning and characterization of a hemolysin gene from Actinobacillus (Haemophilus) pleuropneumoniae. DNA 8:635-647. (Pubitemid 19286622)
    • (1989) DNA , vol.8 , Issue.9 , pp. 635-647
    • Chang, Y.-F.1    Young, R.2    Struck, D.K.3
  • 206
    • 0027479031 scopus 로고
    • Cloning and characterization of the Actinobacillus pleuropneumoniae-RTX- toxin III (ApxIII) gene
    • Jansen R, Briaire J, Kamp EM, Gielkens AL, Smits MA. 1993. Cloning and characterization of the Actinobacillus pleuropneumoniae-RTX-toxin III (ApxIII) gene. Infect. Immun. 61:947-954. (Pubitemid 23059653)
    • (1993) Infection and Immunity , vol.61 , Issue.3 , pp. 947-954
    • Jansen, R.1    Briaire, J.2    Kamp, E.M.3    Gielkens, A.L.J.4    Smits, M.A.5
  • 207
    • 0037142203 scopus 로고    scopus 로고
    • Characterization of Aqx and its operon: The hemolytic RTX determinant of Actinobacillus equuli
    • DOI 10.1016/S0378-1135(02)00048-2, PII S0378113502000482
    • Berthoud H, Frey J, Kuhnert P. 2002. Characterization of Aqx and its operon: the hemolytic RTX determinant of Actinobacillus equuli. Vet. Microbiol. 87:159-174. (Pubitemid 34603390)
    • (2002) Veterinary Microbiology , vol.87 , Issue.2 , pp. 159-174
    • Berthoud, H.1    Frey, J.2    Kuhnert, P.3
  • 208
    • 0037472042 scopus 로고    scopus 로고
    • An RTX operon in hemolytic Moraxella bovis is absent from nonhemolytic strains
    • DOI 10.1016/S0378-1135(02)00410-8, PII S0378113502004108
    • Angelos JA, Hess JF, George LW. 2003. An RTX operon in hemolytic Moraxella bovis is absent from nonhemolytic strains. Vet. Microbiol. 92:363-377. (Pubitemid 36120597)
    • (2003) Veterinary Microbiology , vol.92 , Issue.4 , pp. 363-377
    • Angelos, J.A.1    Hess, J.F.2    George, L.W.3
  • 209
    • 34250343430 scopus 로고    scopus 로고
    • Segments crucial for membrane translocation and pore-forming activity of Bordetella adenylate cyclase toxin
    • DOI 10.1074/jbc.M611226200
    • Basler M, Knapp O, Masin J, Fiser R, Maier E, Benz R, Šebo P, Osicka R. 2007. Segments crucial for membrane translocation and poreforming activity of Bordetella adenylate cyclase toxin. J. Biol. Chem. 282:12419-12429. (Pubitemid 47100613)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12419-12429
    • Basler, M.1    Knapp, O.2    Masin, J.3    Fiser, R.4    Maier, E.5    Benz, R.6    Sebo, P.7    Osicka, R.8
  • 210
    • 0028020244 scopus 로고
    • Adenylate cyclase toxin (CyaA) of Bordetella pertussis. Evidence for the formation of small ion-permeable channels and comparison with HlyA of Escherichia coli
    • Benz R, Maier E, Ladant D, Ullmann A, Šebo P. 1994. Adenylate cyclase toxin (CyaA) of Bordetella pertussis. Evidence for the formation of small ion-permeable channels and comparison with HlyA of Escherichia coli. J. Biol. Chem. 269:27231-27239.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27231-27239
    • Benz, R.1    Maier, E.2    Ladant, D.3    Ullmann, A.4    Šebo, P.5
  • 211
    • 0025081152 scopus 로고
    • Deletion analysis resolves cell-binding and lytic domains of the Pasteurella leukotoxin
    • Cruz WT, Young R, Chang YF, Struck DK. 1990. Deletion analysis resolves cell-binding and lytic domains of the Pasteurella leukotoxin. Mol. Microbiol. 4:1933-1939.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1933-1939
    • Cruz, W.T.1    Young, R.2    Chang, Y.F.3    Struck, D.K.4
  • 212
    • 0030008163 scopus 로고    scopus 로고
    • Permeability increase induced by Escherichia coli hemolysin a in human macrophages is due to the formation of ionic pores: A patch clamp characterization
    • DOI 10.1007/s002329900012
    • Menestrina G, Pederzolli C, Dalla Serra M, Bregante M, Gambale F. 1996. Permeability increase induced by Escherichia coli hemolysin A in human macrophages is due to the formation of ionic pores: a patch clamp characterization. J. Membr. Biol. 149:113-121. (Pubitemid 26076097)
    • (1996) Journal of Membrane Biology , vol.149 , Issue.2 , pp. 113-121
    • Menestrina, G.1    Pederzolli, C.2    Dalla, S.M.3    Bregante, M.4    Gambale, F.5
  • 213
    • 0342445437 scopus 로고    scopus 로고
    • An amphipathic alpha-helix including glutamates 509 and 516 is crucial for membrane translocation of adenylate cyclase toxin and modulates formation and cation selectivity of its membrane channels
    • Osickova A, Osicka R, Maier E, Benz R, Šebo P. 1999. An amphipathic alpha-helix including glutamates 509 and 516 is crucial for membrane translocation of adenylate cyclase toxin and modulates formation and cation selectivity of its membrane channels. J. Biol. Chem. 274:37644-37650. (Pubitemid 30026821)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 37644-37650
    • Osickova, A.1    Osicka, R.2    Maier, E.3    Benz, R.4    Sebo, P.5
  • 215
    • 0025879152 scopus 로고
    • High-level synthesis of active adenylate cyclase toxin of Bordetella pertussis in a reconstructed Escherichia coli system
    • Šebo P, Glaser P, Sakamoto H, Ullmann A. 1991. High-level synthesis of active adenylate cyclase toxin of Bordetella pertussis in a reconstructed Escherichia coli system. Gene 104:19-24.
    • (1991) Gene , vol.104 , pp. 19-24
    • Šebo, P.1    Glaser, P.2    Sakamoto, H.3    Ullmann, A.4
  • 216
    • 0031033823 scopus 로고    scopus 로고
    • Structure-function studies of the adenylate cyclase toxin of Bordetella pertussis and the leukotoxin of Pasteurella haemolytica by heterologous C protein activation and construction of hybrid proteins
    • Westrop G, Hormozi K, da Costa N, Parton R, Coote J. 1997. Structure-function studies of the adenylate cyclase toxin of Bordetella pertussis and the leukotoxin of Pasteurella haemolytica by heterologous C protein activation and construction of hybrid proteins. J. Bacteriol. 179:871-879. (Pubitemid 27051845)
    • (1997) Journal of Bacteriology , vol.179 , Issue.3 , pp. 871-879
    • Westrop, G.1    Hormozi, K.2    Da, C.N.3    Parton, R.4    Coote, J.5
  • 218
    • 0028567924 scopus 로고
    • Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
    • Stanley P, Packman LC, Koronakis V, Hughes C. 1994. Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. Science 266:1992-1996.
