메뉴 건너뛰기




Volumn 11, Issue 8, 2016, Pages 2254-2264

Characterization of the Post-Assembly Line Tailoring Processes in Teicoplanin Biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; AGLYCONE; GLYCOSYLTRANSFERASE; LONG CHAIN FATTY ACID COENZYME A LIGASE; TEICOPLANIN; THIOL ESTER HYDROLASE;

EID: 84983335554     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00018     Document Type: Article
Times cited : (14)

References (61)
  • 1
    • 84890255189 scopus 로고    scopus 로고
    • New and alternative approaches to tackling antibiotic resistance
    • Tillotson, G. S. and Theriault, N. (2013) New and alternative approaches to tackling antibiotic resistance F1000Prime Rep. 7, 1-7 10.12703/P5-51
    • (2013) F1000Prime Rep. , vol.7 , pp. 1-7
    • Tillotson, G.S.1    Theriault, N.2
  • 2
    • 84895932868 scopus 로고    scopus 로고
    • Vancomycin resistant enterococci healthcare associated infections
    • Orsi, G. B. and Ciorba, V. (2013) Vancomycin resistant enterococci healthcare associated infections Ann. Iq. 25, 485-492 10.7416/ai.2013.1948
    • (2013) Ann. Iq. , vol.25 , pp. 485-492
    • Orsi, G.B.1    Ciorba, V.2
  • 3
    • 84882261313 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus infections
    • Taylor, A. R. (2013) Methicillin-resistant Staphylococcus aureus infections Prim. Care 40, 637-654 10.1016/j.pop.2013.06.002
    • (2013) Prim. Care , vol.40 , pp. 637-654
    • Taylor, A.R.1
  • 5
    • 84926642568 scopus 로고    scopus 로고
    • Antibiotics and bacterial resistance in the 21st century
    • Fair, R. J. and Tor, Y. (2014) Antibiotics and bacterial resistance in the 21st century Perspect. Med. Chem. 6, 25-64 10.4137/PMC.S14459
    • (2014) Perspect. Med. Chem. , vol.6 , pp. 25-64
    • Fair, R.J.1    Tor, Y.2
  • 6
    • 84879108210 scopus 로고    scopus 로고
    • Antimicrobial resistance: Action to combat the rising microbial challenges
    • Paphitou, N. I. (2013) Antimicrobial resistance: action to combat the rising microbial challenges Int. J. Antimicrob. Agents 42, S25 10.1016/j.ijantimicag.2013.04.007
    • (2013) Int. J. Antimicrob. Agents , vol.42 , pp. S25
    • Paphitou, N.I.1
  • 8
    • 0027360728 scopus 로고
    • Teicoplanin versus vancomycin in the empirical treatment of febrile neutropenic patients
    • Chow, A. V., Jewesson, P. J., Kureishi, A., and Phillips, G. L. (1993) Teicoplanin versus vancomycin in the empirical treatment of febrile neutropenic patients Eur. J. Haematol. 54, 18-24 10.1111/j.1600-0609.1993.tb01901.x
    • (1993) Eur. J. Haematol. , vol.54 , pp. 18-24
    • Chow, A.V.1    Jewesson, P.J.2    Kureishi, A.3    Phillips, G.L.4
  • 9
    • 2342623351 scopus 로고    scopus 로고
    • Glycopeptide antibiotics from conventional molecules to new derivatives
    • Van Bambeke, F., Van Laethem, Y., Courvalin, P., and Tulkens, P. M. (2004) Glycopeptide antibiotics from conventional molecules to new derivatives Drugs 64, 913-936 10.2165/00003495-200464090-00001
    • (2004) Drugs , vol.64 , pp. 913-936
    • Van Bambeke, F.1    Van Laethem, Y.2    Courvalin, P.3    Tulkens, P.M.4
  • 11
    • 78649671049 scopus 로고    scopus 로고
    • Oritavancin disrupts membrane integrity of Staphylococcus aureus and vancomycin-resistant enterococci to effect rapid bacterial killing
