Rate and Equilibrium Constants for an Enzyme Conformational Change during Catalysis by Orotidine 5′-Monophosphate Decarboxylase

[Image: see text] The caged complex between orotidine 5′-monophosphate decarboxylase (ScOMPDC) and 5-fluoroorotidine 5′-monophosphate (FOMP) undergoes decarboxylation ∼300 times faster than the caged complex between ScOMPDC and the physiological substrate, orotidine 5′-monophosphate (OMP). Consequen...

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Detalles Bibliográficos
Autores principales: Goryanova, Bogdana, Goldman, Lawrence M., Ming, Shonoi, Amyes, Tina L., Gerlt, John A., Richard, John P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2015
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4520626/
https://www.ncbi.nlm.nih.gov/pubmed/26135041
http://dx.doi.org/10.1021/acs.biochem.5b00591

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4520626/
https://www.ncbi.nlm.nih.gov/pubmed/26135041
http://dx.doi.org/10.1021/acs.biochem.5b00591

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