    • (1994) Science , vol.266 , pp. 1992-1996
    • Stanley, P.1    Packman, L.C.2    Koronakis, V.3    Hughes, C.4
  • 219
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coil hemolysin: A unique protein lipidation mechanism underlying toxin function
    • Stanley P, Koronakis V, Hughes C. 1998. Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function. Microbiol. Mol. Biol. Rev. 62:309-333. (Pubitemid 28270277)
    • (1998) Microbiology and Molecular Biology Reviews , vol.62 , Issue.2 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 220
    • 0035856528 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of HlyC, the internal protein acyltransferase that activates Escherichia coli hemolysin toxin
    • DOI 10.1021/bi011032h
    • Worsham LMS, Trent MS, Earls L, Jolly C, Ernst-Fonberg ML. 2001. Insights into the catalytic mechanism of HlyC, the internal protein acyltransferases that activates Escherichia coli hemolysin toxin. Biochemistry 40:13607-13616. (Pubitemid 33130788)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13607-13616
    • Worsham, L.M.S.1    Trent, M.S.2    Earls, L.3    Jolly, C.4    Ernst-Fonberg, M.L.5
  • 221
    • 0033428684 scopus 로고    scopus 로고
    • An ordered reaction mechanism for bacterial toxin acylation by the specialized acyltransferase HlyC: Formation of a ternary complex with acylACP and protoxin substrates
    • Stanley P, Hyland C, Koronakis V, Hughes C. 1999. An ordered reaction mechanism for bacterial toxin acylation by the specialized acyltransferases HlyC: formation of a ternary complex with acylACP and protoxin substrates. Mol. Microbiol. 34:887-901. (Pubitemid 30000308)
    • (1999) Molecular Microbiology , vol.34 , Issue.5 , pp. 887-901
    • Stanley, P.1    Hyland, C.2    Koronakis, V.3    Hughes, C.4
  • 222
    • 0032584294 scopus 로고    scopus 로고
    • The biochemistry of hemolysin toxin activation: Characterization of HlyC, an internal protein acyltransferase
    • DOI 10.1021/bi971588y
    • Trent MS, Worsham SMS, Ernst-Fonberg ML. 1998. The biochemistry of hemolysin toxin activation: characterization of HlyC, an internal protein acyltransferase. Biochemistry 37:4644-4652. (Pubitemid 28217183)
    • (1998) Biochemistry , vol.37 , Issue.13 , pp. 4644-4652
    • Trent, M.S.1    Worsham, L.M.S.2    Ernst-Fonberg, M.L.3
  • 224
    • 0033587587 scopus 로고    scopus 로고
    • HlyC, the internal protein acyltransferase that activates hemolysin toxin: Roles of various conserved residues in enzymatic activity as probed by site-directed mutagenesis
    • Trent MS, Worsham LMS, Ernst-Fonberg ML. 1999. HlyC, the internal protein acyltransferase that activates hemolysin toxin: roles of various conserved residues in enzymatic activity as probed by site-directed mutagenesis. Biochemistry 38:9541-9548.
    • (1999) Biochemistry , vol.38 , pp. 9541-9548
    • Trent, M.S.1    Worsham, L.M.S.2    Ernst-Fonberg, M.L.3
  • 225
    • 13444278560 scopus 로고    scopus 로고
    • Thermodynamics of a protein acylation: Activation of Escherichia coli hemolysin toxin
    • DOI 10.1021/bi048479l
    • Worsham LMS, Langston KG, Ernst-Fonberg ML. 2005. Thermodynamics of a protein acylation: activation of Escherichia coli hemolysin toxin. Biochemistry 44:1329-1337. (Pubitemid 40209012)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1329-1337
    • Worsham, L.M.S.1    Langston, K.G.2    Ernst-Fonberg, M.L.3
  • 226
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • DOI 10.1038/379177a0
    • Dodds AW, Ren XD, Willis AC, Law SKA. 1996. The reaction mechanism of the internal thioester in the human complement component C4. Nature 379:177-179. (Pubitemid 26020202)
    • (1996) Nature , vol.379 , Issue.6561 , pp. 177-179
    • Dodds, A.W.1    Ren, X.-D.2    Willis, A.C.3    Law, S.K.A.4
  • 227
    • 0029009588 scopus 로고
    • The effect of residue 1106 on the thioester-mediated covalent binding reaction of human complement protein C4 and the monomeric rat α-macroglobulin α1I3
    • Ren XD, Dodds AW, Enghild JJ, Chu CT, Law SKA. 1995. The effect of residue 1106 on the thioester-mediated covalent binding reaction of human complement protein C4 and the monomeric rat α-macroglobulin α1I3. FEBS Lett. 368:87-91.
    • (1995) FEBS Lett. , vol.368 , pp. 87-91
    • Ren, X.D.1    Dodds, A.W.2    Enghild, J.J.3    Chu, C.T.4    Law, S.K.A.5
  • 228
    • 0344609226 scopus 로고    scopus 로고
    • The conserved lysine 860 in the additional fatty acylation site of Bordetella pertussis adenylate cyclase is crucial for toxin function independently of its acylation status
    • Basar T, Havlicek V, Bezouskova S, Halada P, Hackett M, Šebo P. 1999. The conserved lysine 860 in the additional fatty acylation site of Bordetella pertussis adenylate cyclase is crucial for toxin function independently of its acylation status. J. Biol. Chem. 274:10777-10783.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10777-10783
    • Basar, T.1    Havlicek, V.2    Bezouskova, S.3    Halada, P.4    Hackett, M.Š.P.5
  • 229
    • 0028519151 scopus 로고
    • Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis
    • Hackett M, Guo L, Shabanowitz J, Hunt DF, Hewlett EL. 1994. Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis. Science 266:433-435. (Pubitemid 24348962)
    • (1994) Science , vol.266 , Issue.5184 , pp. 433-435
    • Hackett, M.1    Guo, L.2    Shabanowitz, J.3    Hunt, D.F.4    Hewlett, E.L.5
  • 231
    • 0035046806 scopus 로고    scopus 로고
    • Mass spectrometric analysis of recombinant adenylate cyclase toxin from Bordetella pertussis strain 18323/pHSP9
    • DOI 10.1002/jms.139
    • Havlicek V, Higgins L, Chen W, Halada P, Šebo P, Sakamoto H, Hackett M. 2001. Mass spectrometric analysis of recombinant adenylate cyclase toxin from Bordetella pertussis strain 18323/pHSP9. J. Mass. Spectrom. 36:384-391. (Pubitemid 32409882)
    • (2001) Journal of Mass Spectrometry , vol.36 , Issue.4 , pp. 384-391
    • Havlicek, V.1    Higgins, L.2    Chen, W.3    Halada, P.4    Sbo, P.5    Sakamoto, H.6    Hackett, M.7
  • 232
    • 0027986805 scopus 로고
    • Identification and immunological characterization of the domain of Actinobacillus actinomycetemcomitans leukotoxin that determines its specificity for human target cells
    • Lally ET, Golub EE, Kieba IR. 1994. Identification and immunological characterization of the domain of Actinobacillus actinomycetemcomitans leukotoxin that determines its specificity for human target cells. J. Biol. Chem. 269:31289-31295. (Pubitemid 24377630)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.49 , pp. 31289-31295
    • Lally, E.T.1    Golub, E.E.2    Kieba, I.R.3
  • 234
    • 84858071530 scopus 로고    scopus 로고
    • Lipase promiscuity and its biochemical applications
    • Kapoor M, Gupta MN. 2012. Lipase promiscuity and its biochemical applications. Process Biochem. 47:555-569.
