An oxidation domain in the BlmIII non-ribosomal peptide synthetase probably catalyzing thiazole formation in the biosynthesis of the anti-tumor drug bleomycin inStreptomyces verticillusATCC15003-Reference-Cited by-同舟云学术

An oxidation domain in the BlmIII non-ribosomal peptide synthetase probably catalyzing thiazole formation in the biosynthesis of the anti-tumor drug bleomycin inStreptomyces verticillusATCC15003

Published:2000-08 Issue:2 Volume:189 Page:171-175
ISSN:0378-1097
Container-title:FEMS Microbiology Letters
language:en
Short-container-title:

Author:

Du Liangcheng,Chen Mei,SÃ¡nchez CÃ©sar,Shen Ben

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

Link

http://academic.oup.com/femsle/article-pdf/189/2/171/19116935/189-2-171.pdf

Reference15 articles.

1. Modular peptide synthetases involved in nonribosomal peptide sysnthesis;Marahiel;Chem. Rev.,1997

2. Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain;Stachelhaus;J. Biol. Chem.,1998

3. The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: molecular characterization of three multi-modular peptide synthetases;Konz;Chem. Biol.,1997

4. The nonribosomal peptide synthetase HMWP2 forms a thiozoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis;Gehring;Biochemistry,1998

5. New lessons for combinatorial biosynthesis from myxobacteria. The myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1;Silakowski;J. Biol. Chem.,1999

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