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Volumn 18, Issue 1, 2005, Pages 81-101

Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

6 O MYCOLYL BETA DEXTRO MANNOPYRANOSYL 1 PHOSPHOHEPTAPRENOL; ABC TRANSPORTER; ACYL CARRIER PROTEIN; ALPHA METHOXYMYCOLIC ACID; ANTIGEN; ANTIGEN 85; ARABINOGALACTAN; ARABINOGALACTAN MYCOLATE; CARBOHYDRATE DERIVATIVE; COENZYME A; CORD FACTOR; DEXTRO MANNOPYRANOSYL 1 PHOSPHOHEPTAPRENOL; FATTY ACID DERIVATIVE; FATTY ACID SYNTHASE; FATTY ACID SYNTHASE I; FATTY ACID SYNTHASE IIA; FATTY ACID SYNTHASE IIB; HYDROLYASE; MYCOLIC ACID; MYCOLYLTRANSFERASE I; MYCOLYLTRANSFERASE II; OXOMYCOLIC ACID; PHOSPHATASE; PHOSPHATE; PHOSPHORUS DERIVATIVE; POLYKETIDE SYNTHASE; POLYKETIDE SYNTHASE 13; TRANSFERASE; TREHALOSE 6 PHOSPHATE; TREHALOSE MONOMYCOLATE; UNCLASSIFIED DRUG;

EID: 12844278679     PISSN: 08938512     EISSN: None     Source Type: Journal    
DOI: 10.1128/CMR.18.1.81-101.2005     Document Type: Review
Times cited : (542)

References (126)
  • 1
    • 0023689742 scopus 로고
    • Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG
    • Abou-Zeid, C., T. L. Ratliff, H. G. Wiker, M. Harboe, J. Beannedsen, and G. A. Rook. 1988. Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG. Infect. Immun. 56:3046-3051.
    • (1988) Infect. Immun. , vol.56 , pp. 3046-3051
    • Abou-Zeid, C.1    Ratliff, T.L.2    Wiker, H.G.3    Harboe, M.4    Beannedsen, J.5    Rook, G.A.6
  • 2
    • 0035918586 scopus 로고    scopus 로고
    • The loading module of rifamycin synthetase is an adenylation-thiolation didomain with substrate tolerance for substituted benzoates
    • Admiraal, S. J., C. T. Walsh, and C. Khosla. 2001. The loading module of rifamycin synthetase is an adenylation-thiolation didomain with substrate tolerance for substituted benzoates. Biochemistry 40:6116-6123.
    • (2001) Biochemistry , vol.40 , pp. 6116-6123
    • Admiraal, S.J.1    Walsh, C.T.2    Khosla, C.3
  • 3
    • 0035937258 scopus 로고    scopus 로고
    • An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (antigen 85B), a mycolyl transferase
    • Andersen, D. H., G. Harth, M. A. Horwitz, and D. Eisenberg. 2001. An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30 kDa major secretory protein (antigen 85B), a mycolyl transferase. J. Mol. Biol. 307:671-681.
    • (2001) J. Mol. Biol. , vol.307 , pp. 671-681
    • Andersen, D.H.1    Harth, G.2    Horwitz, M.A.3    Eisenberg, D.4
  • 4
    • 0033983325 scopus 로고    scopus 로고
    • Disruption of the genes encoding antigen 85A and antigen 85B of Mycobacterium tuberculosis H37Rv: Effect on growth in culture and in macrophages
    • Armitige, L. Y., C. Jagannath, A. R. Wanger, and S. J. Norris. 2000. Disruption of the genes encoding antigen 85A and antigen 85B of Mycobacterium tuberculosis H37Rv: effect on growth in culture and in macrophages. Infect. Immun. 68:767-778.
    • (2000) Infect. Immun. , vol.68 , pp. 767-778
    • Armitige, L.Y.1    Jagannath, C.2    Wanger, A.R.3    Norris, S.J.4
  • 6
    • 0014473122 scopus 로고
    • Structure des acides α-mycoliques isoles de la souche Canetti de Mycobacterium tuberculosis
    • Asselineau, C., H. Montrozier, and J.-C. Prome. 1969. Structure des acides α-mycoliques isoles de la souche Canetti de Mycobacterium tuberculosis. Bull. Soc. Chem. Fr. 1969:592-596.
    • (1969) Bull. Soc. Chem. Fr. , vol.1969 , pp. 592-596
    • Asselineau, C.1    Montrozier, H.2    Prome, J.-C.3
  • 7
    • 0035987048 scopus 로고    scopus 로고
    • The biosynthesis of mycolic acids by mycobacteria. Current and alternative hypotheses
    • Asselineau, C., J. Asselineau, G. Laneelle, and M. A. Laneelle. 2002. The biosynthesis of mycolic acids by mycobacteria. Current and alternative hypotheses. Prog. Lipid Res. 41:501-523.
    • (2002) Prog. Lipid Res. , vol.41 , pp. 501-523
    • Asselineau, C.1    Asselineau, J.2    Laneelle, G.3    Laneelle, M.A.4
  • 8
    • 0000883209 scopus 로고
    • Structure of the mycolic acids of mycobacteria
    • Asselineau, J., and E. Lederer. 1950. Structure of the mycolic acids of mycobacteria. Nature 166:782-783.
    • (1950) Nature , vol.166 , pp. 782-783
    • Asselineau, J.1    Lederer, E.2
  • 9
    • 0001072149 scopus 로고
    • Studies on the firmly bound lipids of human tubercle bacillus. II. Isolation of arabinose mycolate and identification of its chemical structure
    • Azuma, I., and Y. Yamamoto. 1963. Studies on the firmly bound lipids of human tubercle bacillus. II. Isolation of arabinose mycolate and identification of its chemical structure. J. Biochem. (Tokyo) 53:274-281.
    • (1963) J. Biochem. (Tokyo) , vol.53 , pp. 274-281
    • Azuma, I.1    Yamamoto, Y.2
  • 13
    • 0031007903 scopus 로고    scopus 로고
    • Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis
    • Belisle, J. T., V. D. Vissa, T. Sievert, K. Takayama, P. J. Brennan, and G. S. Besra. 1997. Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 276:1420-1422.
