Merck

Closing in on complete pathways of biotin biosynthesis.

Molecular bioSystems (2011-03-26)
Steven Lin, John E Cronan
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Biotin, ≥99.0% (T)
Sigma-Aldrich
Biotin, tested according to Ph. Eur.
Sigma-Aldrich
Biotin, powder, BioReagent, suitable for cell culture, suitable for insect cell culture, suitable for plant cell culture, ≥99%
Sigma-Aldrich
Biotin, meets USP testing specifications
SAFC
BIOTIN
Biotin, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
Biotin, Vetec, reagent grade, ≥99%
Supelco
Biotin, certified reference material, TraceCERT®
USP
Biotin, United States Pharmacopeia (USP) Reference Standard
Supelco
Biotin, Pharmaceutical Secondary Standard; Certified Reference Material