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Volumn 407, Issue 6801, 2000, Pages 215-218

Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase

Author keywords

[No Author keywords available]

Indexed keywords

GRAMICIDIN; SYNTHETASE; TYROCIDINE;

EID: 0034648798     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35025116     Document Type: Article
Times cited : (279)

References (24)
  • 1
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations and mutations
    • Cane, D. E., Walsh, C. T. & Khosla, C. Harnessing the biosynthetic code: combinations, permutations and mutations. Science 282, 63-68 (1998).
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 2
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel, M. A., Stachelhaus, T. & Mootz, H. D. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97, 2651-2674 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 3
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily-the phosphopantetheinyl-transferases
    • Lambalot, R. H. et al. A new enzyme superfamily-the phosphopantetheinyl-transferases. Chem. Biol. 3, 923-936 (1996).
    • (1996) Chem. Biol. , vol.3 , pp. 923-936
    • Lambalot, R.H.1
  • 4
    • 0028141817 scopus 로고
    • Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi
    • Lawson, D. M. et al. Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry 33, 9382-9388 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9382-9388
    • Lawson, D.M.1
  • 5
    • 0029758922 scopus 로고    scopus 로고
    • Conversion of serine-114 to cysteme-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi
    • Li, J., Szitlner, R., Derewenda, Z. S. & Meighen, E. A. Conversion of serine-114 to cysteme-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi. Biochemistry 35, 9967-9973 (1996).
    • (1996) Biochemistry , vol.35 , pp. 9967-9973
    • Li, J.1    Szitlner, R.2    Derewenda, Z.S.3    Meighen, E.A.4
  • 6
    • 0033150199 scopus 로고    scopus 로고
    • Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. coli EntF catalyses both elongation and cyclolactonization
    • Shaw-Reid, C. A. et al. Assembly line enzymology by multimodular nonribosomal peptide synthetases: the thioesterase domain of E. coli EntF catalyses both elongation and cyclolactonization. Chem. Biol. 6, 385-400 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 385-400
    • Shaw-Reid, C.A.1
  • 7
    • 0029092263 scopus 로고
    • The thioesterase domain of the erythromycin-producing polyketide synthase: Mechanistic studies in vitro to investigate its mode of action and substrate specificity
    • Aggarwal, R., Caffrey, P., Leadlay, P. F., Smith, C. J. & Staunton, J. The thioesterase domain of the erythromycin-producing polyketide synthase: mechanistic studies in vitro to investigate its mode of action and substrate specificity. J. Chem. Soc. Chem. Comm. 15, 1519-1520 (1995).
    • (1995) J. Chem. Soc. Chem. Comm. , vol.15 , pp. 1519-1520
    • Aggarwal, R.1    Caffrey, P.2    Leadlay, P.F.3    Smith, C.J.4    Staunton, J.5
  • 8
    • 0033079834 scopus 로고    scopus 로고
    • Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase
    • Gokhale, R. S., Hunziker, D., Cane, D. E. & Khosla, C. Mechanism and specificity of the terminal thioesterase domain from the erythromycin polyketide synthase. Chem. Biol. 6, 117-125 (1998).
    • (1998) Chem. Biol. , vol.6 , pp. 117-125
    • Gokhale, R.S.1    Hunziker, D.2    Cane, D.E.3    Khosla, C.4
  • 9
    • 0029027352 scopus 로고
    • Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage
    • Cortes, J. et al. Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage. Science 268, 1487-1489 (1995).
    • (1995) Science , vol.268 , pp. 1487-1489
    • Cortes, J.1
  • 10
    • 0030723673 scopus 로고    scopus 로고
    • Gain of function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone
    • Kao, C. M. et al. Gain of function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone. J. Am. Chem. Soc. 119, 11339-11340 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11339-11340
    • Kao, C.M.1
  • 11
    • 0030875774 scopus 로고    scopus 로고
    • Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase
    • Jacobsen, J. R., Hutchinson, C. R., Cane, D. E. & Khosla, C. Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase. Science 277, 367-369 (1997).