    • (1997) Science , vol.276 , pp. 1420-1422
    • Belisle, J.T.1    Vissa, V.D.2    Sievert, T.3    Takayama, K.4    Brennan, P.J.5    Besra, G.S.6
  • 15
    • 0027981084 scopus 로고
    • Cloning, molecular characterization, and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: A dual lysis system of modular design
    • Birkeland, N. K. 1994. Cloning, molecular characterization, and expression of the genes encoding the lytic functions of lactococcal bacteriophage phi LC3: a dual lysis system of modular design. Can. J. Microbiol. 40:658-665.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 658-665
    • Birkeland, N.K.1
  • 16
    • 0017324326 scopus 로고
    • Control mechanism for fatty acid synthesis in Mycobacterium smegmatis
    • Bloch, K. 1977. Control mechanism for fatty acid synthesis in Mycobacterium smegmatis. Adv. Enzymol. 45:1-84.
    • (1977) Adv. Enzymol. , vol.45 , pp. 1-84
    • Bloch, K.1
  • 17
    • 0033819143 scopus 로고    scopus 로고
    • The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis
    • Braibant, M., P. Gilot, and J. Content. 2000. The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol. Rev. 24:449-467.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 449-467
    • Braibant, M.1    Gilot, P.2    Content, J.3
  • 18
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner, S. 1988. The molecular evolution of genes and proteins: a tale of two serines. Nature 334:528-530.
    • (1988) Nature , vol.334 , pp. 528-530
    • Brenner, S.1
  • 19
    • 12844267371 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention, Atlanta, Ga
    • Centers for Disease Control and Prevention. 2004. TB elimination: now is the time! Centers for Disease Control and Prevention, Atlanta, Ga.
    • (2004) TB Elimination: Now Is the Time!
  • 20
    • 0034623067 scopus 로고    scopus 로고
    • Identification and substrate specificity of β-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis
    • Choi, K. H., L. Kremer, G. S. Besra, and C. O. Rock. 2000. Identification and substrate specificity of β-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J. Biol. Chem. 275:28201-28207.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28201-28207
    • Choi, K.H.1    Kremer, L.2    Besra, G.S.3    Rock, C.O.4
  • 21
    • 0036299101 scopus 로고    scopus 로고
    • Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis
    • Cohen-Gonsaud, M., S. Ducasse, F. Hoh, D. Zerbib, G. Labesse, and A. Quemard. 2002. Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis. J. Mol. Biol. 320:249-261.
    • (2002) J. Mol. Biol. , vol.320 , pp. 249-261
    • Cohen-Gonsaud, M.1    Ducasse, S.2    Hoh, F.3    Zerbib, D.4    Labesse, G.5    Quemard, A.6
  • 22
    • 0035931926 scopus 로고    scopus 로고
    • Massive gene decay in the leprosy bacillus
    • Cole, S. T., K. Eiglmeier, J. Parkhill, et al. 2001. Massive gene decay in the leprosy bacillus. Nature 409:1007-1011.
    • (2001) Nature , vol.409 , pp. 1007-1011
    • Cole, S.T.1    Eiglmeier, K.2    Parkhill, J.3
  • 23
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S. T., R. Brosch, J. Parkhill, et al. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393:537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 24
    • 12844277090 scopus 로고    scopus 로고
    • A new class of phosphotransferases phosphorylated on an aspartate residue in an ammo-terminal DXDX(TTV) motif
    • Collet, J. F., V. Stroobant, M. Pirard, G. Delpierre, and E. van Schaftingen. 1998. A new class of phosphotransferases phosphorylated on an aspartate residue in an ammo-terminal DXDX(TTV) motif. J. Biol. Chem. 274:33985-33990.
    • (1998) J. Biol. Chem. , vol.274 , pp. 33985-33990
    • Collet, J.F.1    Stroobant, V.2    Pirard, M.3    Delpierre, G.4    Van Schaftingen, E.5
  • 25
    • 0023933734 scopus 로고
    • Derived amino acid sequence and identification of active site residues of Escherichia coli β-hydroxydecanoyl thioester dehydrase
    • Cronan, J. E., Jr., W. B. Li, R. Coleman, M. Narasimhan, D. de Mendoza, and J. M. Schwab. 1988. Derived amino acid sequence and identification of active site residues of Escherichia coli β-hydroxydecanoyl thioester dehydrase. J. Biol. Chem. 263:4641-4646.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4641-4646
    • Cronan Jr., J.E.1    Li, W.B.2    Coleman, R.3    Narasimhan, M.4    De Mendoza, D.5    Schwab, J.M.6
  • 26
    • 0027247941 scopus 로고
    • Biosynthesis of a novel 3-oxo-2-tetradecyloctadecanoate-containing phospholipid by a cell-free extract of Corynebacterium diphtheriae
    • Datta, A. K., and K. Takayama. 1993. Biosynthesis of a novel 3-oxo-2-tetradecyloctadecanoate-containing phospholipid by a cell-free extract of Corynebacterium diphtheriae. Biochim. Biophys. Acta 1169:135-145.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 135-145
    • Datta, A.K.1    Takayama, K.2
  • 27
    • 0018770510 scopus 로고
    • Isoniazid inhibition of the synthesis of monounsaturated long-chain fatty acids in Mycobacterium tuberculosis H37Ra
    • Davidson, L. A., and K. Takayama. 1979. Isoniazid inhibition of the synthesis of monounsaturated long-chain fatty acids in Mycobacterium tuberculosis H37Ra. Antimicrob. Agents Chemother. 16:104-105.
    • (1979) Antimicrob. Agents Chemother. , vol.16 , pp. 104-105
    • Davidson, L.A.1    Takayama, K.2
  • 28
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of in Mycobacterium tuberculosis
    • Dessen, A., A. Quemard, J. S. Blanchard, W. R. Jacobs, and J. C. Sacchettini. 1995. Crystal structure and function of the isoniazid target of in Mycobacterium tuberculosis. Science 267:1638-1641.
