메뉴 건너뛰기




Volumn 61, Issue 5, 2006, Pages 1294-1307

A glutamic acid 3-methyltransferase encoded by an accessory gene locus important for daptomycin biosynthesis in Streptomyces roseosporus

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLGLUTAMIC ACID; AMINO ACID DERIVATIVE; CALCIUM; CYCLOPEPTIDE; DAPTOMYCIN; GENE PRODUCT; GLUTAMIC ACID; GLUTAMIC ACID 3 METHYLTRANSFERASE; LIPOPEPTIDE; METHYLTRANSFERASE; PEPTIDE SYNTHASE; POLYPEPTIDE ANTIBIOTIC AGENT; THIOL ESTER HYDROLASE; TRYPTOPHAN 2,3 DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 33747056235     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05305.x     Document Type: Article
Times cited : (60)

References (59)
  • 1
    • 0032971513 scopus 로고    scopus 로고
    • Differential regulation of glutamate, aspartate and gamma-amino-butyrate release by N-methyl-D-aspartate receptors in rat striatum after partial and extensive lesions to the nigro-striatal dopamine pathway
    • Abarca, J., and Bustos, G. (1999) Differential regulation of glutamate, aspartate and gamma-amino-butyrate release by N-methyl-D-aspartate receptors in rat striatum after partial and extensive lesions to the nigro-striatal dopamine pathway. Neurochem Int 35: 19-33.
    • (1999) Neurochem Int , vol.35 , pp. 19-33
    • Abarca, J.1    Bustos, G.2
  • 2
    • 0002994344 scopus 로고
    • Genetic recombination by protoplast fusion in Streptomyces
    • Baltz, R.H. (1980) Genetic recombination by protoplast fusion in Streptomyces. Dev Indust Microbiol 21: 43-54.
    • (1980) Dev Indust Microbiol , vol.21 , pp. 43-54
    • Baltz, R.H.1
  • 3
    • 0010581441 scopus 로고    scopus 로고
    • Lipopeptide antibiotics produced by Streptomyces roseosporus and Streptomyces fradiae
    • Strohl, W.R. (ed.). New York: Marcel Dekker
    • Baltz, R.H. (1997) Lipopeptide antibiotics produced by Streptomyces roseosporus and Streptomyces fradiae. In Biotechnology of Antibiotics. Strohl, W.R. (ed.). New York: Marcel Dekker, pp. 415-435.
    • (1997) Biotechnology of Antibiotics , pp. 415-435
    • Baltz, R.H.1
  • 4
    • 30844455997 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of lipopeptide antibiotics in Streptomyces roseosporus
    • Baltz, R.H., Brian, P., Miao, V., and Wrigley, S.K. (2006) Combinatorial biosynthesis of lipopeptide antibiotics in Streptomyces roseosporus. J Ind Microbiol Biotechnol 33: 66-74.
    • (2006) J Ind Microbiol Biotechnol , vol.33 , pp. 66-74
    • Baltz, R.H.1    Brian, P.2    Miao, V.3    Wrigley, S.K.4
  • 5
    • 0030988484 scopus 로고    scopus 로고
    • Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
    • Barkovich, R.J., Shtanko, A., Shepherd, J.A., Lee, P.T., Myles, D.C., Tzagoloff, A., and Clarke, C.F. (1997) Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis. J Biol Chem 272: 9182-9188.
    • (1997) J Biol Chem , vol.272 , pp. 9182-9188
    • Barkovich, R.J.1    Shtanko, A.2    Shepherd, J.A.3    Lee, P.T.4    Myles, D.C.5    Tzagoloff, A.6    Clarke, C.F.7
  • 7
    • 0022404392 scopus 로고
    • Cloning and analysis of the promoter region of the erythromycin resistance gene (ermE) of Streptomyces erythraeus
    • Bibb, M.J., Janssen, G.R., and Ward, J.M. (1985) Cloning and analysis of the promoter region of the erythromycin resistance gene (ermE) of Streptomyces erythraeus. Gene 38: 215-226.
