The Enzymes of Biotin Dependent CO(2) Metabolism: What Structures Reveal about Their Reaction Mechanisms

Authors

Grover L. Waldrop, Louisiana State University
Hazel M. Holden, University of Wisconsin - Madison
Martin St. Maurice, Marquette UniversityFollow

Document Type

Article

Language

eng

Format of Original

23 p.

Publication Date

11-2012

Publisher

Wiley

Source Publication

Protein Science

Source ISSN

0961-8368

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.

Comments

Accepted version. Protein Science, Vol. 21, No. 11 (November, 2012): 1597-1619. Permalink. © 2012 Wiley-Blackwell. Used with permission.

Recommended Citation

Waldrop, Grover L.; Holden, Hazel M.; and Maurice, Martin St., "The Enzymes of Biotin Dependent CO(2) Metabolism: What Structures Reveal about Their Reaction Mechanisms" (2012). Biological Sciences Faculty Research and Publications. 119.
https://epublications.marquette.edu/bio_fac/119