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 29
    • 0037470224 scopus 로고    scopus 로고
    • Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain deviod of methoxy- and ketomycolates
    • Dinadayala, P., F. Laval, C. Raynaud, A. Lemassu, M. A. Laneelle, G. Laneelle, and M. Daffe. 2003. Tracking the putative biosynthetic precursors of oxygenated mycolates of Mycobacterium tuberculosis. Structural analysis of fatty acids of a mutant strain deviod of methoxy- and ketomycolates. J. Biol. Chem. 278:7310-7319.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7310-7319
    • Dinadayala, P.1    Laval, F.2    Raynaud, C.3    Lemassu, A.4    Laneelle, M.A.5    Laneelle, G.6    Daffe, M.7
  • 30
    • 1942421808 scopus 로고    scopus 로고
    • Comparative cell wall core biosynthesis in mycolated pathogens, Mycobacterium tuberculosis and Corynebacterium diphtheriae
    • Dover, L. B., A. M. Cerdeno-Tarraga, M. J. Pallen, J. Parkhill, and G. S. Besra. 2004. Comparative cell wall core biosynthesis in mycolated pathogens, Mycobacterium tuberculosis and Corynebacterium diphtheriae. FEMS Microbiol. Rev. 28:225-250.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 225-250
    • Dover, L.B.1    Cerdeno-Tarraga, A.M.2    Pallen, M.J.3    Parkhill, J.4    Besra, G.S.5
  • 33
    • 2542483729 scopus 로고    scopus 로고
    • Cloning and expression of the trehalose-phosphate phosphatase of Mycobacterium tuberculosis: Comparison to the enzyme from Mycobacterium smegmatis
    • Edavana, V. K., I. Pastuszak, J. D. Carroll, P. Thampi, E. C. Abraham, and A. D. Elbein. 2004. Cloning and expression of the trehalose-phosphate phosphatase of Mycobacterium tuberculosis: comparison to the enzyme from Mycobacterium smegmatis. Arch. Biochem. Biophys. 426:250-257.
    • (2004) Arch. Biochem. Biophys. , vol.426 , pp. 250-257
    • Edavana, V.K.1    Pastuszak, I.2    Carroll, J.D.3    Thampi, P.4    Abraham, E.C.5    Elbein, A.D.6
  • 34
    • 4243478408 scopus 로고
    • Biosyntheses de l'acide α-smegmamycolique
    • Etemadi, A. H., and E. Lederer. 1965. Biosyntheses de l'acide α-smegmamycolique. Biochim. Biophys. Acta 98:160-167.
    • (1965) Biochim. Biophys. Acta , vol.98 , pp. 160-167
    • Etemadi, A.H.1    Lederer, E.2
  • 35
    • 0013798316 scopus 로고
    • Sur la structure des acides α-mycoliques de la souche humaine test de Mycobacterium tuberculosis
    • Etemadi, A. H., and E. Lederer. 1965. Sur la structure des acides α-mycoliques de la souche humaine Test de Mycobacterium tuberculosis. Bull. Soc. Chem. Fr. 1965:2640-2645.
    • (1965) Bull. Soc. Chem. Fr. , vol.1965 , pp. 2640-2645
    • Etemadi, A.H.1    Lederer, E.2
  • 36
    • 7244242397 scopus 로고    scopus 로고
    • Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis
    • 35a. Gande, R., K. J. Gibson, A. K. Brown, K. Krumbach, L. G. Dover, H. Sahm, S. Shioyama, T. Oikawa, G. S. Besra, and L. Eggeling. 2004. Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis. J. Biol. Chem. 279:44847-44857.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44847-44857
    • Gande, R.1    Gibson, K.J.2    Brown, A.K.3    Krumbach, K.4    Dover, L.G.5    Sahm, H.6    Shioyama, S.7    Oikawa, T.8    Besra, G.S.9    Eggeling, L.10
  • 37
    • 0141677776 scopus 로고    scopus 로고
    • Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: Implications for therapy
    • Gao, L. Y., F. Laval, E. H. Lawson, R. K. Groger, A. Woodruff, J. H. Morisaki, J. S. Cox, M. Daffe, and E. J. Brown. 2003. Requirement for kasB in Mycobacterium mycolic acid biosynthesis, cell wall impermeability and intracellular survival: implications for therapy. Mol. Microbiol. 49:1547-1563.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1547-1563
    • Gao, L.Y.1    Laval, F.2    Lawson, E.H.3    Groger, R.K.4    Woodruff, A.5    Morisaki, J.H.6    Cox, J.S.7    Daffe, M.8    Brown, E.J.9
  • 38
    • 0001193861 scopus 로고
    • Biosynthesis of corynomycolic acid from two molecules of palmitic acid
    • Gastambide-Odier, M., and E. Lederer. 1959. Biosynthesis of corynomycolic acid from two molecules of palmitic acid. Nature 184:1563-1564.
    • (1959) Nature , vol.184 , pp. 1563-1564
    • Gastambide-Odier, M.1    Lederer, E.2
  • 39
    • 0017503852 scopus 로고
    • Structure of mycobacterial cis-cyclopropane mycolates by mass spectrometry
    • Gensler, W. J., and J. P. Marshall. 1977. Structure of mycobacterial cis-cyclopropane mycolates by mass spectrometry. Chem. Phys. Lipids 19:128-143.
    • (1977) Chem. Phys. Lipids , vol.19 , pp. 128-143
    • Gensler, W.J.1    Marshall, J.P.2
  • 40
    • 0028972283 scopus 로고
    • The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2
    • George, K. M., Y. Yuan, D. R. Sherman, C. E. Barry III. 1995. The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. J. Biol. Chem. 270: 27292-27298.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27292-27298
    • George, K.M.1    Yuan, Y.2    Sherman, D.R.3    Barry III, C.E.4
  • 41
    • 0037424531 scopus 로고    scopus 로고
    • The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the α-mycolic acid
    • Glickman, M. S. 2003. The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the α-mycolic acid. J. Biol. Chem. 278:7844-7849.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7844-7849
    • Glickman, M.S.1
  • 42
    • 0033634971 scopus 로고    scopus 로고
    • A novel mycolic acid cyclopropane synthetase is required for coding persistence, and virulence of Mycobacterium tuberculosis
    • Glickman, M. S., J. S. Cox, and W. R. Jacobs, Jr. 2000. A novel mycolic acid cyclopropane synthetase is required for coding persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 5:717-727.
    • (2000) Mol. Cell , vol.5 , pp. 717-727
    • Glickman, M.S.1    Cox, J.S.2    Jacobs Jr., W.R.3
  • 43
    • 0035910583 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase
    • Glickman, M. S., S. M. Cahill, and W. R. Jacobs, Jr. 2001. The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase. J. Biol. Chem. 276:2228-2233.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2228-2233
    • Glickman, M.S.1    Cahill, S.M.2    Jacobs Jr., W.R.3
  • 44
    • 0016662064 scopus 로고
    • Mesosomes: Membraneous bacterial organelles
    • Greenawalt, J. W., and T. L. Whiteside. 1975. Mesosomes: membraneous bacterial organelles. Bacteriol. Rev. 30:405-463.