    • (1985) Gene , vol.38 , pp. 215-226
    • Bibb, M.J.1    Janssen, G.R.2    Ward, J.M.3
  • 8
    • 0000013349 scopus 로고
    • N-methyltransferase function of the multifunctional enzyme enniatin synthetase
    • Billich, A., and Zocher, R. (1987) N-methyltransferase function of the multifunctional enzyme enniatin synthetase. Biochemistry 26: 8417-8423.
    • (1987) Biochemistry , vol.26 , pp. 8417-8423
    • Billich, A.1    Zocher, R.2
  • 10
    • 0033133991 scopus 로고    scopus 로고
    • Impact of thioesterase activity on tylosin biosynthesis in Streptomyces fradiae
    • Butler, A.R., Bate, N., and Cundliffe, E. (1999) Impact of thioesterase activity on tylosin biosynthesis in Streptomyces fradiae. Chem Biol 6: 287-292.
    • (1999) Chem Biol , vol.6 , pp. 287-292
    • Butler, A.R.1    Bate, N.2    Cundliffe, E.3
  • 13
    • 0034077625 scopus 로고    scopus 로고
    • Occurrence of D-aspartic acid and N-methyl-D-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release
    • D'Aniello, A., Di Fiore, M.M., Fisher, G.H., Milone, A., Seleni, A., D'Aniello, S., et al. (2000) Occurrence of D-aspartic acid and N-methyl-D-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release. FASEB J 14: 699-714.
    • (2000) FASEB J , vol.14 , pp. 699-714
    • D'Aniello, A.1    Di Fiore, M.M.2    Fisher, G.H.3    Milone, A.4    Seleni, A.5    D'Aniello, S.6
  • 14
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 15
    • 0023204011 scopus 로고
    • A21978C, a complex of new acidic peptide antibiotics: Isolation, chemistry, and mass spectral structure elucidation
    • Debono, M., Barnhart, M., Carrell, C.B., Hoffmann, J.A., Occolowitz, J.L., Abbott, B.J., et al. (1987) A21978C, a complex of new acidic peptide antibiotics: isolation, chemistry, and mass spectral structure elucidation. J Antibiot 40: 761-777.
    • (1987) J Antibiot , vol.40 , pp. 761-777
    • Debono, M.1    Barnhart, M.2    Carrell, C.B.3    Hoffmann, J.A.4    Occolowitz, J.L.5    Abbott, B.J.6
  • 16
    • 0034646227 scopus 로고    scopus 로고
    • The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates
    • Ehmann, D.E., Shaw-Reid, C.A., Losey, H.C., and Walsh, C.T. (2000) The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Proc Natl Acad Sci USA 97: 2509-2514.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2509-2514
    • Ehmann, D.E.1    Shaw-Reid, C.A.2    Losey, H.C.3    Walsh, C.T.4
  • 17
    • 4544230403 scopus 로고    scopus 로고
    • Lipopeptides, focusing on daptomycin, for the treatment of Gram-positive infections
    • Eisenstein, B.I. (2004) Lipopeptides, focusing on daptomycin, for the treatment of Gram-positive infections. Expert Opin Invest Drugs 13: 1159-1169.
    • (2004) Expert Opin Invest Drugs , vol.13 , pp. 1159-1169
    • Eisenstein, B.I.1
  • 18
    • 0037199494 scopus 로고    scopus 로고
    • Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics
    • Eppelmann, K., Stachelhaus, T., and Marahiel, M.A. (2002) Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics. Biochemistry 41: 9718-9726.
    • (2002) Biochemistry , vol.41 , pp. 9718-9726
    • Eppelmann, K.1    Stachelhaus, T.2    Marahiel, M.A.3
  • 19
    • 0025373211 scopus 로고
    • A54145, a new lipopeptide antibiotic complex: Isolation and characterization
    • Fukuda, D.S., Du Bus, R.H., Baker, P.J., Berry, D.M., and Mynderse, J.S. (1990) A54145, a new lipopeptide antibiotic complex: isolation and characterization. J Antibiot 43: 594-600.