    • Belley, A., McKay, G. A., Arhin, F. F., Sarmiento, I., Beaulieu, S., Fadhil, I., Parr, T. R., Jr., and Moeck, G. (2010) Oritavancin disrupts membrane integrity of Staphylococcus aureus and vancomycin-resistant enterococci to effect rapid bacterial killing Antimicrob. Agents Chemother. 54, 5369-5371 10.1128/AAC.00760-10
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 5369-5371
    • Belley, A.1    McKay, G.A.2    Arhin, F.F.3    Sarmiento, I.4    Beaulieu, S.5    Fadhil, I.6    Parr, Jr.T.R.7    Moeck, G.8
  • 12
    • 34247092376 scopus 로고    scopus 로고
    • Dalbavancin: A novel antimicrobial
    • Chen, A. Y., Zervos, M. J., and Vazquez, J. A. (2007) Dalbavancin: a novel antimicrobial Int. J. Clin Pract. 61, 853-863 10.1111/j.1742-1241.2007.01318.x
    • (2007) Int. J. Clin Pract. , vol.61 , pp. 853-863
    • Chen, A.Y.1    Zervos, M.J.2    Vazquez, J.A.3
  • 14
    • 0037450076 scopus 로고    scopus 로고
    • Vancomycin assembly: Nature's way
    • Hubbard, B. K. and Walsh, C. T. (2003) Vancomycin assembly: nature's way Angew. Chem., Int. Ed. 42, 730-765 10.1002/anie.200390202
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 730-765
    • Hubbard, B.K.1    Walsh, C.T.2
  • 15
    • 14844339524 scopus 로고    scopus 로고
    • Glycopeptide and lipoglycopeptide antibiotics
    • Kahne, D., Leimkuhler, C., Lu, W., and Walsh, C. (2005) Glycopeptide and lipoglycopeptide antibiotics Chem. Rev. 105, 425-448 10.1021/cr030103a
    • (2005) Chem. Rev. , vol.105 , pp. 425-448
    • Kahne, D.1    Leimkuhler, C.2    Lu, W.3    Walsh, C.4
  • 16
    • 53549095165 scopus 로고    scopus 로고
    • Synopsis of structural, biosynthetic and chemical aspects of glycopeptide antibiotics
    • Wolter, F., Schoof, S., and Süssmuth, R. D. (2007) Synopsis of structural, biosynthetic and chemical aspects of glycopeptide antibiotics Top Curr. Chem. 267, 143-185 10.1007/128-041
    • (2007) Top Curr. Chem. , vol.267 , pp. 143-185
    • Wolter, F.1    Schoof, S.2    Süssmuth, R.D.3
  • 17
    • 84862094645 scopus 로고    scopus 로고
    • Redesign of glycopeptides antibiotics: Back to the future
    • James, R. C., Pierce, J. G., Okano, A., Xie, J., and Boger, D. L. (2012) Redesign of glycopeptides antibiotics: back to the future ACS Chem. Biol. 7, 797-804 10.1021/cb300007j
    • (2012) ACS Chem. Biol. , vol.7 , pp. 797-804
    • James, R.C.1    Pierce, J.G.2    Okano, A.3    Xie, J.4    Boger, D.L.5
  • 18
    • 84855978013 scopus 로고    scopus 로고
    • Total synthesis of [ [C(=S)NH]Tpg4] vancomycin aglycon, [ [C(=NH)NH]Tpg4] vancomycin aglycon, and related key compounds: Reengineering vancomycin for dual D-Ala-D-Ala and D-Ala-D-Lac binding
    • Xie, J., Okano, A., Pierce, J. G., James, R. C., Stamm, S., Crane, C. M., and Boger, D. L. (2012) Total synthesis of [ [C(=S)NH]Tpg4] vancomycin aglycon, [ [C(=NH)NH]Tpg4] vancomycin aglycon, and related key compounds: reengineering vancomycin for dual D-Ala-D-Ala and D-Ala-D-Lac binding J. Am. Chem. Soc. 134, 1284-1297 10.1021/ja209937s
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1284-1297
    • Xie, J.1    Okano, A.2    Pierce, J.G.3    James, R.C.4    Stamm, S.5    Crane, C.M.6    Boger, D.L.7
  • 19
    • 84878634623 scopus 로고    scopus 로고
    • Chemical Tailoring of Teicoplanin with Site-Selective Reactions
    • Pathak, T. P. and Miller, S. J. (2013) Chemical Tailoring of Teicoplanin with Site-Selective Reactions J. Am. Chem. Soc. 135, 8415-8422 10.1021/ja4038998
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8415-8422
    • Pathak, T.P.1    Miller, S.J.2