    • (1975) Bacteriol. Rev. , vol.30 , pp. 405-463
    • Greenawalt, J.W.1    Whiteside, T.L.2
  • 45
    • 0029926496 scopus 로고    scopus 로고
    • Roles of the FabA and FabZ β-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis
    • Heath, R. J., and C. O. Rock. 1996. Roles of the FabA and FabZ β-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis. J. Biol. Chem. 271:27795-27801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27795-27801
    • Heath, R.J.1    Rock, C.O.2
  • 46
    • 0032982736 scopus 로고    scopus 로고
    • Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope
    • Jackson, M., C. Raynaud, M. A. Laneelle, C. Guilhot, C. Laurent-Winter, D. Ensergueix, B. Gicquel, and M. Daffe. 1999. Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope. Mol. Microbiol. 31: 1573-1587.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1573-1587
    • Jackson, M.1    Raynaud, C.2    Laneelle, M.A.3    Guilhot, C.4    Laurent-Winter, C.5    Ensergueix, D.6    Gicquel, B.7    Daffe, M.8
  • 48
    • 0020455141 scopus 로고
    • Synthesis of trehalose dimycolate (cord factor) by a cell-free system of Mycobacterium smegmatis
    • Kilburn, J. O., K. Takayama, and E. L. Armstrong. 1982. Synthesis of trehalose dimycolate (cord factor) by a cell-free system of Mycobacterium smegmatis. Biochem. Biophys. Res. Commun. 108:132-139.
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 132-139
    • Kilburn, J.O.1    Takayama, K.2    Armstrong, E.L.3
  • 49
    • 0037073685 scopus 로고    scopus 로고
    • Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin
    • Kim, B. S., T. A. Cropp, B. J. Beck, D. H. Sherman, and K. A. Reynolds. 2002. Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin. J. Biol. Chem. 277:48028-48034.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48028-48034
    • Kim, B.S.1    Cropp, T.A.2    Beck, B.J.3    Sherman, D.H.4    Reynolds, K.A.5
  • 51
    • 0000255856 scopus 로고    scopus 로고
    • Genetics of mycolic acid biosynthesis
    • G. F. Hatfull and W. R. Jacobs, Jr. (ed.) . ASM Press, Washington, D.C.
    • Kremer, L., A. R. Baulard, and G. S. Besra. 2000. Genetics of mycolic acid biosynthesis, p. 173-190. In G. F. Hatfull and W. R. Jacobs, Jr. (ed.), Molecular genetics of mycobacteria. ASM Press, Washington, D.C.
    • (2000) Molecular Genetics of Mycobacteria , pp. 173-190
    • Kremer, L.1    Baulard, A.R.2    Besra, G.S.3
  • 52
    • 0035958944 scopus 로고    scopus 로고
    • Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (intFabD), two major components of Mycobacterium tuberculosis fatty acid synthetase II
    • Kremer, L., K. M. Nampoothiri, S. Lesjean, L. G. Dover, S. Graham, J. Betts, P. J. Brennan, D. E. Minnikin, C. Locht, and G. S. Besra. 2001. Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (intFabD), two major components of Mycobacterium tuberculosis fatty acid synthetase II. J. Biol. Chem. 276:27967-27974.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27967-27974
    • Kremer, L.1    Nampoothiri, K.M.2    Lesjean, S.3    Dover, L.G.4    Graham, S.5    Betts, J.6    Brennan, P.J.7    Minnikin, D.E.8    Locht, C.9    Besra, G.S.10
  • 55
    • 12844280992 scopus 로고
    • C-methylation in biological systems
    • Lederer, E. 1965. C-methylation in biological systems. Israel J. Med. Sci. 1: 1129-1147.
    • (1965) Israel J. Med. Sci. , vol.1 , pp. 1129-1147
    • Lederer, E.1
  • 56
    • 0004754193 scopus 로고
    • Chemistry of mycobacterial cord factor and related natural and synthetic trehalose esters
    • G. P. Kubica and L. G. Wayne (ed.) . Marcel Dekker, Inc., New York, N.Y.
    • Lederer, E. 1984. Chemistry of mycobacterial cord factor and related natural and synthetic trehalose esters, p. 361-378. In G. P. Kubica and L. G. Wayne (ed.), The mycobacteria, a sourcebook, part A. Marcel Dekker, Inc., New York, N.Y.
    • (1984) The Mycobacteria, a Sourcebook, Part A , pp. 361-378
    • Lederer, E.1
  • 57
    • 0016864934 scopus 로고
    • Cell walls of mycobacteria and related organisms: Chemistry and immunological stimulant properties
    • Lederer, E., A. Adam, R. Clorbaru, J.-F. Petit, and J. Wietzerbin. 1975. Cell walls of mycobacteria and related organisms: chemistry and immunological stimulant properties. Mol. Cell Biochem. 7:87-104.
    • (1975) Mol. Cell Biochem. , vol.7 , pp. 87-104
    • Lederer, E.1    Adam, A.2    Clorbaru, R.3    Petit, J.-F.4    Wietzerbin, J.5
  • 58
    • 2142710129 scopus 로고    scopus 로고
    • Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis
    • Linne, U., D. Schwarzer, G. N. Schroeder, and M. A. Marahiel. 2004. Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis. Eur. J. Biochem. 271:1536-1545.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1536-1545
    • Linne, U.1    Schwarzer, D.2    Schroeder, G.N.3    Marahiel, M.A.4
  • 59
    • 1242341327 scopus 로고    scopus 로고
    • Macro-array and bioinformatic analyses reveal mycobacterial 'core' genes, variation in the ESAT-6 gene family and new phylogenetic markers for the Mycobacterium tuberculosis complex
    • Marmiesse, M., P. Brodin, C. Buchrieser, C. Gutierrez, N. Simoes, V. Vincent, P. Glaser, S. T. Cole, and R. Brosch. 2004. Macro-array and bioinformatic analyses reveal mycobacterial 'core' genes, variation in the ESAT-6 gene family and new phylogenetic markers for the Mycobacterium tuberculosis complex. Microbiology 150:483-496.
    • (2004) Microbiology , vol.150 , pp. 483-496
    • Marmiesse, M.1    Brodin, P.2    Buchrieser, C.3    Gutierrez, C.4    Simoes, N.5    Vincent, V.6    Glaser, P.7    Cole, S.T.8    Brosch, R.9
  • 60
    • 0033962136 scopus 로고    scopus 로고
    • InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
    • Marrakchi, H., G. Laneelle, and A. Quemard. 2000. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 146:289-296.
    • (2000) Microbiology , vol.146 , pp. 289-296
    • Marrakchi, H.1    Laneelle, G.2    Quemard, A.3
  • 61
    • 0037160079 scopus 로고    scopus 로고
    • A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae
    • Marrakchi, H., K. H. Choi, and C. O. Rock. 2002. A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae. J. Biol. Chem. 277:44809-44816.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44809-44816
    • Marrakchi, H.1    Choi, K.H.2    Rock, C.O.3
  • 63
    • 0015123122 scopus 로고
    • Utilization of palmitic acid by Mycobacterium avium
    • McCarthy, C. 1971. Utilization of palmitic acid by Mycobacterium avium. Infect. Immun. 4:199-204.)
