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Article

Conformational changes in orotidine 5'-monophosphate decarboxylase: "remote" residues that stabilize the active conformation.

Biochemistry - 4 May 2010

Wood B McKay, Amyes Tina L, Fedorov Alexander A, Fedorov Elena V, Shabila Andrew, Almo Steven C, Richard John P, Gerlt John A

Abstract excerpt

The structural factors responsible for the extraordinary rate enhancement ( approximately 10(17)) of the reaction catalyzed by orotidine 5'-monophosphate decarboxylase (OMPDC) have not been defined. Catalysis requires a conformational change that closes an active site loop and "clamps" the orotate base proximal to hydrogen-bonded networks that destabilize the substrate and stabilize the intermediate. In the OMPDC...

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Identifiers

PMID: 20369850
DOI: 10.1021/bi100443a
PMCID: PMC3245974

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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