Orotidine 5′-Monophosphate Decarboxylase: Transition State Stabilization from Remote Protein–Phosphodianion Interactions
作者： Tina L. Amyes , Shonoi A. Ming , Lawrence M. Goldman , B. McKay Wood , Bijoy J. Desai
DOI: 10.1021/BI300585E
关键词: Reaction rate constant 、 Stereochemistry 、 Substrate (chemistry) 、 Enzyme 、 Orotic acid 、 Side chain 、 Decarboxylation 、 Orotidine 、 Chemistry 、 Mutant
摘要: Mutants of orotidine 5′-monophosphate decarboxylase containing all possible single (Q215A, Y217F, and R235A), double, triple substitutions the side chains that interact with phosphodianion group substrate have been prepared. Essentially entire effect these mutations on decarboxylation truncated neutral 1-(β-d-erythrofuranosyl)orotic acid lacks a is expressed as decrease in third-order rate constant for activation by phosphite dianion. The results are consistent model which binding interactions utilized to stabilize rare closed enzyme form exhibits high catalytic activity decarboxylation.
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