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Volumn 6, Issue 8, 1999, Pages 507-517

Identification and characterization of a type II peptidyl carrier protein from the bleomycin producer Streptomyces verticillus ATCC 15003

Author keywords

Biosynthesis; Bleomycin; Nonribosomal peptide synthetase; Peptidyl carrier protein; Streptomyces verticillus

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA; STREPTOMYCES; STREPTOMYCES VERTICILLUS;

EID: 0033179342     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80083-0     Document Type: Article
Times cited : (43)

References (45)
  • 1
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D.E., Walsh, C.T. & Khosla, C. (1998). Harnessing the biosynthetic code: Combinations, permutations, and mutations. Science 282, 63-68.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 2
    • 0029921158 scopus 로고    scopus 로고
    • A nonribosomal system of peptide biosynthesis
    • Kleinkauf, H. & von Döhren, H. (1996). A nonribosomal system of peptide biosynthesis. Eur. J. Biochem. 236, 335-351.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 335-351
    • Kleinkauf, H.1    Von Döhren, H.2
  • 3
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel, M.A., Stachelhaus, T. & Mootz, H.D. (1997). Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97, 2651-2673.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2673
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 5
    • 0024315871 scopus 로고
    • Fatty acid synthase, a proficient multifunctional enzyme
    • Wakil, S.J. (1989). Fatty acid synthase, a proficient multifunctional enzyme. Biochemistry 28, 4523-4530.
    • (1989) Biochemistry , vol.28 , pp. 4523-4530
    • Wakil, S.J.1
  • 6
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood, D.A. (1997). Genetic contributions to understanding polyketide synthases. Chem Rev. 97, 2465-2497.
    • (1997) Chem Rev. , vol.97 , pp. 2465-2497
    • Hopwood, D.A.1
  • 7
    • 0030292865 scopus 로고    scopus 로고
    • Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases
    • Stachelhaus, T., Hüser, A. & Marahiel, M.A. (1996). Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases. Chem. Biol. 3, 913-921.
    • (1996) Chem. Biol. , vol.3 , pp. 913-921
    • Stachelhaus, T.1    Hüser, A.2    Marahiel, M.A.3
  • 8
    • 0029978534 scopus 로고    scopus 로고
    • The multiple carrier model of nonribosomal peptide biosynthesis at modular multienzymatic templates
    • Stein, T., et al., & Morris, H.R. (1996). The multiple carrier model of nonribosomal peptide biosynthesis at modular multienzymatic templates. J. Biol. Chem. 271, 15428-15435.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15428-15435
    • Stein, T.1    Morris, H.R.2
  • 9
    • 0028908601 scopus 로고
    • Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA
    • Stachlhaus, T., & Marahiel, M.A. (1995). Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA. J. Biol. Chem. 270, 6163-6169.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6163-6169
    • Stachlhaus, T.1    Marahiel, M.A.2
  • 10
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis, catalytic role of the condensation domain
    • Stachlhaus, T., Mootz, H.D., Bergendahl, V., & Marahiel, M.A. (1998). Peptide bond formation in nonribosomal peptide biosynthesis, catalytic role of the condensation domain. J. Biol. Chem. 273, 22773-22781.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachlhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 11
    • 0028837014 scopus 로고
    • Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis
    • Stachelhaus, T., & Marahiel, M.A. (1995). Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis. FEMS Microbiol. Lett. 125, 3-14.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 3-14
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 12
    • 0028503009 scopus 로고
    • A general approach for identifying and cloning peptide synthetase genes
    • Turgay, K. & Marahiel, M.A. (1994). A general approach for identifying and cloning peptide synthetase genes. Pept. Res. 7, 238-241.