    • (1971) Infect. Immun. , vol.4 , pp. 199-204
    • McCarthy, C.1
  • 64
    • 0025815311 scopus 로고
    • Location of the mycolyl ester substituent in the cell walls of mycobacteria
    • McNeil, M., M. Daffe, and P. J. Brennan. 1991. Location of the mycolyl ester substituent in the cell walls of mycobacteria. J. Biol. Chem. 266: 13217-13223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13217-13223
    • McNeil, M.1    Daffe, M.2    Brennan, P.J.3
  • 66
    • 0002259015 scopus 로고
    • Lipids: Complex lipids, their chemistry, biosynthesis and roles
    • C. Ratledge and J. Stanford (ed.) . Academic Press, New York, N.Y.
    • Minnikin, D. E. 1982. Lipids: complex lipids, their chemistry, biosynthesis and roles, p. 95-184. In C. Ratledge and J. Stanford (ed.), The biology of the mycobacteria, vol. 1. Physiology, identification and classification. Academic Press, New York, N.Y.
    • (1982) The Biology of the Mycobacteria, Vol. 1. Physiology, Identification and Classification , vol.1 , pp. 95-184
    • Minnikin, D.E.1
  • 67
    • 37049133945 scopus 로고
    • Structural studies on the mycolic acids
    • Minnikin, D. E., and N. Polgar. 1967. Structural studies on the mycolic acids. Chem. Commun. 1967:312-314.
    • (1967) Chem. Commun. , vol.1967 , pp. 312-314
    • Minnikin, D.E.1    Polgar, N.2
  • 68
    • 0000900934 scopus 로고
    • The methoxymycolic and ketomycolic acids from human tubercle bacilli
    • Minnikin, D. E., and N. Polgar. 1967. The methoxymycolic and ketomycolic acids from human tubercle bacilli. Chem. Commun. 1967:1172-1174.
    • (1967) Chem. Commun. , vol.1967 , pp. 1172-1174
    • Minnikin, D.E.1    Polgar, N.2
  • 69
    • 37049119478 scopus 로고
    • The mycolic acids from the human and avium tubercle bacilli
    • Minnikin, D. E., and N. Polgar. 1967. The mycolic acids from the human and avium tubercle bacilli. Chem. Commun. 1967:916-918.
    • (1967) Chem. Commun. , vol.1967 , pp. 916-918
    • Minnikin, D.E.1    Polgar, N.2
  • 70
    • 0016227602 scopus 로고
    • Structure and immunological properties of D-arabino-D-galactan isolated from Mycobacterium species
    • Misaki, A., N. Seto, and I. Azuma. 1974. Structure and immunological properties of D-arabino-D-galactan isolated from Mycobacterium species. J. Biochem. (Tokyo) 76:15-27.
    • (1974) J. Biochem. (Tokyo) , vol.76 , pp. 15-27
    • Misaki, A.1    Seto, N.2    Azuma, I.3
  • 71
    • 0032528950 scopus 로고    scopus 로고
    • The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate side chains for catalysis
    • Modis, Y., S. A. Filppula, D. K. Novikov, B. Norledge, J. K. Hiltunen, and R. K. Wierenga. 1998. The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate side chains for catalysis. Structure 6:957-970.
    • (1998) Structure , vol.6 , pp. 957-970
    • Modis, Y.1    Filppula, S.A.2    Novikov, D.K.3    Norledge, B.4    Hiltunen, J.K.5    Wierenga, R.K.6
  • 72
    • 0028584330 scopus 로고
    • An Eschenchia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to FabA and suppression of mutations in lipid A biosynthesis
    • Mohan, S., T. M. Kelly, S. S. Eveland, C. R. Raetz, and M. S. Anderson. 1994. An Eschenchia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to FabA and suppression of mutations in lipid A biosynthesis. J. Biol. Chem. 269:32896-32903.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32896-32903
    • Mohan, S.1    Kelly, T.M.2    Eveland, S.S.3    Raetz, C.R.4    Anderson, M.S.5
  • 73
    • 12844256899 scopus 로고
    • Studies on the chemistry of the cord factor of Mycobacterium tuberculosis
    • Noll, H., and H. Bloch. 1955. Studies on the chemistry of the cord factor of Mycobacterium tuberculosis. J. Biol. Chem. 224:149-163.
    • (1955) J. Biol. Chem. , vol.224 , pp. 149-163
    • Noll, H.1    Bloch, H.2
  • 74
    • 0001468560 scopus 로고
    • The chemical structure of the cord factor of Mycobacterium tuberculosis
    • Noll, H., J. Asselineau, and E. Lederer. 1956. The chemical structure of the cord factor of Mycobacterium tuberculosis. Biochim. Biophys. Acta 20:299-309.
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 299-309
    • Noll, H.1    Asselineau, J.2    Lederer, E.3
  • 75
    • 1842428465 scopus 로고    scopus 로고
    • Mycobacterial polyketide-associated proteins are acyltransferases: Proof of principle with Mycobacterium tuberculosis PapAS
    • Onwueme, K. C., J. A. Ferreras, J. Buglino, C. D. Lima, and L. E. N. Quadri. 2004. Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapAS. Proc. Natl. Acad. Sci. USA 101:4608-4613.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4608-4613
    • Onwueme, K.C.1    Ferreras, J.A.2    Buglino, J.3    Lima, C.D.4    Quadri, L.E.N.5
  • 77
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • Portevin, D., C. de Sousa-D'Auria, C. Houssin, C. Grimaldi, M. Chami, M. Daffe, and C. Guilhot. 2004. A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms. Proc. Natl. Acad. Sci. USA 101:314-319.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3    Grimaldi, C.4    Chami, M.5    Daffe, M.6    Guilhot, C.7
  • 78
    • 0036090968 scopus 로고    scopus 로고
    • Evidence for a partial redundancy of the fibronectin-binding proteins for transfer of mycoloyl residues onto the cell wall arabinogalactan termini of Mycobacterium tuberculosis
    • Puech, V., C. Guilhot, E. Perez, M. Tropis, L. Y. Armitige, B. Glcquel, and M. Daffe. 2002. Evidence for a partial redundancy of the fibronectin-binding proteins for transfer of mycoloyl residues onto the cell wall arabinogalactan termini of Mycobacterium tuberculosis. Mol. Microbiol. 44:1109-1122.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1109-1122
    • Puech, V.1    Guilhot, C.2    Perez, E.3    Tropis, M.4    Armitige, L.Y.5    Glcquel, B.6    Daffe, M.7
  • 79
    • 0034145295 scopus 로고    scopus 로고
    • Characterization of the in vivo acceptors of the mycoloyl residues transferred by the corynebacterial PS1 and the related mycobacterial antigen 85
    • Puech, V., N. Bayan, K. Salim, G. Leblon, and M. Daffe. 2000. Characterization of the in vivo acceptors of the mycoloyl residues transferred by the corynebacterial PS1 and the related mycobacterial antigen 85. Mol. Microbiol. 35:1026-1041.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1026-1041
    • Puech, V.1    Bayan, N.2    Salim, K.3    Leblon, G.4    Daffe, M.5
  • 82
    • 12844274205 scopus 로고
    • 58) from Mycobacterium tuberculosis H37Ra by high performance liquid chromatography
    • 58) from Mycobacterium tuberculosis H37Ra by high performance liquid chromatography. J. Liquid Chromatog. 4:1207-1218.
