Conformational Changes in Orotidine 5’-Monophosphate Decarboxylase: A Structure-Based Explanation for How the 5’-Phosphate Group Activates the Enzyme

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...

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Auteurs principaux: Desai, Bijoy J., Wood, McKay, Fedorov, Alexander A., Fedorov, Elena V., Goryanova, Bogdana, Amyes, Tina L., Richard, John P., Almo, Steven C., Gerlt, John A.
Format: Artigo
Langue:Inglês
Publié: 2012
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Article
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC3549026/
https://ncbi.nlm.nih.gov/pubmed/23030629
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi301188k
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