Unknown

Dataset Information

0

Orotidine 5'-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions.


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-(?-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.

SUBMITTER: Amyes TL 

PROVIDER: S-EPMC3431445 | BioStudies | 2012-01-01

REPOSITORIES: biostudies

Similar Datasets

2014-01-01 | S-EPMC4227808 | BioStudies
2015-01-01 | S-EPMC4520626 | BioStudies
2013-01-01 | S-EPMC3838641 | BioStudies
2018-01-01 | S-EPMC6317530 | BioStudies
2008-01-01 | S-EPMC2652672 | BioStudies
2019-01-01 | S-EPMC6735427 | BioStudies
2010-01-01 | S-EPMC2876347 | BioStudies
2011-01-01 | S-EPMC3099264 | BioStudies
2009-01-01 | S-EPMC2754381 | BioStudies
2013-01-01 | S-EPMC3898665 | BioStudies