    • (2012) Process Biochem. , vol.47 , pp. 555-569
    • Kapoor, M.1    Gupta, M.N.2
  • 235
    • 54549084559 scopus 로고    scopus 로고
    • Enzymatic biodiesel production: Technical and economical considerations
    • Nielsen PM, Brask J, Fjerbaek L. 2008. Enzymatic biodiesel production: technical and economical considerations. Eur. J. Lipid Sci. Technol. 110:692-700.
    • (2008) Eur. J. Lipid Sci. Technol. , vol.110 , pp. 692-700
    • Nielsen, P.M.1    Brask, J.2    Fjerbaek, L.3
  • 237
  • 238
    • 71549149350 scopus 로고    scopus 로고
    • Biodiesel production through lipase catalyzed transesterification: An overview
    • Bajaj A, Lohan P, Jha PN, Mehrotra R. 2010. Biodiesel production through lipase catalyzed transesterification: an overview. J. Mol. Catal. B Enzym. 62:9-14.
    • (2010) J. Mol. Catal. B Enzym. , vol.62 , pp. 9-14
    • Bajaj, A.1    Lohan, P.2    Jha, P.N.3    Mehrotra, R.4
  • 239
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • DOI 10.1146/annurev.micro.53.1.315
    • Jaeger KE, Dijkstra BW, Reetz MT. 1999. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu. Rev. Microbiol. 53:315-351. (Pubitemid 29503734)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 315-351
    • Jaeger, K.-E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 241
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and α/β hydrolase fold
    • Schrag JD, Cygler M. 1997. Lipases and α/β hydrolase fold. Methods Enzymol. 284:85-107.
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 242
    • 0027023208 scopus 로고
    • Structural and evolutionary relationships in lipase mechanism and activation
    • Dodson GG, Lawson DM, Winkler FK. 1992. Structural and evolutionary relationships in lipase mechanism and activation. Faraday Discuss. 93:95-105.
    • (1992) Faraday Discuss. , vol.93 , pp. 95-105
    • Dodson, G.G.1    Lawson, D.M.2    Winkler, F.K.3
  • 243
    • 76649108895 scopus 로고    scopus 로고
    • Janus-faced enzymes yeast Tgl3p and Tgl5p catalyze lipase and acyltransferase reactions
    • Rajakumari S, Daum G. 2010. Janus-faced enzymes yeast Tgl3p and Tgl5p catalyze lipase and acyltransferase reactions. Mol. Biol. Cell 21:501-510.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 501-510
    • Rajakumari, S.1    Daum, G.2
  • 244
    • 0033046562 scopus 로고    scopus 로고
    • Metabolic engineering of poly(3-hydroxyalkanoates): From DNA to plastic
    • Madison LL, Huisman GW. 1999. Metabolic engineering of poly(3-hydroxyalkanoates): from DNA to plastic. Microbiol. Mol. Biol. Rev. 63:21-53. (Pubitemid 29116086)
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.1 , pp. 21-53
    • Madison, L.L.1    Huisman, G.W.2
  • 245
    • 77954757413 scopus 로고    scopus 로고
    • Bacterial polymers: Biosynthesis, modifications and applications
    • Rehm BHA. 2010. Bacterial polymers: biosynthesis, modifications and applications. Nat. Rev. Microbiol. 8:578-592.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 578-592
    • Rehm, B.H.A.1
  • 246
    • 0035155574 scopus 로고    scopus 로고
    • Identification of a new class of biopolymer: Bacterial synthesis of a sulfur-containing polymer with thioester linkages
    • Lütke-Eversloh T, Bergander K, Luftmann H, Steinbüchel A. 2001. Identification of a new class of biopolymer: bacterial synthesis of a sulfur-containing polymer with thioester linkages. Microbiology 147:11-19.
    • (2001) Microbiology , vol.147 , pp. 11-19
    • Lütke-Eversloh, T.1    Bergander, K.2    Luftmann, H.3    Steinbüchel, A.4
  • 248
    • 0030536814 scopus 로고    scopus 로고
    • Synthesis and production of biodegradable thermoplastics and elastomers: Current state and outlook
    • Steinbüchel A. 1996. Synthesis and production of biodegradable thermoplastics and elastomers: current state and outlook. Kautschuk Gummi Kunststoffe 49:120-124.
    • (1996) Kautschuk Gummi Kunststoffe , vol.49 , pp. 120-124
    • Steinbüchel, A.1
  • 249
    • 27844566753 scopus 로고    scopus 로고
    • Non-biodegradable biopolymers from renewable resources: Perspectives and impacts
    • Steinbüchel A. 2005. Non-biodegradable biopolymers from renewable resources: perspectives and impacts. Curr. Opin. Biotechnol. 16:607-613.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 607-613
    • Steinbüchel, A.1
  • 250
    • 41449087762 scopus 로고    scopus 로고
    • Biological degradation of plastics: A comprehensive review
    • Shah AA, Hasan F, Hameed A, Ahmed S. 2008. Biological degradation of plastics: a comprehensive review. Biotechnol. Adv. 26:246-265.