    • (1990) J Antibiot , vol.43 , pp. 594-600
    • Fukuda, D.S.1    Du Bus, R.H.2    Baker, P.J.3    Berry, D.M.4    Mynderse, J.S.5
  • 20
    • 11244286128 scopus 로고    scopus 로고
    • Synthesis and derivatization of daptomycin: A chemoenzymatic route to acidic lipopeptide antibiotics
    • Grunewald, J., Sieber, S.A., Mahlert, C., Linne, U., and Marahiel, M.A. (2004) Synthesis and derivatization of daptomycin: a chemoenzymatic route to acidic lipopeptide antibiotics. J Am Chem Soc 126: 17025-17031.
    • (2004) J Am Chem Soc , vol.126 , pp. 17025-17031
    • Grunewald, J.1    Sieber, S.A.2    Mahlert, C.3    Linne, U.4    Marahiel, M.A.5
  • 21
    • 15744372279 scopus 로고    scopus 로고
    • Mechanisms of action of newer antibiotics for Gram-positive pathogens
    • Hancock, R.E. (2005) Mechanisms of action of newer antibiotics for Gram-positive pathogens. Lancet Infect Dis 5: 209-218.
    • (2005) Lancet Infect Dis , vol.5 , pp. 209-218
    • Hancock, R.E.1
  • 22
    • 0037310949 scopus 로고    scopus 로고
    • A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis
    • Heinzelmann, E., Berger, S., Puk, O., Reichenstein, B., Wohlleben, W., and Schwartz, D. (2003) A glutamate mutase is involved in the biosynthesis of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. Antimicrob Agents Chemother 47: 447-457.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 447-457
    • Heinzelmann, E.1    Berger, S.2    Puk, O.3    Reichenstein, B.4    Wohlleben, W.5    Schwartz, D.6
  • 23
    • 0036848817 scopus 로고    scopus 로고
    • Structure, biosynthetic origin, and engineered biosynthesis of calcium-dependent antibiotics from Streptomyces coelicolor
    • Hojati, Z., Milne, C., Harvey, B., Gordon, L., Borg, M., Flett, F., et al. (2002) Structure, biosynthetic origin, and engineered biosynthesis of calcium-dependent antibiotics from Streptomyces coelicolor. Chem Biol 9: 1175-1187.
    • (2002) Chem Biol , vol.9 , pp. 1175-1187
    • Hojati, Z.1    Milne, C.2    Harvey, B.3    Gordon, L.4    Borg, M.5    Flett, F.6
  • 24
    • 0031036748 scopus 로고    scopus 로고
    • Use of rpsL for dominance selection and gene replacement in Streptomyces roseosporus
    • Hosted, T.J., and Baltz, R.H. (1997) Use of rpsL for dominance selection and gene replacement in Streptomyces roseosporus. J Bacteriol 179: 180-186.
    • (1997) J Bacteriol , vol.179 , pp. 180-186
    • Hosted, T.J.1    Baltz, R.H.2
  • 25
    • 0023939492 scopus 로고
    • The formation of daptomycin by supplying decanoic acid to Streptomyces roseosporus cultures producing the antibiotic complex A21978C
    • Huber, F.M., Pieper, R.L., and Tietz, A.J. (1988) The formation of daptomycin by supplying decanoic acid to Streptomyces roseosporus cultures producing the antibiotic complex A21978C. J Biotechnol 7: 283-292.
    • (1988) J Biotechnol , vol.7 , pp. 283-292
    • Huber, F.M.1    Pieper, R.L.2    Tietz, A.J.3
  • 26
    • 3342942636 scopus 로고    scopus 로고
    • Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin
    • Jung, D., Rozek, A., Okon, M., and Hancock, R.E. (2004) Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin. Chem Biol 11: 949-957.
    • (2004) Chem Biol , vol.11 , pp. 949-957
    • Jung, D.1    Rozek, A.2    Okon, M.3    Hancock, R.E.4
  • 27
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan, R.M., and Clarke, S. (1994) Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys 310: 417-427.
    • (1994) Arch Biochem Biophys , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 28
    • 0030900768 scopus 로고    scopus 로고
    • CDA: Calcium-dependent peptide antibiotics from Streptomyces coelicolor A3(2) containing unusual residues
    • Kempter, C., Kaiser, D., Haag, S., Nicholson, G., Gnau, V., Walk, T., et al. (1997) CDA: calcium-dependent peptide antibiotics from Streptomyces coelicolor A3(2) containing unusual residues. Angew Chem Int Ed Engl 36: 498-501.
