期刊
PROTEIN SCIENCE
卷 21, 期 11, 页码 1597-1619出版社
WILEY
DOI: 10.1002/pro.2156
关键词
biotin; vitamin H; vitamin B-7; biotin-dependent enzymes; CO2 metabolism; carboxylases; decarboxylases; transcarboxylases; ATP-grasp superfamily of enzymes; crotonase superfamily of enzymes
资金
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0841143] Funding Source: National Science Foundation
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.
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