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Article

Conformational changes in orotidine 5'-monophosphate decarboxylase: a structure-based explanation for how the 5'-phosphate group activates the enzyme.

Biochemistry - 30 Oct 2012

Desai Bijoy J, Wood B McKay, Fedorov Alexander A, Fedorov Elena V, Goryanova Bogdana, Amyes Tina L, Richard John P, Almo Steven C, Gerlt John A

Abstract excerpt

The binding of a ligand to orotidine 5'-monophosphate decarboxylase (OMPDC) is accompanied by a conformational change from an open, inactive conformation (E(o)) to a closed, active conformation (E(c)). As the substrate traverses the reaction coordinate to form the stabilized vinyl carbanion/carbene intermediate, interactions that destabilize the carboxylate group of the substrate and stabilize the intermediate...

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Identifiers

PMID: 23030629
DOI: 10.1021/bi301188k
PMCID: PMC3549026

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