    • (1994) Pept. Res. , vol.7 , pp. 238-241
    • Turgay, K.1    Marahiel, M.A.2
  • 13
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin
    • Quadri, L.E.N., Sello, J., Keating, T.A., Paul, H.W. & Walsh, C.T. (1998). Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5, 631-645.
    • (1998) Chem. Biol. , vol.5 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Paul, H.W.4    Walsh, C.T.5
  • 14
    • 0031459595 scopus 로고    scopus 로고
    • The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: Molecular characterization of three multi-modular peptide synthetases
    • Konz, D., Klens, A., Schorgendorfer, K. & Marahiel, M.A. (1997) The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: Molecular characterization of three multi-modular peptide synthetases. Chem. Biol. 4, 927-937.
    • (1997) Chem. Biol. , vol.4 , pp. 927-937
    • Konz, D.1    Klens, A.2    Schorgendorfer, K.3    Marahiel, M.A.4
  • 16
    • 0031046794 scopus 로고    scopus 로고
    • Substrate specificity of hybrid modules from peptide synthetases
    • Elsner, A., et al., & Bernhard, F. (1997). Substrate specificity of hybrid modules from peptide synthetases. J. Biol. Chem. 272, 4814-4819.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4814-4819
    • Elsner, A.1    Bernhard, F.2
  • 17
    • 0032562142 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
    • Gehring, A.M., Mori, I. & Walsh, C.T. (1998). Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 37, 2648-2659.
    • (1998) Biochemistry , vol.37 , pp. 2648-2659
    • Gehring, A.M.1    Mori, I.2    Walsh, C.T.3
  • 18
    • 0032544193 scopus 로고    scopus 로고
    • The nonribosomal peptide synthetase HMWP2 forms a thiozoline ring during biogensis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis
    • Gehring, A.M., Mori, I., Perry, R.D. & Walsh, C.T. (1998). The nonribosomal peptide synthetase HMWP2 forms a thiozoline ring during biogensis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 37, 11637-11650.
    • (1998) Biochemistry , vol.37 , pp. 11637-11650
    • Gehring, A.M.1    Mori, I.2    Perry, R.D.3    Walsh, C.T.4
  • 19
    • 0032502031 scopus 로고    scopus 로고
    • Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase
    • Weinreb, P.H., Quadri, L.E.N., Walsh, C.T. & Zuber, P. (1998). Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase. Biochemistry 37, 1575-1584.
    • (1998) Biochemistry , vol.37 , pp. 1575-1584
    • Weinreb, P.H.1    Quadri, L.E.N.2    Walsh, C.T.3    Zuber, P.4
  • 20
    • 0030669091 scopus 로고    scopus 로고
    • The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains
    • Mootz, H.D. & Marahiel, M.A. (1997). The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179, 6843-6850.
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 21
    • 0029048654 scopus 로고
    • Characterization of tyrocidine synthetases 1 (TY1): Requirement of posttranslational modification for peptide biosynthesis
    • Pfeifer, E., Pavela-Francis, M., von Döhren, H. & Kleinkauf, H. (1995). Characterization of tyrocidine synthetases 1 (TY1): Requirement of posttranslational modification for peptide biosynthesis. Biochemistry 34, 7450-7459.
    • (1995) Biochemistry , vol.34 , pp. 7450-7459
    • Pfeifer, E.1    Pavela-Francis, M.2    Von Döhren, H.3    Kleinkauf, H.4
  • 22
    • 0027996536 scopus 로고
    • Bacterial expression of catalytically active fragments of the multifunctional enzyme enniatin synthetase
    • Haese, A., Pieper, R., von Ostrowski, T. & Zocher, R. (1994). Bacterial expression of catalytically active fragments of the multifunctional enzyme enniatin synthetase. J. Mol. Biol. 243, 116-122.
    • (1994) J. Mol. Biol. , vol.243 , pp. 116-122
    • Haese, A.1    Pieper, R.2    Von Ostrowski, T.3    Zocher, R.4
  • 23
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily - the phosphopantetheinyl transferases
    • Lambalot, R.H., et al., & Walsh, C.T. (1996). A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3, 923-936.
