Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation

S. V. Taylor, N. L. Kelleher, C. Kinsland, H. J. Chiu, C. A. Costello, A. D. Backstrom, F. W. McLafferty, T. P. Begley*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

135 Scopus citations

Abstract

ThiFSGH and ThiI are required for the biosynthesis of the thiazole moiety of thiamin in Escherichia coli. The overproduction, purification, and characterization of ThiFS and the identification of two of the early steps in the biosynthesis of the thiazole moiety of thiamin are described here. ThiS isolated from E. coli thiI+ is posttranslationally modified by converting the carboxylic acid group of the thiocarboxylate because ThiS isolated from a thiI- strain does not contain this modification. ThiF catalyzes the adenylation by ATP of the carboxyl-terminal glycine of ThiS. This reaction is likely to be involved in the activation of ThiS for sulfur transfer from cysteine or from a cysteine-derived sulfur donor.

Original languageEnglish (US)
Pages (from-to)16555-16560
Number of pages6
JournalJournal of Biological Chemistry
Volume273
Issue number26
DOIs
StatePublished - Jun 26 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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