    • (1981) J. Liquid Chromatog. , vol.4 , pp. 1207-1218
    • Qureshi, N.1    Takayama, K.2    Schnoes, H.K.3
  • 83
    • 0018102546 scopus 로고
    • Characterization of the purified components of a homologous series of α-mycolic acids from Mycobacterium tuberculosis H37Ra
    • Qureshi, N., K. Takayama, H. C. Jordi, and H. K. Schnoes. 1978. Characterization of the purified components of a homologous series of α-mycolic acids from Mycobacterium tuberculosis H37Ra. J. Biol. Chem. 253:5411-5417.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5411-5417
    • Qureshi, N.1    Takayama, K.2    Jordi, H.C.3    Schnoes, H.K.4
  • 85
    • 0042818111 scopus 로고    scopus 로고
    • The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities
    • Reuter, G., T. Janvilisri, H. Venter, S. Shahi, L. Balakrishnan, and H. W. van Veen. 2003. The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities. J. Biol. Chem. 278:35193-35198.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35193-35198
    • Reuter, G.1    Janvilisri, T.2    Venter, H.3    Shahi, S.4    Balakrishnan, L.5    Van Veen, H.W.6
  • 86
    • 77957038779 scopus 로고
    • Regulation of bacterial membrane synthesis
    • Rock, C. O., and J. E. Cronan, Jr. 1982. Regulation of bacterial membrane synthesis. Curr. Top. Membr. Transp. 17:209-233.
    • (1982) Curr. Top. Membr. Transp. , vol.17 , pp. 209-233
    • Rock, C.O.1    Cronan Jr., J.E.2
  • 87
    • 0033960935 scopus 로고    scopus 로고
    • Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines
    • Ronning, D. R., T. Klabunde, G. S. Besra, V. D. Vissa, J. T. Belisle, and J. C. Sacchettini. 2000. Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nat. Struct. Biol. 7:141-146.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 141-146
    • Ronning, D.R.1    Klabunde, T.2    Besra, G.S.3    Vissa, V.D.4    Belisle, J.T.5    Sacchettini, J.C.6
  • 88
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high-density mutagenesis
    • Sassetti, C. M., D. H. Boyd, and E. J. Rubin. 2002. Genes required for mycobacterial growth defined by high-density mutagenesis. Mol. Microbiol. 48:77-84.
    • (2002) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 89
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti, C. M., and E. J. Rubin. 2003. Genetic requirements for mycobacterial survival during infection. Proc. Natl. Acad. Sci. USA 100:12989-12994.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 90
    • 0023645726 scopus 로고
    • Purification and characterization of a novel mycolic acid exchange enzyme from Mycobacterium smegmatis
    • Sathyamoorthy, N., and K. Takayama. 1987. Purification and characterization of a novel mycolic acid exchange enzyme from Mycobacterium smegmatis. J. Biol. Chem. 262:13417-13423.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13417-13423
    • Sathyamoorthy, N.1    Takayama, K.2
  • 91
    • 0035827542 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III
    • Scardale, J. N., G. Kazanina, X. He, K. A. Reynolds, and H. T. Wright. 2001. Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III. J. Biol. Chem. 276:20516-20522.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20516-20522
    • Scardale, J.N.1    Kazanina, G.2    He, X.3    Reynolds, K.A.4    Wright, H.T.5
  • 92
    • 0035861550 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB
    • Schaeffer, M. L., G. Agnihotri, C. Volker, H. Kallender, P. J. Brennan, and J. T. Lonsdale. 2001. Purification and biochemical characterization of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthases KasA and KasB. J. Biol. Chem. 276:47029-47037.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47029-47037
    • Schaeffer, M.L.1    Agnihotri, G.2    Volker, C.3    Kallender, H.4    Brennan, P.J.5    Lonsdale, J.T.6
  • 93
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer, D., H. D. Mootz, U. Linne, and M. A. Marahiel. 2002. Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl. Acad. Sci. USA 99:14083-14088.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14083-14088
    • Schwarzer, D.1    Mootz, H.D.2    Linne, U.3    Marahiel, M.A.4
  • 94
    • 0034663370 scopus 로고    scopus 로고
    • Essential role of trehalose in the synthesis and subsequent metabolism of corynomycolic acid in Corynebacterium matruchotii
    • Shimakata, T., and Y. Minatogawa. 2000. Essential role of trehalose in the synthesis and subsequent metabolism of corynomycolic acid in Corynebacterium matruchotii. Arch. Biochem. Biophys. 380:331-338.
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 331-338
    • Shimakata, T.1    Minatogawa, Y.2
  • 95
    • 0036448224 scopus 로고    scopus 로고
    • The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
    • Slayden, R. A., and C. E. Barry III. 2002. The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis. Tuberculosis 82:149-160.
    • (2002) Tuberculosis , vol.82 , pp. 149-160
    • Slayden, R.A.1    Barry III, C.E.2
  • 96
    • 0034682618 scopus 로고    scopus 로고
    • MDP-1, a novel eukaryotic magnesium-dependent phosphatase
    • Slengut, J. D., and R. R. Levine. 2000. MDP-1, a novel eukaryotic magnesium-dependent phosphatase. Biochemistry 39:8315-8324.
    • (2000) Biochemistry , vol.39 , pp. 8315-8324
    • Slengut, J.D.1    Levine, R.R.2
  • 97
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • Smith, S., A. Witkowski, and A. K. Joshi. 2003. Structural and functional organization of the animal fatty acid synthase. Prog. Lipid Res. 42:289-317.
