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An oxidation domain in the blmiii non-ribosomal peptide synthetase probably catalyzing thiazole formation in the biosynthesis of the anti-tumor drug bleomycin in streptomyces verticillus atcc15003

Academic Article
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Overview

authors

  • Du, L. C.
  • Chen, M.
  • Sanchez, C.
  • Shen, Ben

publication date

  • August 2000

journal

  • FEMS Microbiology Letters  Journal

abstract

  • We have previously proposed that the BlmIV and BlmIII non-ribosomal peptide synthetases are involved in the formation of the bithiazole moiety of the anti-tumor drug bleomycin in Streptomyces verticillus ATCC15003. We report here the identification and characterization of an oxidation domain in BlmIII. The oxidation domain shows local homology to a family of oxidoreductases and is present in all thiazole-forming non-ribosomal peptide synthetase modules known to date. Both the blmIII-Ox domain and blmIII gene were expressed in Escherichia coli, and the resulting BlmIII-Ox and BlmIII proteins were purified to homogeneity. The oxidation domain contains one molar equivalent of non-covalently bound FMN as a prosthetic group. These results provide experimental evidence for an oxidation domain within non-ribosomal peptide synthetases, suggesting that BlmIII-Ox probably catalyzes the thiazoline to thiazole oxidation in bleomycin biosynthesis.

subject areas

  • Amino Acid Sequence
  • Bleomycin
  • Catalysis
  • Molecular Sequence Data
  • Peptide Synthases
  • Sequence Alignment
  • Streptomyces
  • Substrate Specificity
  • Thiazoles
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Research

keywords

  • Streptomyces verticillus
  • biosynthesis
  • bleomycin
  • non-ribosomal peptide synthetase
  • oxidation domain
  • thiazole
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Identity

International Standard Serial Number (ISSN)

  • 0378-1097

Digital Object Identifier (DOI)

  • 10.1111/j.1574-6968.2000.tb09225.x

PubMed ID

  • 10930733
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Additional Document Info

start page

  • 171

end page

  • 175

volume

  • 189

issue

  • 2

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