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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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| Publicado no: | Biochemistry |
|---|---|
| Main Authors: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American
Chemical Society
2020
|
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7207223/ https://ncbi.nlm.nih.gov/pubmed/32250105 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.0c00175 |
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