    • (2003) Prog. Lipid Res. , vol.42 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 98
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • Stauton, J., and K. J. Weissman. 2001. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18:380-416.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Stauton, J.1    Weissman, K.J.2
  • 100
    • 0346252661 scopus 로고    scopus 로고
    • Visualization and interpretation of protein networks in Mycobacterium tuberculosis based on hierarchical clustering of genome-wide functional linkage maps
    • Strong, M., T. G. Graeber, M. Beeby, M. Pellegrini, M. J. Thompson, T. O. Yeates, and D. Eisenberg. 2003. Visualization and interpretation of protein networks in Mycobacterium tuberculosis based on hierarchical clustering of genome-wide functional linkage maps. Nucleic Acids Res. 31:7099-7109.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 7099-7109
    • Strong, M.1    Graeber, T.G.2    Beeby, M.3    Pellegrini, M.4    Thompson, M.J.5    Yeates, T.O.6    Eisenberg, D.7
  • 101
    • 0000355908 scopus 로고
    • Structure and synthesis of lipids
    • G. P. Kubica and L. G. Wayne (ed.) . Marcel Dekker, Inc., New York, N.Y.
    • Takayama, K., and N. Qureshi. 1984. Structure and synthesis of lipids, p. 315-344. In G. P. Kubica and L. G. Wayne (ed.), The mycobacteria, a sourcebook, part A. Marcel Dekker, Inc., New York, N.Y.
    • (1984) The Mycobacteria, a Sourcebook, Part A , pp. 315-344
    • Takayama, K.1    Qureshi, N.2
  • 102
    • 0016529811 scopus 로고
    • Site of inhibitory action of isoniazid in the synthesis of mycolic acid in Mycobacterium tuberculosis
    • Takayama, K., H. K. Schnoes, E. L. Armstrong, and R. W. Boyle. 1975. Site of inhibitory action of isoniazid in the synthesis of mycolic acid in Mycobacterium tuberculosis. J. Lipid Res. 16:308-317.
    • (1975) J. Lipid Res. , vol.16 , pp. 308-317
    • Takayama, K.1    Schnoes, H.K.2    Armstrong, E.L.3    Boyle, R.W.4
  • 103
    • 0018114380 scopus 로고
    • Isolation and characterization of the monounsaturated long chain fatty acids of Mycobacterium tuberculosis
    • Takayama, K., N. Qureshi, and H. K. Schnoes. 1978. Isolation and characterization of the monounsaturated long chain fatty acids of Mycobacterium tuberculosis. Lipids 13:575-579.
    • (1978) Lipids , vol.13 , pp. 575-579
    • Takayama, K.1    Qureshi, N.2    Schnoes, H.K.3
  • 104
    • 3543012692 scopus 로고
    • 47 fatty acids from Mycobacterium tuberculosis H37Ra as their p-bromophenacyl esters by high performance liquid chromatography
    • G. L. Hawk (ed.). Chromatographic science series . Marcel Dekker, Inc., New York, N.Y.
    • 47 fatty acids from Mycobacterium tuberculosis H37Ra as their p-bromophenacyl esters by high performance liquid chromatography, p. 375-394. In G. L. Hawk (ed.), Biological/biomedical applications of liquid chromatography II. Chromatographic science series, vol. 12. Marcel Dekker, Inc., New York, N.Y.
    • (1979) Biological/biomedical Applications of Liquid Chromatography II , vol.12 , pp. 375-394
    • Takayama, K.1    Qureshi, N.2    Jordi, H.C.3    Schnoes, H.K.4
  • 106
    • 0031820043 scopus 로고    scopus 로고
    • Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily
    • Thaller, M. C., S. Schippa, and G. M. Rossolini. 1998. Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily. Protein Sci. 7:1647-1652.
    • (1998) Protein Sci. , vol.7 , pp. 1647-1652
    • Thaller, M.C.1    Schippa, S.2    Rossolini, G.M.3
  • 107
    • 0027968068 scopus 로고    scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specifc gap penalties and weight matrix choice
    • Thomson, J. D., D. G. Higgins, and T. J. Gibson. 1997. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specifc gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1997) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thomson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 108
    • 1842577641 scopus 로고    scopus 로고
    • Enzymatic activation and transfer of fatty acids as acyladenylates in mycobacteria
    • Trivedi, O. A., P. Arora, V. Sridharan, R. Tickoo, D. Mohanty, and R. S. Gokhale. 2004. Enzymatic activation and transfer of fatty acids as acyladenylates in mycobacteria. Nature 428:441-445.
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 109
    • 0038487321 scopus 로고    scopus 로고
    • Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: Inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition
    • Tzvetkov, M., C. Klopprogge, O. Zelder, and W. Liebl. 2003. Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition. Microbiology 149:1659-1673.
    • (2003) Microbiology , vol.149 , pp. 1659-1673
    • Tzvetkov, M.1    Klopprogge, C.2    Zelder, O.3    Liebl, W.4
  • 110
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • van Helvoort, A., A. J. Smith, H. Sprong, I. Fritzsche, A. H. Schinkel, P. Borst, and G. van Meer. 1996. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87:507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Helvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Van Meer, G.7
  • 111
    • 0031034056 scopus 로고    scopus 로고
    • 6-NBD-sphingomyelin is translocated across the plasma membrane by a multidrug transporter activity
    • 6-NBD-sphingomyelin is translocated across the plasma membrane by a multidrug transporter activity. J. Cell Sci. 110:75-83.
    • (1997) J. Cell Sci. , vol.110 , pp. 75-83
    • Helvoort, A.1    Giudici, M.L.2    Thielemans, M.3    Van Meer, G.4
  • 112
    • 0038410325 scopus 로고    scopus 로고
    • Inactivation of the inhA -encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis
    • Vilcheze, C., H. R. Moribidoni, T. R. Weisbrod, H. Iwamoto, M. Kuo, J. C. Sacchettini, and W. R. Jacobs, Jr. 2000. Inactivation of the inhA -encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182:4059-4067.
    • (2000) J. Bacteriol. , vol.182 , pp. 4059-4067
    • Vilcheze, C.1    Moribidoni, H.R.2    Weisbrod, T.R.3    Iwamoto, H.4    Kuo, M.5    Sacchettini, J.C.6    Jacobs Jr., W.R.7
  • 113
    • 0015893808 scopus 로고
    • 32 β-keto ester from palmitic acid in a cell-free system of Corynebacterium diphtheriae
    • 32 β-keto ester from palmitic acid in a cell-free system of Corynebacterium diphtheriae. Biochim. Biophys. Acta 326:52-62.