    • (2008) Biotechnol. Adv. , vol.26 , pp. 246-265
    • Shah, A.A.1    Hasan, F.2    Hameed, A.3    Ahmed, S.4
  • 251
    • 0033802118 scopus 로고    scopus 로고
    • Polymer production by two newly isolated extremely halophilic archaea: Application of a novel corrosion-resistant bioreactor
    • Hezayen FF, Rehm BHA, Eberhardt R, Steinbüchel A. 2000. Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl. Microbiol. Biotechnol. 54:319-325.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 319-325
    • Hezayen, F.F.1    Rehm, B.H.A.2    Eberhardt, R.3    Steinbüchel, A.4
  • 252
    • 0025282845 scopus 로고
    • Effects of culture conditions on poly(beta-hydroxybutyrate acid) production by Haloferax mediterranei
    • Lillo JG, Rodriguez-Valera F. 1990. Effects of culture conditions on poly(β-hydroxybutyric acid) production by Haloferax mediterranei. Appl. Environ. Microbiol. 56:2517-2521. (Pubitemid 20235698)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.8 , pp. 2517-2521
    • Garcia, L.J.1    Rodriguez-Valera, F.2
  • 253
    • 0001038052 scopus 로고
    • Formation and utilization of poly-beta-hydroxybutyric acid by knallgas bacteria (Hydrogenomonas)
    • Schlegel HG, Gottschalk G, Von Bartha R. 1961. Formation and utilization of poly-beta-hydroxybutyric acid by knallgas bacteria (Hydrogenomonas). Nature 191:463-465.
    • (1961) Nature , vol.191 , pp. 463-465
    • Schlegel, H.G.1    Gottschalk, G.2    Von Bartha, R.3
  • 254
    • 0024713037 scopus 로고
    • Synthesis of poly-3-hydroxyalkanoates is a common feature of fluorescent pseudomonads
    • Huisman GW, de Leeuw O, Eggink G, Witholt B. 1989. Synthesis of poly-3-hydroxyalkanoates is a common feature of fluorescent pseudomonads. Appl. Environ. Microbiol. 55:1949-1954.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 1949-1954
    • Huisman, G.W.1    De Leeuw, O.2    Eggink, G.3    Witholt, B.4
  • 255
    • 0025002088 scopus 로고
    • Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acids from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads
    • Timm A, Steinbüchel A. 1990. Formation of polyesters consisting of medium-chain-length 3-hydroxyalkanoic acids from gluconate by Pseudomonas aeruginosa and other fluorescent pseudomonads. Appl. Environ. Microbiol. 56:3360-3367.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3360-3367
    • Timm, A.1    Steinbüchel, A.2
  • 256
    • 0032508549 scopus 로고    scopus 로고
    • A new metabolic link between fatty acid de novo synthesis and polyhydroxyalkanoic acid synthesis
    • Rehm BHA, Krüger N, Steinbüchel A. 1998. A new metabolic link between fatty acid de novo synthesis and polyhydroxyalkanoic acid synthesis. J. Biol. Chem. 273:24044-24051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24044-24051
    • Rehm, B.H.A.1    Krüger, N.2    Steinbüchel, A.3
  • 257
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: Natural catalysts for plastics
    • DOI 10.1042/BJ20031254
    • Rehm BHA. 2003. Polyester synthases: natural catalysts for plastics. Biochem. J. 376:15-33. (Pubitemid 37487200)
    • (2003) Biochemical Journal , vol.376 , Issue.1 , pp. 15-33
    • Rehm, B.H.A.1
  • 258
    • 0035882164 scopus 로고    scopus 로고
    • Matrix-assisted in vitro refolding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli
    • DOI 10.1042/0264-6021:3580263
    • Rehm BHA, Qi QS, Beermann BB, Hinz HJ, Steinbüchel A. 2001. Matrix-assisted in vitro folding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli. Biochem. J. 358:263-268. (Pubitemid 32778122)
    • (2001) Biochemical Journal , vol.358 , Issue.1 , pp. 263-268
    • Rehm, B.H.A.1    Qi, Q.2    Beermann, B..B.3    Hinz, H.-J.4    Steinbuchel, A.5
  • 260
    • 0028151543 scopus 로고
    • Purification and characterization of the poly(hydroxyalkanoic acid) synthase from Chromatium vinosum and localization of the enzyme at the surface of poly(hydroxyalkanoic acid) granules
    • DOI 10.1111/j.1432-1033.1994.tb20027.x
    • Liebergesell M, Sonomoto K, Madkour M, Mayer F, Steinbüchel A. 1994. Purification and characterization of the poly(hydroxyalkanoic acid) synthase from Chromatium vinosum and localization of the enzyme at the surface of poly(hydroxyalkanoic acid) granules. Eur. J. Biochem. 226:71-80. (Pubitemid 24348670)
    • (1994) European Journal of Biochemistry , vol.226 , Issue.1 , pp. 71-80
    • Liebergesell, M.1    Sonomoto, K.2    Madkour, M.3    Mayer, F.4    Steinbuchel, A.5
  • 262
    • 0041328584 scopus 로고    scopus 로고
    • Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: Identification of catalytic residues
    • DOI 10.1042/BJ20030431
    • Amara AA, Rehm BHA. 2003. Replacement of the catalytic nucleophile Cys-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa-mediated synthesis of a new polyester: identification of catalytic residues. Biochem. J. 374:413-421. (Pubitemid 37094100)
    • (2003) Biochemical Journal , vol.374 , Issue.2 , pp. 413-421
    • Amara, A.A.1    Rehm, B.H.A.2
  • 263
    • 0034636122 scopus 로고    scopus 로고
    • Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase
    • DOI 10.1021/bi9928086
    • Jia Y, Kappock TJ, Frick T, Sinskey AJ, Stubbe J. 2000. Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase. Biochemistry 39:3927-3936. (Pubitemid 30210368)
    • (2000) Biochemistry , vol.39 , Issue.14 , pp. 3927-3936
    • Jia, Y.1    Kappock, T.J.2    Frick, T.3    Sinskey, A.J.4    Stubbe, J.5
  • 264
    • 0035218357 scopus 로고    scopus 로고
    • Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: Molecular characterization of the polyhydroxybutyrate synthase
    • Qi Q, Rehm BH. 2001. Polyhydroxybutyrate biosynthesis in Caulobacter crescentus: molecular characterization of the polyhydroxybutyrate synthase. Microbiology 147:3353-3358. (Pubitemid 33150341)
    • (2001) Microbiology , vol.147 , Issue.12 , pp. 3353-3358
    • Qi, Q.1    Rehm, B.H.A.2
  • 265
    • 0037203912 scopus 로고    scopus 로고
    • Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: In vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model
    • Rehm BHA, Antonio RV, Spiekermann P, Amara AA, Steinbüchel A. 2002. Molecular characterization of the poly(3-hydroxybutyrate) (PHB) synthase from Ralstonia eutropha: in vitro evolution, site-specific mutagenesis and development of a PHB synthase protein model. Biochim. Biophys. Acta 1594:178-190.
