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The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.

Protein science : a publication of the Protein Society (2012-09-13)
Grover L Waldrop, Hazel M Holden, Martin St Maurice
ABSTRACT

Biotin is the major cofactor involved in carbon dioxide metabolism. Indeed, biotin-dependent enzymes are ubiquitous in nature and are involved in a myriad of metabolic processes including fatty acid synthesis and gluconeogenesis. The cofactor, itself, is composed of a ureido ring, a tetrahydrothiophene ring, and a valeric acid side chain. It is the ureido ring that functions as the CO₂ carrier. A complete understanding of biotin-dependent enzymes is critically important for translational research in light of the fact that some of these enzymes serve as targets for anti-obesity agents, antibiotics, and herbicides. Prior to 1990, however, there was a dearth of information regarding the molecular architectures of biotin-dependent enzymes. In recent years there has been an explosion in the number of three-dimensional structures reported for these proteins. Here we review our current understanding of the structures and functions of biotin-dependent enzymes. In addition, we provide a critical analysis of what these structures have and have not revealed about biotin-dependent catalysis.

MATERIALS
Product Number
Brand
Product Description

Supelco
Biotin, certified reference material, TraceCERT®
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
Sigma-Aldrich
Biotin, tested according to Ph. Eur.
Sigma-Aldrich
Biotin, ≥99.0% (T)
Biotin, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
Biotin, Vetec, reagent grade, ≥99%
Supelco
Biotin, Pharmaceutical Secondary Standard; Certified Reference Material
SAFC
BIOTIN
USP
Biotin, United States Pharmacopeia (USP) Reference Standard