    • (1973) Biochim. Biophys. Acta , vol.326 , pp. 52-62
    • Walker, R.W.1    Prome, J.C.2    Lacave, C.S.3
  • 114
    • 0035987344 scopus 로고    scopus 로고
    • Location of functional groups in mycobacterial meromycolate chains; the recognition of new structural principles in mycolic acids
    • Watanabe, M., Y. Aoyagi, H. Mitome, T. Fujita, H. Naoki, M. Ridell, and D. E. Minnikin. 2002. Location of functional groups in mycobacterial meromycolate chains; the recognition of new structural principles in mycolic acids. Microbiology 148:1881-1902.
    • (2002) Microbiology , vol.148 , pp. 1881-1902
    • Watanabe, M.1    Aoyagi, Y.2    Mitome, H.3    Fujita, T.4    Naoki, H.5    Ridell, M.6    Minnikin, D.E.7
  • 115
    • 0015392912 scopus 로고
    • Relationship between oleic acid uptake and lipid metabolism in Mycobacterium smegmatis
    • Weir, M. P., W. H. R. Langridge, and R. W. Walker. 1972. Relationship between oleic acid uptake and lipid metabolism in Mycobacterium smegmatis. Am. Rev. Respir. Dis. 106:450-457.
    • (1972) Am. Rev. Respir. Dis. , vol.106 , pp. 450-457
    • Weir, M.P.1    Langridge, W.H.R.2    Walker, R.W.3
  • 116
    • 0346996696 scopus 로고    scopus 로고
    • The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic α/β hydrolases
    • Wilson, R. A., W. N. Maughan, L. Kremer, G. S. Besra, and K. Futterer. 2004. The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic α/β hydrolases. J. Mol. Biol. 335:519-530.
    • (2004) J. Mol. Biol. , vol.335 , pp. 519-530
    • Wilson, R.A.1    Maughan, W.N.2    Kremer, L.3    Besra, G.S.4    Futterer, K.5
  • 117
    • 0000143137 scopus 로고
    • Mode of action of the antimycobacterial agents and associated aspects of the molecular biology of the mycobactria
    • C. Ratledge and J. Stanford (ed.). Academic Press, New York, N.Y.
    • Winder, F. G. 1982. Mode of action of the antimycobacterial agents and associated aspects of the molecular biology of the mycobactria, p. 353-438. In C. Ratledge and J. Stanford (ed.), The biology of the mycobacteria, vol. 1. Physiology, identification and classification. Academic Press, New York, N.Y.
    • (1982) The Biology of the Mycobacteria, Vol. 1. Physiology, Identification and Classification , vol.1 , pp. 353-438
    • Winder, F.G.1
  • 118
    • 0041528533 scopus 로고    scopus 로고
    • Three pathways for trehalose metabolism in Corynebacterium glutamicum ATCC13032 and their significance in response to osmotic stress
    • Wolf, A., R. Kramer, and S. Morbach. 2003. Three pathways for trehalose metabolism in Corynebacterium glutamicum ATCC13032 and their significance in response to osmotic stress. Mol. Microbiol. 49:1119-1134.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1119-1134
    • Wolf, A.1    Kramer, R.2    Morbach, S.3
  • 119
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong, H. C., G. Liu, Y. M. Zhang, C. O. Rock, C. O., and J. Zheng. 2002. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277:15874-15880.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.M.3    Rock, C.O.4    Zheng, J.5
  • 121
    • 0029803546 scopus 로고    scopus 로고
    • A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Proc
    • Yuan, Y., and C. E. Barry III. 1996. A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 93:12828-12833.
    • (1996) Natl. Acad. Sci. USA , vol.93 , pp. 12828-12833
    • Yuan, Y.1    Barry III, C.E.2
  • 122
    • 0032516871 scopus 로고    scopus 로고
    • The biosynthesis of mycolic acids in Mycobacterium tuberculosis. Enzymatic methyl(ene) transfer to acyl carrier protein bound meromycolic acid in vitro
    • Yuan, Y., D. Mead, B. G. Schroeder, Y. Zhu, and C. E. Barry III. 1998. The biosynthesis of mycolic acids in Mycobacterium tuberculosis. Enzymatic methyl(ene) transfer to acyl carrier protein bound meromycolic acid in vitro. J. Biol. Chem. 273:21282-21290.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21282-21290
    • Yuan, Y.1    Mead, D.2    Schroeder, B.G.3    Zhu, Y.4    Barry III, C.E.5
  • 123
    • 0031001270 scopus 로고    scopus 로고
    • MMAS-1 the branch point between cis- And trans-cyclopropane containing oxygenated mycolates in Mycobacterium tuberculosis
    • Yuan, Y., D. C. Crane, J. M. Musser, S. Sreevatsan, and C. E. Barry, III. 1997. MMAS-1 the branch point between cis- and trans-cyclopropane containing oxygenated mycolates in Mycobacterium tuberculosis. J. Biol. Chem. 272:10041-10048.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10041-10048
    • Yuan, Y.1    Crane, D.C.2    Musser, J.M.3    Sreevatsan, S.4    Barry III, C.E.5
  • 124
    • 0029048109 scopus 로고
    • Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis
    • Yuan, Y., R. E. Lee, G. S. Besra, J. T. Belisle, and C. E. Barry III. 1995. Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 92: 6630-6634.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6630-6634
    • Yuan, Y.1    Lee, R.E.2    Besra, G.S.3    Belisle, J.T.4    Barry III, C.E.5
  • 125
    • 0031694056 scopus 로고    scopus 로고
    • The effect of oxygenated mycolic acid composition on cell wall function and macrophage growth in Mycobacterium tuberculosis
    • Yuan, Y., Y. Zhu, D. D. Crane, and C. E. Barry III. 1998. The effect of oxygenated mycolic acid composition on cell wall function and macrophage growth in Mycobacterium tuberculosis. Mol. Microbiol. 29:1449-1458.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1449-1458
    • Yuan, Y.1    Zhu, Y.2    Crane, D.D.3    Barry III, C.E.4
  • 126
    • 0037238269 scopus 로고    scopus 로고
    • The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase
    • Zhang, Y. M., H. Marrakchi, S. W. White, and C. O. Rock. 2003. The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase. J. Lipid Res. 44:1-10.
    • (2003) J. Lipid Res. , vol.44 , pp. 1-10
    • Zhang, Y.M.1    Marrakchi, H.2    White, S.W.3    Rock, C.O.4


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