  • 20
    • 84883121575 scopus 로고    scopus 로고
    • Asymmetric Catalysis at a Distance: Catalytic, Site-Selective Phosphorylation of Teicoplanin
    • Han, S. and Miller, S. J. (2013) Asymmetric Catalysis at a Distance: Catalytic, Site-Selective Phosphorylation of Teicoplanin J. Am. Chem. Soc. 135, 12414-12421 10.1021/ja406067v
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12414-12421
    • Han, S.1    Miller, S.J.2
  • 21
    • 84911899902 scopus 로고    scopus 로고
    • X-ray Crystal Structure of Teicoplanin A2-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy
    • Han, S., Le, B. V., Hajare, H. S., Baxter, R. H. G., and Miller, S. J. (2014) X-ray Crystal Structure of Teicoplanin A2-2 Bound to a Catalytic Peptide Sequence via the Carrier Protein Strategy J. Org. Chem. 79, 8550-8556 10.1021/jo501625f
    • (2014) J. Org. Chem. , vol.79 , pp. 8550-8556
    • Han, S.1    Le, B.V.2    Hajare, H.S.3    Baxter, R.H.G.4    Miller, S.J.5
  • 22
    • 69249210987 scopus 로고    scopus 로고
    • Biosynthesis, biotechnological production, and application of teicoplanin: Current state and perspectives
    • Jung, H. M., Jeya, M., Kim, S. Y., Moon, H. J., Kumar Singh, R., Zhang, Y. W., and Lee, J. K. (2009) Biosynthesis, biotechnological production, and application of teicoplanin: current state and perspectives Appl. Microbiol. Biotechnol. 84, 417-428 10.1007/s00253-009-2107-4
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 417-428
    • Jung, H.M.1    Jeya, M.2    Kim, S.Y.3    Moon, H.J.4    Kumar Singh, R.5    Zhang, Y.W.6    Lee, J.K.7
  • 23
    • 80054090960 scopus 로고    scopus 로고
    • Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin
    • Article number 82
    • Taurino, C., Frattini, L., Marcone, G. L., Gastaldo, L., and Marinelli, F. (2011) Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin Microb. Cell Fact. 10, 1-13 10.1186/1475-2859-10-82
    • (2011) Microbial Cell Factories , vol.10
    • Taurino, C.1    Frattini, L.2    Marcone, G.L.3    Gastaldo, L.4    Marinelli, F.5
  • 24
    • 1142306159 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: Characterization of two glycosyltransferases and the key acyltransferase
    • Li, T. L., Huang, F., Haydock, S. F., Mironenko, T., Leadlay, P. F., and Spencer, J. B. (2004) Biosynthetic gene cluster of the glycopeptide antibiotic teicoplanin: characterization of two glycosyltransferases and the key acyltransferase Chem. Biol. 11, 107-119 10.1016/j.chembiol.2004.01.001
    • (2004) Chem. Biol. , vol.11 , pp. 107-119
    • Li, T.L.1    Huang, F.2    Haydock, S.F.3    Mironenko, T.4    Leadlay, P.F.5    Spencer, J.B.6
  • 25
    • 1642401951 scopus 로고    scopus 로고
    • Organization of the teicoplanin gene cluster in Actinoplanes teichomyceticus
    • Sosio, M., Kloosterman, H., Bianchi, A., de Vreugd, P., Dijkhuizen, L., and Donadio, S. (2004) Organization of the teicoplanin gene cluster in Actinoplanes teichomyceticus Microbiology 150, 95-102 10.1099/mic.0.26507-0
    • (2004) Microbiology , vol.150 , pp. 95-102
    • Sosio, M.1    Kloosterman, H.2    Bianchi, A.3    De Vreugd, P.4    Dijkhuizen, L.5    Donadio, S.6
  • 26
    • 12344249865 scopus 로고    scopus 로고
    • Tailoring of glycopeptide scaffolds by the acyltransferases from the teicoplanin and A-40,926 biosynthetic operons
