Jump to main content
Jump to site search

Issue 6, 2011
Previous Article Next Article

Closing in on complete pathways of biotin biosynthesis

Author affiliations


Biotin is an enzyme cofactor indispensable to metabolic fixation of carbon dioxide in all three domains of life. Although the catalytic and physiological roles of biotin have been well characterized, the biosynthesis of biotin remains to be fully elucidated. Studies in microbes suggest a two-stage biosynthetic pathway in which a pimelate moiety is synthesized and used to begin assembly of the biotin bicyclic ring structure. The enzymes involved in the bicyclic ring assembly have been studied extensively. In contrast the synthesis of pimelate, a seven carbon α,ω-dicarboxylate, has long been an enigma. Support for two different routes of pimelate synthesis has recently been obtained in Escherichia coli and Bacillus subtilis. The E. coli BioC–BioH pathway employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes whereas the B. subtilis BioI–BioW pathway utilizes oxidative cleavage of fatty acyl chains. Both pathways produce the pimelate thioester precursor essential for the first step in assembly of the fused rings of biotin. The enzymatic mechanisms and biochemical strategies of these pimelate synthesis models will be discussed in this review.

Graphical abstract: Closing in on complete pathways of biotin biosynthesis

Back to tab navigation

Article information

21 Jan 2011
02 Mar 2011
First published
24 Mar 2011

Mol. BioSyst., 2011,7, 1811-1821
Article type
Review Article

Closing in on complete pathways of biotin biosynthesis

S. Lin and J. E. Cronan, Mol. BioSyst., 2011, 7, 1811
DOI: 10.1039/C1MB05022B

Search articles by author