    • (1996) Chem. Biol. , vol.3 , pp. 923-936
    • Lambalot, R.H.1    Walsh, C.T.2
  • 24
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri, L.E.N., et al., & Walsh, C.T. (1998). Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37, 1585-1595.
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.N.1    Walsh, C.T.2
  • 25
    • 0030936547 scopus 로고    scopus 로고
    • Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase
    • Gehring, A.M., Lambalot, R.H., Vogel, K.W., Drueckhammer, D.G. & Walsh, C.T. (1996). Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase. Chem. Biol. 4, 17-24.
    • (1996) Chem. Biol. , vol.4 , pp. 17-24
    • Gehring, A.M.1    Lambalot, R.H.2    Vogel, K.W.3    Drueckhammer, D.G.4    Walsh, C.T.5
  • 26
    • 0031105254 scopus 로고    scopus 로고
    • Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with a phosphopantetheinyl transferase
    • Ku, J., Mirmira, R.G., Liu, L., & Santi, D.V. (1997). Expression of a functional non-ribosomal peptide synthetase module in Escherichia coli by coexpression with a phosphopantetheinyl transferase. Chem. Biol. 4, 203-207.
    • (1997) Chem. Biol. , Issue.4 , pp. 203-207
    • Ku, J.1    Mirmira, R.G.2    Liu, L.3    Santi, D.V.4
  • 27
    • 0032830741 scopus 로고    scopus 로고
    • Bleomycin biosynthesis in Streptomyces verticillus ATCC15003: A model of hybrid peptide and polyketide biosynthesis
    • Shen, B., Du, L., Sanchez, C., Chen, M. & Edwards, D.J. (1999). Bleomycin biosynthesis in Streptomyces verticillus ATCC15003: A model of hybrid peptide and polyketide biosynthesis. Bioorg. Chem. 27, 155-171.
    • (1999) Bioorg. Chem. , vol.27 , pp. 155-171
    • Shen, B.1    Du, L.2    Sanchez, C.3    Chen, M.4    Edwards, D.J.5
  • 28
    • 0028575322 scopus 로고
    • Characterization by molecular cloning of two genes from Streptomyces verticillus encoding resistance to bleomycin
    • Sugiyama, M., et al., & Davies, J. (1994). Characterization by molecular cloning of two genes from Streptomyces verticillus encoding resistance to bleomycin. Gene 151, 11-16.
    • (1994) Gene , vol.151 , pp. 11-16
    • Sugiyama, M.1    Davies, J.2
  • 29
    • 0028555351 scopus 로고
    • Gene organization in the bleomycin-resistance region of the producer organism Streptomyces verticillus
    • Calcutt, M.J. & Schmidt, F.J. (1994). Gene organization in the bleomycin-resistance region of the producer organism Streptomyces verticillus. Gene 151, 17-21.
    • (1994) Gene , vol.151 , pp. 17-21
    • Calcutt, M.J.1    Schmidt, F.J.2
  • 30
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S.F., et al., & Lipman, D.J. (1997). Gapped PSI and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Lipman, D.J.2
  • 32
    • 0028882690 scopus 로고
    • Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase
    • Lambalot, R.H. & Walsh, C.T. (1995). Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 270, 24658-24661.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24658-24661
    • Lambalot, R.H.1    Walsh, C.T.2
  • 33
    • 0030936596 scopus 로고    scopus 로고
    • Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins
    • Cox, R.J., et al., & Simpson, T.J. (1997). Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins. FEBS Lett. 405, 267-272.
    • (1997) FEBS Lett. , vol.405 , pp. 267-272
    • Cox, R.J.1    Simpson, T.J.2
  • 34
    • 0030880889 scopus 로고    scopus 로고
    • Utilization of enzymatically phosphopantetheinylated acyl carrier proteins and acetyl-acyl carrier proteins by the actinorhodin polyketide synthase
    • Carreras, C.W., Gehring, A.M., Walsh, C.T., & Khosla, C. (1997). Utilization of enzymatically phosphopantetheinylated acyl carrier proteins and acetyl-acyl carrier proteins by the actinorhodin polyketide synthase. Biochemistry 36, 11757-11761.
    • (1997) Biochemistry , vol.36 , pp. 11757-11761
    • Carreras, C.W.1    Gehring, A.M.2    Walsh, C.T.3    Khosla, C.4
  • 35
    • 0031689645 scopus 로고    scopus 로고