    • Kruger, R. G., Lu, W., Oberthür, M., Tao, J., Kahne, D., and Walsh, C. T. (2005) Tailoring of glycopeptide scaffolds by the acyltransferases from the teicoplanin and A-40,926 biosynthetic operons Chem. Biol. 12, 131-140 10.1016/j.chembiol.2004.12.005
    • (2005) Chem. Biol. , vol.12 , pp. 131-140
    • Kruger, R.G.1    Lu, W.2    Oberthür, M.3    Tao, J.4    Kahne, D.5    Walsh, C.T.6
  • 27
    • 34548157165 scopus 로고    scopus 로고
    • Kinetic analysis of teicoplanin glycosyltransferases and acyltransferase reveal ordered tailoring of aglyconescaffold to reconstitute mature teicoplanin
    • Howard-Jones, A. R., Kruger, R. G., Lu, W., Tao, J., Leimkuhler, C., Kahne, D., and Walsh, C. T. (2007) Kinetic analysis of teicoplanin glycosyltransferases and acyltransferase reveal ordered tailoring of aglyconescaffold to reconstitute mature teicoplanin J. Am. Chem. Soc. 129, 10082-10083 10.1021/ja0735857
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10082-10083
    • Howard-Jones, A.R.1    Kruger, R.G.2    Lu, W.3    Tao, J.4    Leimkuhler, C.5    Kahne, D.6    Walsh, C.T.7
  • 28
    • 43149119251 scopus 로고    scopus 로고
    • The role of Cep15 in the biosynthesis of chloroeremomycin: Reactivation of an ancestral catalytic function
    • Truman, A. W., Fan, Q., Röttgen, M., Stegmann, E., Leadlay, P. F., and Spencer, J. B. (2008) The role of Cep15 in the biosynthesis of chloroeremomycin: reactivation of an ancestral catalytic function Chem. Biol. 15, 476-484 10.1016/j.chembiol.2008.03.019
    • (2008) Chem. Biol. , vol.15 , pp. 476-484
    • Truman, A.W.1    Fan, Q.2    Röttgen, M.3    Stegmann, E.4    Leadlay, P.F.5    Spencer, J.B.6
  • 29
    • 67649563070 scopus 로고    scopus 로고
    • Chimeric glycosyltransferases for the generation of hybrid glycopeptides
    • Truman, A. W., Dias, M. V., Wu, S., Blundell, T. L., Huang, F., and Spencer, J. B. (2009) Chimeric glycosyltransferases for the generation of hybrid glycopeptides Chem. Biol. 16, 676-685 10.1016/j.chembiol.2009.04.013
    • (2009) Chem. Biol. , vol.16 , pp. 676-685
    • Truman, A.W.1    Dias, M.V.2    Wu, S.3    Blundell, T.L.4    Huang, F.5    Spencer, J.B.6
  • 30
    • 64249110009 scopus 로고    scopus 로고
    • Molecular genetic approaches to analyze glycopeptide biosynthesis
    • Wohlleben, W., Stegmann, E., and Süssmuth, R. D. (2009) Molecular genetic approaches to analyze glycopeptide biosynthesis Methods Enzymol. 458, 459-486 10.1016/S0076-6879(09)04818-6
    • (2009) Methods Enzymol. , vol.458 , pp. 459-486
    • Wohlleben, W.1    Stegmann, E.2    Süssmuth, R.D.3
  • 31
    • 44949234793 scopus 로고    scopus 로고
    • Application of conjugation using phiC31 att/int system for Actinoplanes teichomyceticus, a producer of teicoplanin
    • Ha, H. S., Hwang, Y. I., and Choi, S. U. (2008) Application of conjugation using phiC31 att/int system for Actinoplanes teichomyceticus, a producer of teicoplanin Biotechnol. Lett. 30, 1233-1238 10.1007/s10529-008-9671-z
    • (2008) Biotechnol. Lett. , vol.30 , pp. 1233-1238
    • Ha, H.S.1    Hwang, Y.I.2    Choi, S.U.3
  • 32
    • 84860188275 scopus 로고    scopus 로고
    • Manipulating the regulatory genes for teicoplanin production in Actinoplanes teichomyceticus
    • Horbal, L., Zaburannyy, N., Ostash, B., Shulga, S., and Fedorenko, V. (2012) Manipulating the regulatory genes for teicoplanin production in Actinoplanes teichomyceticus World J. Microbiol. Biotechnol. 28, 2095-2100 10.1007/s11274-012-1013-6