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 178-190
    • Rehm, B.H.A.1    Antonio, R.V.2    Spiekermann, P.3    Amara, A.A.4    Steinbüchel, A.5
  • 266
    • 33750993043 scopus 로고    scopus 로고
    • Sequence analysis and structure prediction of type II Pseudomonas sp. USM 4-55 PHA synthase and an insight into its catalytic mechanism
    • Wahab HA, Ahmad Khairudin NB, Samian MR, Najimudin N. 2006. Sequence analysis and structure prediction of type II Pseudomonas sp. USM 4-55 PHA synthase and an insight into its catalytic mechanism. BMC Struct. Biol. 6:23-37.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 23-37
    • Wahab, H.A.1    Ahmad Khairudin, N.B.2    Samian, M.R.3    Najimudin, N.4
  • 268
    • 0343485085 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa phaG gene product is involved in the synthesis of polyhydroxyalkanoic acid consisting of medium-chain-length constituents from non-related carbon sources
    • Hoffmann N, Steinbüchel A, Rehm BHA. 2000. The Pseudomonas aeruginosa phaG gene product is involved in the synthesis of polyhydroxyalkanoic acid consisting of medium-chain-length constituents from non-related carbon sources. FEMS Microbiol. Lett. 184:253-259.
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 253-259
    • Hoffmann, N.1    Steinbüchel, A.2    Rehm, B.H.A.3
  • 269
    • 0037044780 scopus 로고    scopus 로고
    • Biochemical characterization of the Pseudomonas putida 3-hydroxyacyl ACP:CoA transacylase, which diverts intermediates of fatty acid de novo biosynthesis
    • DOI 10.1074/jbc.M207821200
    • Hoffmann N, Amara AA, Beermann BB, Qi A, Hinz HJ, Rehm BHA. 2002. Biochemical characterization of the Pseudomonas putida 3-hydroxyacyl ACP:CoA transacylase, which diverts intermediates of fatty acid de novo biosynthesis. J. Biol. Chem. 277:42926-42936. (Pubitemid 35285670)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42926-42936
    • Hoffmann, N.1    Amara, A.A.2    Beermann, B..B.3    Qi, N.4    Hinz, H.-J.5    Rehm, B.H.A.6
  • 270
    • 0035511957 scopus 로고    scopus 로고
    • Accumulation of Polyhydroxyalkanoic Acid Containing Large Amounts of Unsaturated Monomers in Pseudomonas fluorescens BM07 Utilizing Saccharides and Its Inhibition by 2-Bromooctanoic Acid
    • Lee HJ, Choi MH, Kim TU, Yoon SC. 2001. Accumulation of polyhydroxyalkanoic acid containing large amounts of unsaturated monomers in Pseudomonas fluorescens BM07 utilizing saccharides and its inhibition by 2-bromooctanoic acid. Appl. Environ. Microbiol. 67:4963-4974. (Pubitemid 33701258)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.3-12 , pp. 4963-4974
    • Lee, H.O.-J.1    Choi, M.H.2    Kim, T.-U.N.3    Yoon, S.C.4
  • 271
    • 12144271300 scopus 로고    scopus 로고
    • Channeling of intermediates derived from medium-chain fatty acids and De novo-synthesized fatty acids to polyhydroxyalkanoic acid by 2-bromooctanoic acid in Pseudomonas fluorescens BM07
    • Lee HJ, Rho JK, Noghabi KA, Lee SE, Choi MH, Yoon SC. 2004. Channeling of intermediates derived from medium-chain fatty acids and de novo-synthesized fatty acids to polyhydroxyalkanoic acid by 2-bromooctanoic acid in Pseudomonas fluorescens BM07. J. Microbiol. Biotechnol. 14:1256-1266. (Pubitemid 40104198)
    • (2004) Journal of Microbiology and Biotechnology , vol.14 , Issue.6 , pp. 1256-1266
    • Lee, H.-J.1    Rho, J.K.2    Noghabi, K.A.3    Lee, S.E.4    Choi, M.H.5    Yoon, S.C.6
  • 272
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones DT, Taylor WR, Thornton JM. 1992. A new approach to protein fold recognition. Nature 358:86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 273
    • 33646002994 scopus 로고    scopus 로고
    • Comparative modeling of protein structure prediction
    • Ginalski K. 2006. Comparative modeling of protein structure prediction. Curr. Opin. Struct. Biol. 16:172-177.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 172-177
    • Ginalski, K.1
  • 274
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22:195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 275
    • 27444440537 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of (R)-3-hydroxyacyl-acyl carrier protein:coenzyme A transacylase from Pseudomonas mendocina LZ
    • DOI 10.1016/j.femsle.2005.09.006, PII S037810970500621X
    • Zheng LZ, Li Z, Tian HL, Li M, Chen GQ. 2005. Molecular cloning and functional analysis of (R)-3-hydroxyacyl-acyl carrier protein:coenzyme A transacylase from Pseudomonas mendocina LZ. FEMS Microbiol. Lett. 252:299-307. (Pubitemid 41531656)
    • (2005) FEMS Microbiology Letters , vol.252 , Issue.2 , pp. 299-307
    • Leo, Z.Z.1    Li, Z.2    Tian, H.-L.3    Li, M.4    Chen, G.-Q.5
  • 276
    • 0037970775 scopus 로고    scopus 로고
    • Identification and characterisation of the catalytic triad of the alkaliphilic thermotolerant PHA depolymerase PhaZ7 of Paucimonas lemoignei
    • DOI 10.1016/S0378-1097(03)00425-7
    • Braaz R, Handrick R, Jendrossek D. 2003. Identification and characterisation of the catalytic triad of the alkaliphilic thermotolerant PHA depolymerase PhaZ7 of Paucimonas lemoignei. FEMS Microbiol. Lett. 224:107-112. (Pubitemid 36830831)
    • (2003) FEMS Microbiology Letters , vol.224 , Issue.1 , pp. 107-112
    • Braaz, R.1    Handrick, R.2    Jendrossek, D.3
  • 277
    • 0026305078 scopus 로고
    • Relationships among serine hydrolases - Evidence for a common structural motif in triacylglyceride lipases and esterases
    • Derewenda ZS, Derewenda U. 1991. Relationships among serine hydrolases - evidence for a common structural motif in triacylglyceride lipases and esterases. Biochem. Cell Biol. 69:842-851.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 842-851
    • Derewenda, Z.S.1    Derewenda, U.2
  • 278
    • 33745542346 scopus 로고    scopus 로고
    • Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterases I/protease I/phospholipase L1
    • Lee LC, Lee YL, Leu RJ, Shaw JF. 2006. Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterases I/protease I/phospholipase L1. Biochem. J. 397:69-76.
