A Biotin Biosynthesis Gene Restricted to Helicobacter

Hongkai Bi, Lei Zhu, Jia Jia, John E. Cronan

Research output: Contribution to journalArticle

Abstract

In most bacteria the last step in synthesis of the pimelate moiety of biotin is cleavage of the ester bond of pimeloyl-acyl carrier protein (ACP) methyl ester. The paradigm cleavage enzyme is Escherichia coli BioH which together with the BioC methyltransferase allows synthesis of the pimelate moiety by a modified fatty acid biosynthetic pathway. Analyses of the extant bacterial genomes showed that bioH is absent from many bioC-containing bacteria and is replaced by other genes. Helicobacter pylori lacks a gene encoding a homologue of the known pimeloyl-ACP methyl ester cleavage enzymes suggesting that it encodes a novel enzyme that cleaves this intermediate. We isolated the H. pylori gene encoding this enzyme, bioV, by complementation of an E. coli bioH deletion strain. Purified BioV cleaved the physiological substrate, pimeloyl-ACP methyl ester to pimeloyl-ACP by use of a catalytic triad, each member of which was essential for activity. The role of BioV in biotin biosynthesis was demonstrated using a reconstituted in vitro desthiobiotin synthesis system. BioV homologues seem the sole pimeloyl-ACP methyl ester esterase present in the Helicobacter species and their occurrence only in H. pylori and close relatives provide a target for development of drugs to specifically treat Helicobacter infections.

Original languageEnglish (US)
Article number21162
JournalScientific reports
Volume6
DOIs
StatePublished - Feb 12 2016

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A Biotin Biosynthesis Gene Restricted to Helicobacter'. Together they form a unique fingerprint.

  • Cite this