    • Characterization of a novel acyl carrier protein, RkpF, encoded by an operon involved in capsular polysaccharide biosynthesis in Sinorhizobium meliloti
    • Epple, G., van der Drift, K.M.G.M., Thomas-Oates, J.E. & Geiger, O. (1998). Characterization of a novel acyl carrier protein, RkpF, encoded by an operon involved in capsular polysaccharide biosynthesis in Sinorhizobium meliloti. J. Bacteriol. 180, 4950-4954.
    • (1998) J. Bacteriol. , vol.180 , pp. 4950-4954
    • Epple, G.1    Van Der Drift, K.M.G.M.2    Thomas-Oates, J.E.3    Geiger, O.4
  • 36
    • 0025991057 scopus 로고
    • A novel highly unsaturated fatty acid moiety of lipo-oligosaccharide signals determines host specificity of rhizobium
    • Spaink, H.P., et al., & Lugtenberg, B.J.J. (1991). A novel highly unsaturated fatty acid moiety of lipo-oligosaccharide signals determines host specificity of rhizobium. Nature 354, 125-130.
    • (1991) Nature , vol.354 , pp. 125-130
    • Spaink, H.P.1    Lugtenberg, B.J.J.2
  • 37
    • 0026520361 scopus 로고
    • Isolation and characterization of sfp: A gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis
    • Nakano, M.M., Corbell, N., Besson, J. & Zuber, P. (1992). Isolation and characterization of sfp: A gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis. Mol. Gen. Genet. 232, 313-321.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 313-321
    • Nakano, M.M.1    Corbell, N.2    Besson, J.3    Zuber, P.4
  • 38
    • 0016417481 scopus 로고
    • Tyrocidine synthetase system
    • Lee, S. & Lipmann, F. (1970). Tyrocidine synthetase system. Methods Enzymol. 43, 585-602.
    • (1970) Methods Enzymol. , vol.43 , pp. 585-602
    • Lee, S.1    Lipmann, F.2
  • 39
    • 0027908038 scopus 로고
    • Enzymatic synthesis of a bacterial polyketide from acetyl and malonyl coenzyme A
    • Shen, B. & Hutchinson, C.R. (1993). Enzymatic synthesis of a bacterial polyketide from acetyl and malonyl coenzyme A. Science 262, 1535-1540.
    • (1993) Science , vol.262 , pp. 1535-1540
    • Shen, B.1    Hutchinson, C.R.2
  • 40
    • 0032474472 scopus 로고    scopus 로고
    • Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis
    • Bao, W., Wendt-Pienkowski, E. & Hutchinson, C.R. (1998). Reconstitution of the iterative type II polyketide synthase for tetracenomycin F2 biosynthesis. Biochemistry 37, 8132-8138.
    • (1998) Biochemistry , vol.37 , pp. 8132-8138
    • Bao, W.1    Wendt-Pienkowski, E.2    Hutchinson, C.R.3
  • 41
    • 0032562124 scopus 로고    scopus 로고
    • Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase
    • Carreras, C.W. & Khosla, C. (1998). Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. Biochemistry 37, 2084-2088.
    • (1998) Biochemistry , vol.37 , pp. 2084-2088
    • Carreras, C.W.1    Khosla, C.2
  • 42
    • 0028982844 scopus 로고
    • Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis
    • Perego, M., Glaser, P., Minutello, A., Strauch, M.A., Leopold, K. & Fischer, W. (1995). Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. J. Biol. Chem. 270, 15598-15606.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15598-15606
    • Perego, M.1    Glaser, P.2    Minutello, A.3    Strauch, M.A.4    Leopold, K.5    Fischer, W.6
  • 43
    • 0029997792 scopus 로고    scopus 로고
    • The D-alanyl carrier protein in Lactobacillus casei: Cloning, sequencing, and expression of dltC
    • Debabov, D.V., Heaton, M.P., Zhang, O., Stewart, K.D., Lambalot, R.H., & Neuhaus, F.C. (1996). The D-alanyl carrier protein in Lactobacillus casei: Cloning, sequencing, and expression of dltC. J. Bacteriol. 178, 3869-3876.
    • (1996) J. Bacteriol. , vol.178 , pp. 3869-3876
    • Debabov, D.V.1    Heaton, M.P.2    Zhang, O.3    Stewart, K.D.4    Lambalot, R.H.5    Neuhaus, F.C.6
  • 44
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • Stachlhaus, T., Schneider, A., & Marahiel, M.A. (1995). Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science 269, 69-72.
    • (1995) Science , vol.269 , pp. 69-72
    • Stachlhaus, T.1    Schneider, A.2    Marahiel, M.A.3


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