    • (2006) Biochem. J. , vol.397 , pp. 69-76
    • Lee, L.C.1    Lee, Y.L.2    Leu, R.J.3    Shaw, J.F.4
  • 280
    • 0029061966 scopus 로고
    • The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Åresolution
    • Serre L, Verbree EC, Dauter Z, Stuitje AR, Derewenda ZS. 1995. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-Åresolution. J. Biol. Chem. 270:12961-12964.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12961-12964
    • Serre, L.1    Verbree, E.C.2    Dauter, Z.3    Stuitje, A.R.4    Derewenda, Z.S.5
  • 281
    • 34249803594 scopus 로고    scopus 로고
    • Malonyl-CoA: Acyl carrier protein transacylase from Helicobacter pylori: Crystal structure and its interaction with acyl carrier protein
    • DOI 10.1110/ps.072757307
    • Zhang L, Liu WL, Xiao J, Hu T, Chen J, Chen K, Jiang H, Shen X. 2007. Malonyl-CoA:acyl carrier protein transacylase from Helicobacter pylori: crystal structure and its interaction with acyl carrier protein. Protein Sci. 16:1184-1192. (Pubitemid 46849226)
    • (2007) Protein Science , vol.16 , Issue.6 , pp. 1184-1192
    • Zhang, L.1    Liu, W.2    Xiao, J.3    Hu, T.4    Chen, J.5    Chen, K.6    Jiang, H.7    Shen, X.8
  • 282
    • 27444436717 scopus 로고    scopus 로고
    • Specific identification of (R)-3-hydroxyacyl-ACP:CoA transacylase gene from Pseudomonas and Burkholderia strains by polymerase chain reaction
    • Zheng Z, Chen JC, Tian HL, Bei FF, Chen GQ. 2005. Specific identification of (R)-3-hydroxyacyl-ACP:CoA transacylase gene from Pseudomonas and Burkholderia strains by polymerase chain reaction. Chin. J. Biotechnol. 21:19-24.
    • (2005) Chin. J. Biotechnol. , vol.21 , pp. 19-24
    • Zheng, Z.1    Chen, J.C.2    Tian, H.L.3    Bei, F.F.4    Chen, G.Q.5
  • 283
    • 0033695263 scopus 로고    scopus 로고
    • Homologous functional expression of cryptic phaG from Pseudomonas oleovorans established the transacylase-mediated polyhydroxyalkanoate biosynthetic pathway
    • Hoffmann N, Steinbüchel A, Rehm BHA. 2000. Homologous functional expression of cryptic phaG from Pseudomonas oleovorans established the transacylase-mediated polyhydroxyalkanoate biosynthetic pathway. Appl. Microbiol. Biotechnol. 54:665-670.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 665-670
    • Hoffmann, N.1    Steinbüchel, A.2    Rehm, B.H.A.3
  • 284
    • 0034883910 scopus 로고    scopus 로고
    • Cloning and characterization of the pseudomonas sp. 61-3phaG gene involved in polyhydroxyalkanoate biosynthesis
    • DOI 10.1021/bm005604+
    • Matsumoto K, Matsusaki H, Taguchi S, Seki M, Doi Y. 2001. Cloning and characterization of the Pseudomonas sp. 61-3 phaG gene involved in polyhydroxyalkanoate biosynthesis. Biomacromolecules 2:142-147. (Pubitemid 32707484)
    • (2001) Biomacromolecules , vol.2 , Issue.1 , pp. 142-147
    • Matsumoto, K.1    Matsusaki, H.2    Taguchi, S.3    Seki, M.4    Doi, Y.5
  • 285
    • 0009709890 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate accumulation in Burkholderia sp.: A molecular approach to elucidate the genes involved in the formation of two homopolymers consisting of short-chain-length 3-hydroxyalkanoic acids
    • Rodrigues MF, Valentin HE, Berger PA, Tran M, Asrar J, Gruys KJ, Steinbüchel A. 2000. Polyhydroxyalkanoate accumulation in Burkholderia sp.: a molecular approach to elucidate the genes involved in the formation of two homopolymers consisting of short-chain-length 3-hydroxyalkanoic acids. Appl. Microbiol. Biotechnol. 53:453-460. (Pubitemid 30236120)
    • (2000) Applied Microbiology and Biotechnology , vol.53 , Issue.4 , pp. 453-460
    • De Andrade, R.M.F.1    Valentin, H.E.2    Berger, P.A.3    Tran, M.4    Asrar, J.5    Gruys, K.J.6    Steinbuchel, A.7
  • 286
    • 0037161195 scopus 로고    scopus 로고
    • PCR cloning of polyhydroxyalkanoate biosynthesis genes from Burkholderia caryophylli and their functional expression in recombinant Escherichia coli
    • DOI 10.1016/S0378-1097(02)00594-3, PII S0378109702005943
    • Hang X, Zhang G, Wang G, Zhao X, Chen GQ. 2002. PCR cloning of polyhydroxyalkanoate biosynthesis genes from Burkholderia caryophylli and their functional expression in recombinant Escherichia coli. FEMS Microbiol. Lett. 210:49-54. (Pubitemid 34521948)
    • (2002) FEMS Microbiology Letters , vol.210 , Issue.1 , pp. 49-54
    • Hang, X.1    Zhang, G.2    Wang, G.3    Zhao, X.4    Chen, G.-Q.5
  • 287
    • 0342369388 scopus 로고    scopus 로고
    • PhaG-mediated synthesis of poly(3-hydroxyalkanoates) consisting of medium-chain-length constituents from nonrelated carbon sources in recombinant Pseudomonas fragi
    • Fiedler S, Steinbüchel A, Rehm BHA. 2000. PhaG-mediated synthesis of poly(3-hydroxyalkanoates) consisting of medium-chain-length constituents from nonrelated carbon sources in recombinant Pseudomonas fragi. Appl. Environ. Micbrobiol. 66:2117-2124.