    • (2012) World J. Microbiol. Biotechnol. , vol.28 , pp. 2095-2100
    • Horbal, L.1    Zaburannyy, N.2    Ostash, B.3    Shulga, S.4    Fedorenko, V.5
  • 33
    • 84888827753 scopus 로고    scopus 로고
    • Evaluation of heterologous promoters for genetic analysis of Actinoplanes teichomyceticus - Producer of teicoplanin, drug of last defense
    • Horbal, L., Kobylyanskyy, A., Yushchuk, O., Zaburannyi, N., Luzhetskyy, A., Ostash, B., Marinelli, F., and Fedorenko, V. (2013) Evaluation of heterologous promoters for genetic analysis of Actinoplanes teichomyceticus - Producer of teicoplanin, drug of last defense J. Biotechnol. 168, 367-372 10.1016/j.jbiotec.2013.10.018
    • (2013) J. Biotechnol. , vol.168 , pp. 367-372
    • Horbal, L.1    Kobylyanskyy, A.2    Yushchuk, O.3    Zaburannyi, N.4    Luzhetskyy, A.5    Ostash, B.6    Marinelli, F.7    Fedorenko, V.8
  • 34
    • 84920250171 scopus 로고    scopus 로고
    • The pathway-specific regulatory genes, tei15∗ and tei16∗, are the master switches of teicoplanin production in Actinoplanes teichomyceticus
    • Horbal, L., Kobylyanskyy, A., Truman, A. W., Zaburranyi, N., Ostash, B., Luzhetskyy, A., Marinelli, F., and Fedorenko, V. (2014) The pathway-specific regulatory genes, tei15∗ and tei16∗, are the master switches of teicoplanin production in Actinoplanes teichomyceticus Appl. Microbiol. Biotechnol. 98, 9295-9309 10.1007/s00253-014-5969-z
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 9295-9309
    • Horbal, L.1    Kobylyanskyy, A.2    Truman, A.W.3    Zaburranyi, N.4    Ostash, B.5    Luzhetskyy, A.6    Marinelli, F.7    Fedorenko, V.8
  • 35
    • 0035910072 scopus 로고    scopus 로고
    • Glycopeptide antibiotic biosynthesis: Enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine
    • Chen, H., Tseng, C. C., Hubbard, B. K., and Walsh, C. T. (2001) Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine Proc. Natl. Acad. Sci. U. S. A. 98, 14901-14906 10.1073/pnas.221582098
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14901-14906
    • Chen, H.1    Tseng, C.C.2    Hubbard, B.K.3    Walsh, C.T.4
  • 36
    • 4644363591 scopus 로고    scopus 로고
    • DpgC is a metal- and cofactor-free 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase in the vancomycin biosynthetic pathway
    • Tseng, C. C., Vaillancourt, F. H., Bruner, S. D., and Walsh, C. T. (2004) DpgC is a metal- and cofactor-free 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase in the vancomycin biosynthetic pathway Chem. Biol. 11, 1195-1203 10.1016/j.chembiol.2004.06.012
    • (2004) Chem. Biol. , vol.11 , pp. 1195-1203
    • Tseng, C.C.1    Vaillancourt, F.H.2    Bruner, S.D.3    Walsh, C.T.4
  • 37
    • 21144439895 scopus 로고    scopus 로고
    • The biosynthesis of vancomycin-type glycopeptide antibiotics - A model for oxidative side-chain crosslinking by oxygenases coupled to the action of peptide synthetases
    • Bischoff, D., Bister, B., Bertazzo, M., Pfeifer, V., Stegmann, E., Nicholson, G. J., Keller, S., Pelzer, S., Wohlleben, W., and Süssmuth, R. D. (2005) The biosynthesis of vancomycin-type glycopeptide antibiotics-a model for oxidative side-chain crosslinking by oxygenases coupled to the action of peptide synthetases ChemBioChem 6, 2267-2272 10.1002/cbic.200400328
    • (2005) ChemBioChem , vol.6 , pp. 2267-2272
    • Bischoff, D.1    Bister, B.2    Bertazzo, M.3    Pfeifer, V.4    Stegmann, E.5    Nicholson, G.J.6    Keller, S.7    Pelzer, S.8    Wohlleben, W.9    Süssmuth, R.D.10
