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The enzymes of biotin dependent CO 2 metabolism: What structures reveal about their reaction mechanisms
Author(s) -
Waldrop Grover L.,
Holden Hazel M.,
Maurice Martin St.
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2156
Subject(s) - biotin , cofactor , enzyme , tetrahydrothiophene , biochemistry , chemistry , valeric acid , ring (chemistry) , stereochemistry , acetic acid , organic chemistry
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 CO 2 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.