    • (1997) Angew Chem Int Ed Engl , vol.36 , pp. 498-501
    • Kempter, C.1    Kaiser, D.2    Haag, S.3    Nicholson, G.4    Gnau, V.5    Walk, T.6
  • 30
    • 0031038898 scopus 로고    scopus 로고
    • A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: Isolation and identification of the Escherichia coli ubiE gene
    • Lee, P.T., Hsu, A.Y., Ha, H.T., and Clarke, C.F. (1997) A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J Bacteriol 179: 1748-1754.
    • (1997) J Bacteriol , vol.179 , pp. 1748-1754
    • Lee, P.T.1    Hsu, A.Y.2    Ha, H.T.3    Clarke, C.F.4
  • 31
    • 0034730091 scopus 로고    scopus 로고
    • Control of directionality in nonribosomal peptide synthesis: Role of the condensation domain in preventing misinitiation and timing of epimerization
    • Linne, U., and Marahiel, M.A. (2000) Control of directionality in nonribosomal peptide synthesis: role of the condensation domain in preventing misinitiation and timing of epimerization. Biochemistry 39: 10439-10447.
    • (2000) Biochemistry , vol.39 , pp. 10439-10447
    • Linne, U.1    Marahiel, M.A.2
  • 32
    • 0022456192 scopus 로고
    • A 2.6 kb DNA sequence of Streptomyces coelicolor A3(2) which functions as a transposable element
    • Lydiate, D.J., Ikeda, H., and Hopwood, D.A. (1986) A 2.6 kb DNA sequence of Streptomyces coelicolor A3(2) which functions as a transposable element. Mol Gen Genet 203: 79-88.
    • (1986) Mol Gen Genet , vol.203 , pp. 79-88
    • Lydiate, D.J.1    Ikeda, H.2    Hopwood, D.A.3
  • 33
    • 0029768888 scopus 로고    scopus 로고
    • Gene transfer and transposition mutagenesis in Streptomyces roseosporus: Mapping of insertions that influence daptomycin or pigment production
    • McHenney, M.A., and Baltz, R.H. (1996) Gene transfer and transposition mutagenesis in Streptomyces roseosporus: mapping of insertions that influence daptomycin or pigment production. Microbiology 142: 2363-2373.
    • (1996) Microbiology , vol.142 , pp. 2363-2373
    • McHenney, M.A.1    Baltz, R.H.2
  • 34
    • 0031963078 scopus 로고    scopus 로고
    • Molecular cloning and physical mapping of the daptomycin gene cluster from Streptomyces roseosporus
    • McHenney, M.A., Hosted, T.J., Dehoff, B.S., Rosteck, P.R., and Baltz, R.H. (1998) Molecular cloning and physical mapping of the daptomycin gene cluster from Streptomyces roseosporus. J Bacteriol 180: 143-151.
    • (1998) J Bacteriol , vol.180 , pp. 143-151
    • McHenney, M.A.1    Hosted, T.J.2    Dehoff, B.S.3    Rosteck, P.R.4    Baltz, R.H.5
  • 35
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin, J.L., and McMillan, F.M. (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12: 783-793.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 36
    • 21044448952 scopus 로고    scopus 로고
    • Daptomycin biosynthesis in Streptomyces roseosporus: Cloning and analysis of the gene cluster and revision of peptide stereochemistry
    • Miao, V., Coëffet-Le Gal, M.-F., Brian, P., Brost, R., Penn, J., Whiting, A., et al. (2005) Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry. Microbiology 151: 1507-1523.
    • (2005) Microbiology , vol.151 , pp. 1507-1523
    • Miao, V.1    Coëffet-Le Gal, M.-F.2    Brian, P.3    Brost, R.4    Penn, J.5    Whiting, A.6
  • 38
    • 33646092531 scopus 로고    scopus 로고
    • Genetic engineering in Streptomyces roseosporus to produce hybrid lipopeptide antibiotics
    • Miao, V., Coëffet-Le Gal, M.-F., Nguyen, K., Brian, P., Penn, J., Whiting, A., et al. (2006b) Genetic engineering in Streptomyces roseosporus to produce hybrid lipopeptide antibiotics. Chem Biol 13: 269-276.
