The Organization of Active Site Side Chains of Glycerol-3-phosphate Dehydrogenase Promotes Efficient Enzyme Catalysis and Rescue of Variant Enzymes

[Image: see text] A comparison of the values of k(cat)/K(m) for reduction of dihydroxyacetone phosphate (DHAP) by NADH catalyzed by wild type and K120A/R269A variant glycerol-3-phosphate dehydrogenase from human liver (hlGPDH) shows that the transition state for enzyme-catalyzed hydride transfer is...

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Detalles Bibliográficos
Autores principales: Cristobal, Judith R., Reyes, Archie C., Richard, John P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7207223/
https://www.ncbi.nlm.nih.gov/pubmed/32250105
http://dx.doi.org/10.1021/acs.biochem.0c00175

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7207223/
https://www.ncbi.nlm.nih.gov/pubmed/32250105
http://dx.doi.org/10.1021/acs.biochem.0c00175

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