    • (1997) Science , vol.277 , pp. 367-369
    • Jacobsen, J.R.1    Hutchinson, C.R.2    Cane, D.E.3    Khosla, C.4
  • 12
    • 0033515090 scopus 로고    scopus 로고
    • Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel "unnatural" natural products
    • McDaniel, R. et al. Multiple genetic modifications of the erythromycin polyketide synthase to produce a library of novel "unnatural" natural products. Proc. Natl Acad. Sci. USA 96, 1846-1851 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1846-1851
    • McDaniel, R.1
  • 13
    • 0034141564 scopus 로고    scopus 로고
    • Formation of functional heterologous complexes using subunits from the picromycin, erythromycin and oleandomycin polyketide synthases
    • Tang, L., Fu, H. & McDaniel, R. Formation of functional heterologous complexes using subunits from the picromycin, erythromycin and oleandomycin polyketide synthases. Chem. Biol. 7, 77-84 (2000).
    • (2000) Chem. Biol. , vol.7 , pp. 77-84
    • Tang, L.1    Fu, H.2    McDaniel, R.3
  • 14
    • 0034598743 scopus 로고    scopus 로고
    • Alternative modular polyketide synthase expression controls macrolactone structure
    • Xue, Y. & Sherman, D. H. Alternative modular polyketide synthase expression controls macrolactone structure. Nature 403, 571-575 (2000).
    • (2000) Nature , vol.403 , pp. 571-575
    • Xue, Y.1    Sherman, D.H.2
  • 15
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • Stachelhaus, T., Schneider, A. & Marahiel, M. A. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science 269, 69-72 (1995).
    • (1995) Science , vol.269 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 17
    • 0034705130 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases by module and domain fusions
    • Mootz, H. D., Schwarzer, D. & Marahiel, M. A. Construction of hybrid peptide synthetases by module and domain fusions. Proc. Natl Acad. Sci. USA 97, 5848-5853 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5848-5853
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 18
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonrinosomal peptide synthesis
    • Belshaw, P. J., Walsh, C. T. & Stachelhaus, T. Aminoacyl-CoAs as probes of condensation domain selectivity in nonrinosomal peptide synthesis. Science 284, 486-489 (1999).
    • (1999) Science , vol.284 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3
  • 19
    • 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. The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179, 6843-6850 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 20
    • 0014937563 scopus 로고
    • Isolation of enzyme-bound peptide intermediates in tyrocidine biosynthesis
    • Roskoski, R., Kleinkauf, H., Gevers, W. & Lipmann, F. Isolation of enzyme-bound peptide intermediates in tyrocidine biosynthesis. Biochemistry 9, 4846-4851 (1970).
    • (1970) Biochemistry , vol.9 , pp. 4846-4851
    • Roskoski, R.1    Kleinkauf, H.2    Gevers, W.3    Lipmann, F.4
  • 21
    • 0024470350 scopus 로고
    • Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1 gene
    • Hori, K. et al. Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1 gene. J. Biochem. (Tokyo) 106, 639-645 (1989).
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 639-645
    • Hori, K.1
  • 22
    • 0026588298 scopus 로고
    • Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay, K., Krause, M. & Marahiel, M. A. Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6, 529-546 (1992).
    • (1992) Mol. Microbiol. , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 23
    • 0034728553 scopus 로고    scopus 로고
    • Tolal syntheses of thiocoraline and BE-22179: Establishment of relative and absolute stereochemistry
    • Boger, D. L. & Ichikawa, S. Tolal syntheses of thiocoraline and BE-22179: establishment of relative and absolute stereochemistry. J. Am. Chem. Soc. 122, 2956-2957 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2956-2957
    • Boger, D.L.1    Ichikawa, S.2
  • 24
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • Jackson, D. Y. et al. A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266, 243-247 (1994).
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.