    • (2006) Chem Biol , vol.13 , pp. 269-276
    • Miao, V.1    Coëffet-Le Gal, M.-F.2    Nguyen, K.3    Brian, P.4    Penn, J.5    Whiting, A.6
  • 39
    • 0029008357 scopus 로고
    • Integrative vectors for heterologous gene expression in Streptomyces spp.
    • Motamedi, H., Shafiee, A., and Cai, S.J. (1995) Integrative vectors for heterologous gene expression in Streptomyces spp. Gene 160: 25-31.
    • (1995) Gene , vol.160 , pp. 25-31
    • Motamedi, H.1    Shafiee, A.2    Cai, S.J.3
  • 40
    • 0345643323 scopus 로고    scopus 로고
    • Identification and analysis of the balhimycin biosynthetic gene cluster and its use for manipulating glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908
    • Pelzer, S., Sussmuth, R., Heckmann, D., Recktenwald, J., Huber, P., Jung, G., and Wohlleben, W. (1999) Identification and analysis of the balhimycin biosynthetic gene cluster and its use for manipulating glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908. Antimicrob Agents Chemother 43: 1565-1573.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1565-1573
    • Pelzer, S.1    Sussmuth, R.2    Heckmann, D.3    Recktenwald, J.4    Huber, P.5    Jung, G.6    Wohlleben, W.7
  • 43
    • 4544326782 scopus 로고    scopus 로고
    • PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa
    • Reimmann, C., Patel, H.M., Walsh, C.T., and Haas, D. (2004) PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa. J Bacteriol 186: 6367-6373.
    • (2004) J Bacteriol , vol.186 , pp. 6367-6373
    • Reimmann, C.1    Patel, H.M.2    Walsh, C.T.3    Haas, D.4
  • 44
    • 20544436705 scopus 로고    scopus 로고
    • Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes
    • Rink, R., Kuipers, A., de Boef, E., Leenhouts, K.J., Driessen, A.J., Moll, G.N., and Kuipers, O.P. (2005) Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes. Biochemistry 44: 8873-8882.
    • (2005) Biochemistry , vol.44 , pp. 8873-8882
    • Rink, R.1    Kuipers, A.2    De Boef, E.3    Leenhouts, K.J.4    Driessen, A.J.5    Moll, G.N.6    Kuipers, O.P.7
  • 45
    • 0022535425 scopus 로고
    • Utilization of ornithine and arginine as specific precursors of clavulanic acid
    • Romero, J., Liras, P., and Martin, J.F. (1986) Utilization of ornithine and arginine as specific precursors of clavulanic acid. Appl Environ Microbiol 52: 892-897.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 892-897
    • Romero, J.1    Liras, P.2    Martin, J.F.3
  • 46
    • 29244472119 scopus 로고    scopus 로고
    • Solution structure of daptomycin
    • Chorev, M., and Sawyer, T.K. (eds). Syracuse, NY: American Peptide Society, Springer Publishing
    • Rotondi, K., and Gierasch, L. (2003) Solution structure of daptomycin. In Peptide Revolution: Genomics, Proteomics and Therapeutics. Chorev, M., and Sawyer, T.K. (eds). Syracuse, NY: American Peptide Society, Springer Publishing, pp. 447-449.
    • (2003) Peptide Revolution: Genomics, Proteomics and Therapeutics , pp. 447-449
    • Rotondi, K.1    Gierasch, L.2
  • 47
    • 20344382979 scopus 로고    scopus 로고
    • A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution
    • Rotondi, K.S., and Gierasch, L.M. (2005) A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers 80: 374-385.
