Document Type
Article
Language
eng
Format of Original
19 p.
Publication Date
2010
Publisher
Bentham Open
Source Publication
The Open Enzyme Inhibition Journal
Source ISSN
1874-9402
Abstract
This review aims to discuss the varied types of inhibitors of biotin-dependent carboxylases, with an emphasis on the inhibitors of pyruvate carboxylase. Some of these inhibitors are physiologically relevant, in that they provide ways of regulating the cellular activities of the enzymes e.g. aspartate and prohibitin inhibition of pyruvate carboxylase. Most of the inhibitors that will be discussed have been used to probe various aspects of the structure and function of these enzymes. They target particular parts of the structure e.g. avidin – biotin, FTP – ATP binding site, oxamate – pyruvate binding site, phosphonoacetate – binding site of the putative carboxyphosphate intermediate.
Recommended Citation
Zeczycki, Tonya N.; Maurice, Martin St.; and Attwood, Paul V., "Inhibitors of Pyruvate Carboxylase" (2010). Biological Sciences Faculty Research and Publications. 356.
https://epublications.marquette.edu/bio_fac/356
Comments
Published version. The Open Enzyme Inhibition Journal, Vol. 3 (2010): 8-26. DOI. © 2010 Bentham Open. Used with permission.
This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/)