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Dissecting the Total Transition State Stabilization Provided by Amino Acid Side-Chains at Orotidine 5′-Monophosphate Decarboxylase: A Two-Part Substrate Approach
Kinetic analysis of decarboxylation catalyzed by S154A, Q215A and S154A/Q215A mutant yeast orotidine 5′-monophosphate decarboxylases with orotidine 5′-monophosphate (OMP) and with a truncated nucleoside substrate (EO) activated by phosphite dianion shows: (1) The side-chain of Ser-154 stabilizes the...
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| Autors principals: | , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2008
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2652672/ https://ncbi.nlm.nih.gov/pubmed/18598058 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi800939k |
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