Conformational Changes in Orotidine 5′-Monophosphate Decarboxylase: “Remote” Residues that Stabilize the Active Conformation()

The structural factors responsible for the extraordinary rate enhancement (~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 t...

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Bibliografische gegevens
Hoofdauteurs: Wood, B. McKay, Amyes, Tina L., Fedorov, Alexander A., Fedorov, Elena V., Shabila, Andrew, Almo, Steven C., Richard, John P., Gerlt, John A.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2010
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Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3245974/
https://ncbi.nlm.nih.gov/pubmed/20369850
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi100443a
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