A canonical biotin synthesis enzyme, 8-amino-7- oxononanoate synthase (BioF), utilizes different acyl chain donors in Bacillus subtilis and Escherichia coli

Miglena Manandhar, John E. Cronan

Research output: Contribution to journalArticle

Abstract

BioF (8-amino-7-oxononanoate synthase) is a strictly conserved enzyme that catalyzes the first step in assembly of the fused heterocyclic rings of biotin. The BioF acyl chain donor has long been thought to be pimeloyl-CoA. Indeed, in vitro the Escherichia coli and Bacillus sphaericus enzymes have been shown to condense pimeloyl-CoA with L-alanine in a pyridoxal 5=-phosphate-dependent reaction with concomitant CoA release and decarboxylation of L-alanine. However, recent in vivo studies of E. coli and Bacillus subtilis suggested that the BioF proteins of the two bacteria could have different specificities for pimelate thioesters in that E. coli BioF may utilize either pimeloyl coenzyme A (CoA) or the pimelate thioester of the acyl carrier protein (ACP) of fatty acid synthesis. In contrast, B. subtilis BioF seemed likely to be specific for pimeloyl-CoA and unable to utilize pimeloyl-ACP. We now report genetic and in vitro data demonstrating that B. subtilis BioF specifically utilizes pimeloyl-CoA.

Original languageEnglish (US)
Article numbere02084-17
JournalApplied and environmental microbiology
Volume84
Issue number1
DOIs
StatePublished - Jan 1 2018

Keywords

  • BioF
  • BioW
  • Biotin
  • Pimelic acid

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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