Orotidine 5′-Monophosphate Decarboxylase: Transition State Stabilization from Remote Protein–Phosphodianion Interactions
Biochemistry2012Vol. 51(23), pp. 4630–4632
Citations Over TimeTop 10% of 2012 papers
Tina L. Amyes, Shonoi A. Ming, Lawrence M. Goldman, B.M. Wood, B. Desai, J.A. Gerlt, John P. Richard
Abstract
Mutants of orotidine 5'-monophosphate decarboxylase containing all possible single (Q215A, Y217F, and R235A), double, and triple substitutions of the side chains that interact with the phosphodianion group of the substrate orotidine 5'-monophosphate have been prepared. Essentially the entire effect of these mutations on the decarboxylation of the truncated neutral substrate 1-(β-d-erythrofuranosyl)orotic acid that lacks a phosphodianion group is expressed as a decrease in the third-order rate constant for activation by phosphite dianion. The results are consistent with a model in which phosphodianion binding interactions are utilized to stabilize a rare closed enzyme form that exhibits a high catalytic activity for decarboxylation.
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