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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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| Hoofdauteurs: | , , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2010
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| Onderwerpen: | |
| 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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