  • 38
    • 70349556435 scopus 로고    scopus 로고
    • Complex oxidation chemistry in the biosynthetic pathways to vancomycin/teicoplanin antibiotics
    • Widboom, P. F. and Bruner, S. D. (2009) Complex oxidation chemistry in the biosynthetic pathways to vancomycin/teicoplanin antibiotics ChemBioChem 10, 1757-1764 10.1002/cbic.200900117
    • (2009) ChemBioChem , vol.10 , pp. 1757-1764
    • Widboom, P.F.1    Bruner, S.D.2
  • 39
    • 84915809650 scopus 로고    scopus 로고
    • Cytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesis
    • Haslinger, K., Maximowitsch, E., Brieke, C., Koch, A., and Cryle, M. J. (2014) Cytochrome P450 OxyBtei catalyzes the first phenolic coupling step in teicoplanin biosynthesis ChemBioChem 15, 2719-2728 10.1002/cbic.201402441
    • (2014) ChemBioChem , vol.15 , pp. 2719-2728
    • Haslinger, K.1    Maximowitsch, E.2    Brieke, C.3    Koch, A.4    Cryle, M.J.5
  • 40
    • 54349099492 scopus 로고    scopus 로고
    • Investigation into the mechanism of phenolic couplings during the biosynthesis of glycopeptide antibiotics
    • Holding, A. N. and Spencer, J. B. (2008) Investigation into the mechanism of phenolic couplings during the biosynthesis of glycopeptide antibiotics ChemBioChem 9, 2209-2214 10.1002/cbic.200800303
    • (2008) ChemBioChem , vol.9 , pp. 2209-2214
    • Holding, A.N.1    Spencer, J.B.2
  • 41
    • 1642496907 scopus 로고    scopus 로고
    • The biosynthesis of glycopeptides antibiotics - A model for complex, non-ribosomally synthesized, peptidic secondary metabolites
    • Süssmuth, R. D. and Wohlleben, W. (2004) The biosynthesis of glycopeptides antibiotics-a model for complex, non-ribosomally synthesized, peptidic secondary metabolites Appl. Microbiol. Biotechnol. 63, 344-350 10.1007/s00253-003-1443-z
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 344-350
    • Süssmuth, R.D.1    Wohlleben, W.2
  • 42
    • 33750983625 scopus 로고    scopus 로고
    • Identification of a Deacetylase Involved in the Maturation of Teicoplanin
    • Truman, A. W., Robinson, L., and Spencer, J. B. (2006) Identification of a Deacetylase Involved in the Maturation of Teicoplanin ChemBioChem 7, 1670-1675 10.1002/cbic.200600308
    • (2006) ChemBioChem , vol.7 , pp. 1670-1675
    • Truman, A.W.1    Robinson, L.2    Spencer, J.B.3
  • 43
    • 84893142381 scopus 로고    scopus 로고
    • Glycopeptide antibiotic biosynthesis
    • Yim, G., Thaker, M. N., Koteva, K., and Wright, G. (2014) Glycopeptide antibiotic biosynthesis J. Antibiot. 67, 31-41 10.1038/ja.2013.117
    • (2014) J. Antibiot. , vol.67 , pp. 31-41
    • Yim, G.1    Thaker, M.N.2    Koteva, K.3    Wright, G.4
  • 45
    • 33749171560 scopus 로고    scopus 로고
    • Vancomycin analogues containing monosaccharides exhibit improved antibiotic activity: A combined one-pot enzymatic glycosylation and chemical diversification strategy
    • Thayer, D. A. and Wong, C. H. (2006) Vancomycin analogues containing monosaccharides exhibit improved antibiotic activity: a combined one-pot enzymatic glycosylation and chemical diversification strategy Chem.-Asian J. 1, 445-452 10.1002/asia.200600084
    • (2006) Chem. - Asian J. , vol.1 , pp. 445-452
    • Thayer, D.A.1    Wong, C.H.2
  • 47
    • 84946114885 scopus 로고    scopus 로고
    • Membrane Disruption and Enhanced Inhibition of Cell-Wall Biosynthesis: A Synergistic Approach to Tackle Vancomycin-Resistant Bacteria