    • (2000) Appl. Environ. Micbrobiol. , vol.66 , pp. 2117-2124
    • Fiedler, S.1    Steinbüchel, A.2    Rehm, B.H.A.3
  • 288
    • 33846678317 scopus 로고    scopus 로고
    • Effect of heterologous expression of phaG [(R)-3-hydroxyacyl-ACP-CoA transferase] on polyhydroxyalkanoate accumulation from the aromatic hydrocarbon phenylacetic acid in Pseudomonas species
    • DOI 10.1111/j.1574-6968.2006.00607.x
    • Tobin KM, O'Leary NDO, Dobson ADW, O'Connor KE. 2007. Effect of heterologous expression of phaG [(R)-3-hydroxyacyl-ACP-CoA transferase] on polyhydroxyalkanoate accumulation from the aromatic hydrocarbon phenylacetic acid in Pseudomonas species. FEMS Microbiol. Lett. 268:9-15. (Pubitemid 46192829)
    • (2007) FEMS Microbiology Letters , vol.268 , Issue.1 , pp. 9-15
    • Tobin, K.M.1    O'Leary, N.D.2    Dobson, A.D.W.3    O'Connor, K.E.4
  • 290
    • 0032924821 scopus 로고    scopus 로고
    • Rhamnose lipids - Biosynthesis, microbial production and application potential
    • DOI 10.1007/s002530051358
    • Lang S, Wullbrandt D. 1999. Rhamnose lipids-biosynthesis, microbial production and application potential. Appl. Microbiol. Biotechnol. 51:22-32. (Pubitemid 29066642)
    • (1999) Applied Microbiology and Biotechnology , vol.51 , Issue.1 , pp. 22-32
    • Lang, S.1    Wullbrandt, D.2
  • 291
    • 0033860175 scopus 로고    scopus 로고
    • Role of rhamnolipid biosurfactants in the uptake and mineralization of hexadecane in Pseudomonas aeruginosa
    • DOI 10.1046/j.1365-2672.2000.01104.x
    • Beal R, Betts WB. 2000. Role of rhamnolipid biosurfactants in the uptake and mineralization of hexadecane in Pseudomonas aeruginosa. J. Appl. Microbiol. 89:158-168. (Pubitemid 30602438)
    • (2000) Journal of Applied Microbiology , vol.89 , Issue.1 , pp. 158-168
    • Beal, R.1    Betts, W.B.2
  • 292
    • 0003124346 scopus 로고
    • Formation and function of biosurfactants for degradation of water-insoluble substrates
    • Ratledge C (ed), Kluwer Academic Publishers, London, United Kingdom
    • Hommel R. 1994. Formation and function of biosurfactants for degradation of water-insoluble substrates, p 63-87. In Ratledge C (ed), Biochemistry of microbial degradation. Kluwer Academic Publishers, London, United Kingdom.
    • (1994) Biochemistry of Microbial Degradation , pp. 63-87
    • Hommel, R.1
  • 293
    • 0036727256 scopus 로고    scopus 로고
    • Rhamnolipid stimulates uptake of hydrophobic compounds by Pseudomonas aeruginosa
    • DOI 10.1128/AEM.68.9.4502-4508.2002
    • Noordman WH, Janssen DB. 2002. Rhamnolipid stimulates uptake of hydrophobic compounds by Pseudomonas aeruginosa. Appl. Environ. Microbiol. 68:4502-4508. (Pubitemid 34988134)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.9 , pp. 4502-4508
    • Noordman, W.H.1    Janssen, D.B.2
  • 294
    • 0042424964 scopus 로고    scopus 로고
    • rhlA is required for the production of a novel biosurfactant promoting swarming motility in Pseudomonas aeruginosa: 3-(3-hydroxyalkanoyloxy)alkanoic acids (HAAs), the precursors of rhamnolipids
    • Déziel E, Lépine F, Milot S, Villemur R. 2003. rhlA is required for the production of a novel biosurfactant promoting swarming motility in Pseudomonas aeruginosa: 3-(3-hydroxyalkanoyloxy)alkanoic acids (HAAs), the precursors of rhamnolipids. Microbiology 149:2005-2013.
    • (2003) Microbiology , vol.149 , pp. 2005-2013
    • Déziel, E.1    Lépine, F.2    Milot, S.3    Villemur, R.4
  • 295
    • 41949089310 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa exhibits sliding motility in the absence of type IV pili and flagella
    • DOI 10.1128/JB.01620-07
    • Murray TS, Kazmierczak BI. 2008. Pseudomonas aeruginosa exhibits sliding motility in the absence of type IV pili and flagella. J. Bacteriol. 190:2700-2708. (Pubitemid 351508170)
    • (2008) Journal of Bacteriology , vol.190 , Issue.8 , pp. 2700-2708
    • Murray, T.S.1    Kazmierczak, B.I.2
  • 296
    • 0033854780 scopus 로고    scopus 로고
    • Rhamnolipid-induced removal of lipopolysaccharide from Pseudomonas aeruginosa: Effect on cell surface properties and interaction with hydrophobic substrates
    • DOI 10.1128/AEM.66.8.3262-3268.2000
    • Al-Tahhan RA, Sandrin TR, Bodour AA, Maier RM. 2000. Rhamnolipid induced removal of lipopolysaccharide from Pseudomonas aeruginosa: effect on cell surface properties and interaction with hydrophobic substrates. Appl. Environ. Microbiol. 66:3262-3268. (Pubitemid 30624566)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.8 , pp. 3262-3268
    • Al-Tahhan, R.A.1    Sandrin, T.R.2    Bodour, A.A.3    Maier, R.M.4
  • 297
    • 43549091320 scopus 로고    scopus 로고
    • Rhamnolipid-biosurfactant permeabilizing effects on gram-positive and gram-negative bacterial strains
    • Sotirova AV, Spasova DI, Galabova DN, Karpenko E, Shulga A. 2008. Rhamnolipid-biosurfactant permeabilizing effects on gram-positive and gram-negative bacterial strains. Curr. Microbiol. 56:639-644.
    • (2008) Curr. Microbiol. , vol.56 , pp. 639-644
    • Sotirova, A.V.1    Spasova, D.I.2    Galabova, D.N.3    Karpenko, E.4    Shulga, A.5
  • 299
    • 33646908499 scopus 로고    scopus 로고
    • Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa
    • DOI 10.1128/IAI.01772-05
    • Zulianello L, Canard C, Köhler T, Caille D, Lacroix JS, Meda P. 2006. Rhamnolipids are virulence factors that promote early infiltration of primary human airway epithelia by Pseudomonas aeruginosa. Infect. Immun. 74:3134-3147. (Pubitemid 43794502)
    • (2006) Infection and Immunity , vol.74 , Issue.6 , pp. 3134-3147
    • Zulianello, L.1    Canard, C.2    Kohler, T.3    Caille, D.4    Lacroix, J.-S.5    Meda, P.6
  • 300
    • 0035408259 scopus 로고    scopus 로고
    • Role of Fatty Acid de novo Biosynthesis in Polyhydroxyalkanoic Acid (PHA) and Rhamnolipid Synthesis by Pseudomonads: Establishment of the Transacylase (PhaG)-Mediated Pathway for PHA Biosynthesis in Escherichia coli
    • DOI 10.1128/AEM.67.7.3102-3109.2001
    • Rehm BHA, Mitsky TA, Steinbüchel A. 2001. Role of fatty acid de novo biosynthesis in polyhydroxyalkanoic acid (PHA) and rhamnolipids synthesis by pseudomonads: establishment of the transacylase (PhaG)-mediated pathway for PHA biosynthesis in Eschericia coli. Appl. Environ. Microbiol. 67:3102-3109. (Pubitemid 33644779)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.7 , pp. 3102-3109
    • Rehm, B.H.A.1    Mitsky, T.A.2    Steinbuchel, A.3
  • 301
    • 78650677960 scopus 로고    scopus 로고
    • Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: Comparative 13C NMR analysis of the products in wild-type and mutants
    • Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC. 2011. Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 13C NMR analysis of the products in wild-type and mutants. J. Biotechnol. 151:30-42.
