Enzyme Architecture: The Activating Oxydianion Binding Domain for Orotidine 5′-Monophophate Decarboxylase
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States
Funder
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja4107513
Reference30 articles.
1. Insight into the Catalytic Mechanism of Orotidine 5′-phosphate Decarboxylase from Crystallography and Mutagenesis
2. Catalytic Proficiency: The Unusual Case of OMP Decarboxylase
3. A Proficient Enzyme
4. Yeast Orotidine-5‘-Phosphate Decarboxylase: Steady-State and Pre-Steady-State Analysis of the Kinetic Mechanism of Substrate Decarboxylation
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4. Enzyme Architecture: Erection of Active Orotidine 5′-Monophosphate Decarboxylase by Substrate-Induced Conformational Changes;Journal of the American Chemical Society;2017-10-23
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