    • Yarlagadda, V., Samaddar, S., Paramanandham, K., Shome, B. R., and Haldar, J. (2015) Membrane Disruption and Enhanced Inhibition of Cell-Wall Biosynthesis: A Synergistic Approach to Tackle Vancomycin-Resistant Bacteria Angew. Chem., Int. Ed. 54, 13644-13649 10.1002/anie.201507567
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 13644-13649
    • Yarlagadda, V.1    Samaddar, S.2    Paramanandham, K.3    Shome, B.R.4    Haldar, J.5
  • 50
    • 84905695318 scopus 로고    scopus 로고
    • Multiple complexes of long aliphatic N-acyltransferases lead to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics, effectively killing vancomycin-resistant enterococcus
    • Lyu, S. Y., Liu, Y. C., Chang, C. Y., Huang, C. J., Chiu, Y. H., Huang, C. M., Hsu, N. S., Lin, K. H., Wu, C. J., Tsai, M. D., and Li, T. L. (2014) Multiple complexes of long aliphatic N-acyltransferases lead to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics, effectively killing vancomycin-resistant enterococcus J. Am. Chem. Soc. 136, 10989-10995 10.1021/ja504125v
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 10989-10995
    • Lyu, S.Y.1    Liu, Y.C.2    Chang, C.Y.3    Huang, C.J.4    Chiu, Y.H.5    Huang, C.M.6    Hsu, N.S.7    Lin, K.H.8    Wu, C.J.9    Tsai, M.D.10    Li, T.L.11
  • 51
    • 0036008849 scopus 로고    scopus 로고
    • Glycopeptie biosynthesis in Amycolatopsis mediterranei DSM5908: Function of a halogenase and a haloperoxidase/perhydrolase
    • Puk, O., Huber, P., Bischoff, D., Recktenwald, J., Jung, G., Süssmuth, R. D., van Pée, K. H., Wohlleben, W., and Pelzer, S. (2002) Glycopeptie biosynthesis in Amycolatopsis mediterranei DSM5908: function of a halogenase and a haloperoxidase/perhydrolase Chem. Biol. 9, 225-235 10.1016/S1074-5521(02)00101-1
    • (2002) Chem. Biol. , vol.9 , pp. 225-235
    • Puk, O.1    Huber, P.2    Bischoff, D.3    Recktenwald, J.4    Jung, G.5    Süssmuth, R.D.6    Van Pée, K.H.7    Wohlleben, W.8    Pelzer, S.9
  • 52
    • 53849091701 scopus 로고    scopus 로고
    • Role of DptE and DptF in the lipidation reaction of daptomycin
    • Wittmann, M., Linne, U., Pohlmann, V., and Marahiel, M. A. (2008) Role of DptE and DptF in the lipidation reaction of daptomycin FEBS J. 275, 5343-5354 10.1111/j.1742-4658.2008.06664.x
    • (2008) FEBS J. , vol.275 , pp. 5343-5354
    • Wittmann, M.1    Linne, U.2    Pohlmann, V.3    Marahiel, M.A.4
  • 53
    • 79251595133 scopus 로고    scopus 로고
    • Structural and functional studies of fatty acyl adenylate ligases from E. Coli and L. Pneumophila
    • Zhang, Z., Zhou, R., Sauder, J. M., Tonge, P. J., Burley, S. K., and Swaminathan, S. (2011) Structural and functional studies of fatty acyl adenylate ligases from E. coli and L. pneumophila J. Mol. Biol. 406, 313-324 10.1016/j.jmb.2010.12.011
    • (2011) J. Mol. Biol. , vol.406 , pp. 313-324
    • Zhang, Z.1    Zhou, R.2    Sauder, J.M.3    Tonge, P.J.4    Burley, S.K.5    Swaminathan, S.6
  • 54
    • 84946593685 scopus 로고    scopus 로고
    • Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit
    • Miyazawa, T., Takahashi, S., Kawata, A., Panthee, S., Hayashi, T., Shimizu, T., Nogawa, T., and Osada, H. (2015) Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit J. Biol. Chem. 290, 26994-27011 10.1074/jbc.M115.677195
    • (2015) J. Biol. Chem. , vol.290 , pp. 26994-27011