    • (2011) J. Biotechnol. , vol.151 , pp. 30-42
    • Choi, M.H.1    Xu, J.2    Gutierrez, M.3    Yoo, T.4    Cho, Y.H.5    Yoon, S.C.6
  • 302
    • 18144442340 scopus 로고    scopus 로고
    • Liquid chromatography/mass spectrometry analysis of mixtures of rhamnolipids produced by Pseudomonas aeruginosa strain 57RP grown on mannitol or naphthalene
    • Déziel E, Lépine F, Dennie D, Boismenu D, Mamer OA, Villemur R. 1999. Liquid chromatography/mass spectrometry analysis of mixtures of rhamnolipids produced by Pseudomonas aeruginosa strain 57RP grown on mannitol or naphthalene. Biochim. Biophys. Acta 1440:244-252.
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 244-252
    • Déziel, E.1    Lépine, F.2    Dennie, D.3    Boismenu, D.4    Mamer, O.A.5    Villemur, R.6
  • 303
    • 42549137476 scopus 로고    scopus 로고
    • RhlA converts beta-hydroxyacyl-acyl carrier protein intermediates in fatty acid synthesis to the beta-hydroxydecanoyl-beta-hydroxydecanoate component of rhamnolipids in Pseudomonas aeruginosa
    • DOI 10.1128/JB.00080-08
    • Zhu K, Rock CO. 2008. RhlA converts β-hydroxyacyl-acyl carrier protein intermediates in fatty acid synthesis to the β-hydroxydecanoyl- β-hydroxydecanoate component of rhamnolipids in Pseudomonas aeruginosa. J. Bacteriol. 190:3147-3154. (Pubitemid 351581409)
    • (2008) Journal of Bacteriology , vol.190 , Issue.9 , pp. 3147-3154
    • Zhu, K.1    Rock, C.O.2
  • 304
    • 0027997539 scopus 로고
    • Isolation, characterization, and expression in Escherichia coli of the Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved in rhamnolipid biosurfactant synthesis
    • Ochsner UA, Fiechter A, Reiser J. 1994. Isolation, characterization, and expression in Escherichia coli of the Pseudomonas aeruginosa rhlAB genes encoding a rhamnosyltransferase involved in rhamnolipid biosurfactant synthesis. J. Biol. Chem. 269:19787-19795. (Pubitemid 24250890)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.31 , pp. 19787-19795
    • Ochsner, U.A.1    Fiechter, A.2    Reiser, J.3
  • 305
    • 0034997723 scopus 로고    scopus 로고
    • Cloning and functional characterization of the Pseudomonas aeruginosa
    • DOI 10.1046/j.1365-2958.2001.02420.x
    • Rahim R, Ochsner UA, Olvera C, Graninger M, Messner P, Lam JS, Soberón-Chávez G. 2001. Cloning and functional characterization of the Pseudomonas aeruginosa rhlC gene that encodes rhamnosyltransferase 2, an enzyme responsible for di-rhamnolipid biosynthesis. Mol. Microbiol. 40:708-718. (Pubitemid 32453123)
    • (2001) Molecular Microbiology , vol.40 , Issue.3 , pp. 708-718
    • Rahim, R.1    Ochsner, U.A.2    Olvera, C.3    Graninger, M.4    Messner, P.5    Lam, J.S.6    Soberon-Chavez, G.7
  • 306
    • 0031750694 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa rhlG gene encodes an NADPH-dependent beta- ketoacyl reductase which is specifically involved in rhamnolipid synthesis
    • Campos-Garcia J, Caro AD, Najera R, Miller-Maier RM, Al-Tahhan RA, Soberon-Chavez G. 1998. The Pseudomonas aeruginosa rhlG gene encodes an NADPH-dependent β-ketoacyl reductase which is specifically involved in rhamnolipid synthesis. J. Bacteriol. 180:4442-4451. (Pubitemid 28405567)
    • (1998) Journal of Bacteriology , vol.180 , Issue.17 , pp. 4442-4451
    • Campos-Garcia, J.1    Caro, A.D.2    Najera, R.3    Miller-Maier, R.M.4    Al-Tahhan, R.A.5    Soberon-Chavez, G.6
  • 307
    • 33745807948 scopus 로고    scopus 로고
    • Structure of RhlG, an essential beta-ketoacyl reductase in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa
    • DOI 10.1074/jbc.M601687200
    • Miller DJ, Zhang YM, Rock CO, White SW. 2006. Structure of RhlG, an essential β-ketoacyl reductase in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa. J. Biol. Chem. 281:18025-18032. (Pubitemid 44035602)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 18025-18032
    • Miller, D.J.1    Zhang, Y.-M.2    Rock, C.O.3    White, S.W.4
  • 308
    • 6444241117 scopus 로고    scopus 로고
    • The role of polyhydroxyalkanoate biosynthesis by Pseudomonas aeruginosa in rhamnolipid and alginate production as well as stress tolerance and biofilm formation
    • DOI 10.1099/mic.0.27357-0
    • Pham TH, Webb JS, Rehm BHA. 2004. The role of polyhydroxyalkanoate biosynthesis by Pseudomonas aeruginosa in rhamnolipid and alginate production as well as stress tolerance and biofilm formation. Microbiology 150:3405-3413. (Pubitemid 39406209)
    • (2004) Microbiology , vol.150 , Issue.10 , pp. 3405-3413
    • Pham, T.H.1    Webb, J.S.2    Rehm, B.H.A.3
  • 309
    • 79960742349 scopus 로고    scopus 로고
    • Regulatory and metabolic network of rhamnolipid biosynthesis: Traditional and advanced engineering towards biotechnological production
    • Müller MM, Hausmann R. 2011. Regulatory and metabolic network of rhamnolipid biosynthesis: traditional and advanced engineering towards biotechnological production. Appl. Microbiol. Biotechnol. 91:251-264.
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 251-264
    • Müller, M.M.1    Hausmann, R.2
  • 310
    • 10744220974 scopus 로고    scopus 로고
    • Mechanism of Pseudomonas aeruginosa RhlR transcriptional regulation of the rhlAB promoter
    • DOI 10.1128/JB.185.20.5976-5983.2003
    • Medina G, Juarez K, Valderrama B, Soberón-Chávez G. 2003. Mechanism of Pseudomonas aeruginosa RhlR transcriptional regulation of the rhlAB promoter. J. Bacteriol. 185:5976-5983. (Pubitemid 37248449)
    • (2003) Journal of Bacteriology , vol.185 , Issue.20 , pp. 5976-5983
    • Medina, G.1    Juarez, K.2    Valderrama, B.3    Soberon-Chavez, G.4


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