    • (2005) Biopolymers , vol.80 , pp. 374-385
    • Rotondi, K.S.1    Gierasch, L.M.2
  • 48
    • 0036176756 scopus 로고    scopus 로고
    • Regulation of the Streptomyces coelicolor calcium-dependent antibiotic by absA, encoding a cluster-linked two-component system
    • Ryding, N.J., Anderson, T.B., and Champness, W.C. (2002) Regulation of the Streptomyces coelicolor calcium-dependent antibiotic by absA, encoding a cluster-linked two-component system. J Bacteriol 184: 794-805.
    • (2002) J Bacteriol , vol.184 , pp. 794-805
    • Ryding, N.J.1    Anderson, T.B.2    Champness, W.C.3
  • 49
    • 0031943369 scopus 로고    scopus 로고
    • Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis
    • Schneider, A., and Marahiel, M.A. (1998) Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis. Arch Microbiol 169: 404-410.
    • (1998) Arch Microbiol , vol.169 , pp. 404-410
    • Schneider, A.1    Marahiel, M.A.2
  • 51
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer, D., Mootz, H.D., Linne, U., and Marahiel, M.A. (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
  • 52
    • 0037524493 scopus 로고    scopus 로고
    • Non-ribosomal peptides: From genes to products
    • Schwarzer, D., Finking, R., and Marahiel, M.A. (2003) Non-ribosomal peptides: from genes to products. Nat Prod Rep 20: 275-287.
    • (2003) Nat Prod Rep , vol.20 , pp. 275-287
    • Schwarzer, D.1    Finking, R.2    Marahiel, M.A.3
  • 53
    • 13744249199 scopus 로고    scopus 로고
    • Prerequisites for combinatorial biosynthesis: Evolution of hybrid NRPS/PKS gene clusters
    • Shen, B., Chen, M., Cheng, Y., Du, L., Edward, D.J., George, N.P., et al. (2005) Prerequisites for combinatorial biosynthesis: evolution of hybrid NRPS/PKS gene clusters. Ernst Schering Res Found Workshop 51: 107-126.
    • (2005) Ernst Schering Res Found Workshop , vol.51 , pp. 107-126
    • Shen, B.1    Chen, M.2    Cheng, Y.3    Du, L.4    Edward, D.J.5    George, N.P.6
  • 54
    • 1642496907 scopus 로고    scopus 로고
    • The biosynthesis of glycopeptide antibiotics - A model for complex, non-ribosomally synthesized, peptidic secondary metabolites
    • Sussmuth, R.D., and Wohlleben, W. (2004) The biosynthesis of glycopeptide antibiotics - a model for complex, non-ribosomally synthesized, peptidic secondary metabolites. Appl Microbiol Biotechnol 63: 344-350.
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 344-350
    • Sussmuth, R.D.1    Wohlleben, W.2
  • 55
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren, J., Svensson, L.A., and Liljas, A. (1994) Crystal structure of catechol O-methyltransferase. Nature 368: 354-358.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 57
    • 0035478654 scopus 로고    scopus 로고
    • Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines
    • Walsh, C.T., Chen, H., Keating, T.A., Hubbard, B.K., Losey, H.C., Luo, L., et al. (2001) Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines. Curr Opin Chem Biol 5: 525-534.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 525-534
    • Walsh, C.T.1    Chen, H.2    Keating, T.A.3    Hubbard, B.K.4    Losey, H.C.5    Luo, L.6
  • 58
    • 0030424714 scopus 로고    scopus 로고
    • Biosynthesis of acylpeptidolactones of the daptomycin type. A comparative analysis of peptide synthetases forming A21978C and A54145
    • Wessels, P., von Dohren, H., and Kleinkauf, H. (1996) Biosynthesis of acylpeptidolactones of the daptomycin type. A comparative analysis of peptide synthetases forming A21978C and A54145. Eur J Biochem 242: 665-673.
    • (1996) Eur J Biochem , vol.242 , pp. 665-673
    • Wessels, P.1    Von Dohren, H.2    Kleinkauf, H.3
  • 59
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor
    • Yeats, C., Bentley, S., and Bateman, A. (2003) New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor. BMC Microbiol 3: 3-20.
    • (2003) BMC Microbiol , vol.3 , pp. 3-20
    • Yeats, C.1    Bentley, S.2    Bateman, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.