    • Miyazawa, T.1    Takahashi, S.2    Kawata, A.3    Panthee, S.4    Hayashi, T.5    Shimizu, T.6    Nogawa, T.7    Osada, H.8
  • 55
    • 0037387025 scopus 로고    scopus 로고
    • Production of teicoplanin by a mutant of Actinoplanes teicomyceticus
    • Lee, J. C., Park, H. R., Park, D. J., Son, K. H., Yoon, K. H., Kim, Y. B., and Kim, C. J. (2003) Production of teicoplanin by a mutant of Actinoplanes teicomyceticus Biotechnol. Lett. 25, 537-540 10.1023/A:1022842203917
    • (2003) Biotechnol. Lett. , vol.25 , pp. 537-540
    • Lee, J.C.1    Park, H.R.2    Park, D.J.3    Son, K.H.4    Yoon, K.H.5    Kim, Y.B.6    Kim, C.J.7
  • 56
    • 64149117037 scopus 로고    scopus 로고
    • Structure and functional analysis of RifR, the Type II thioesterase from the rifamycin biosynthetic pathway
    • Claxton, H. B., Akey, D. L., Silver, M. K., Admiraal, S. J., and Smith, J. L. (2009) Structure and functional analysis of RifR, the Type II thioesterase from the rifamycin biosynthetic pathway J. Biol. Chem. 284, 5021-5029 10.1074/jbc.M808604200
    • (2009) J. Biol. Chem. , vol.284 , pp. 5021-5029
    • Claxton, H.B.1    Akey, D.L.2    Silver, M.K.3    Admiraal, S.J.4    Smith, J.L.5
  • 57
    • 0017861884 scopus 로고
    • Purification and properties of a thioesterase from lactating rat mammary gland which modifies the product specificity of fatty acid synthetase
    • Libertini, L. J. and Smith, S. (1978) Purification and properties of a thioesterase from lactating rat mammary gland which modifies the product specificity of fatty acid synthetase J. Biol. Chem. 253, 1393-1401
    • (1978) J. Biol. Chem. , vol.253 , pp. 1393-1401
    • Libertini, L.J.1    Smith, S.2
  • 58
    • 84906243702 scopus 로고    scopus 로고
    • Characterization of type II thioesterases involved in natamycin biosynthesis in Streptomyces chattanoogensis L10
    • Wang, Y.-Y., Ran, X.-X., Chen, W.-B., Zhang, X.-S., Guo, Y.-Y., Jiang, X.-H., Jiang, H., Li, Y.-Q., and Liu, S.-P. (2014) Characterization of type II thioesterases involved in natamycin biosynthesis in Streptomyces chattanoogensis L10 FEBS Lett. 588, 3259-3264 10.1016/j.febslet.2014.07.010
    • (2014) FEBS Lett. , vol.588 , pp. 3259-3264
    • Wang, Y.-Y.1    Ran, X.-X.2    Chen, W.-B.3    Zhang, X.-S.4    Guo, Y.-Y.5    Jiang, X.-H.6    Jiang, H.7    Li, Y.-Q.8    Liu, S.-P.9
  • 59
    • 2142710129 scopus 로고    scopus 로고
    • Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis
    • Linne, U., Schwarzer, D., Schroeder, G. N., and Marahiel, M. (2004) Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis Eur. J. Biochem. 271, 1536-1545 10.1111/j.1432-1033.2004.04063.x
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1536-1545
    • Linne, U.1    Schwarzer, D.2    Schroeder, G.N.3    Marahiel, M.4
  • 61
    • 1142275128 scopus 로고    scopus 로고
    • Valine influences production and complex composition of glycopeptide antibiotic A40926 in fermentations of Nonomuraea sp. ATCC 39727
    • Beltrametti, F., Jovetic, S., Feroggio, M., Gastaldo, L., Selva, E., and Marinelli, F. (2004) Valine influences production and complex composition of glycopeptide antibiotic A40926 in fermentations of Nonomuraea sp. ATCC 39727 J. Antibiot. 57, 37-44 10.7164/antibiotics.57.37
    • (2004) J. Antibiot. , vol.57 , pp. 37-44
    • Beltrametti, F.1    Jovetic, S.2    Feroggio, M.3    Gastaldo, L.4    Selva, E.5    Marinelli, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.