Enzyme Architecture: Self-Assembly of Enzyme and Substrate Pieces of Glycerol-3-Phosphate Dehydrogenase into a Robust Catalyst of Hydride Transfer

[Image: see text] The stabilization of the transition state for hlGPDH-catalyzed reduction of DHAP due to the action of the phosphodianion of DHAP and the cationic side chain of R269 is between 12.4 and 17 kcal/mol. The R269A mutation of glycerol-3-phosphate dehydrogenase (hlGPDH) results in a 9.1 k...

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Detalles Bibliográficos
Autores principales: Reyes, Archie C., Amyes, Tina L., Richard, John P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291162/
https://www.ncbi.nlm.nih.gov/pubmed/27792325
http://dx.doi.org/10.1021/jacs.6b09936

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5291162/
https://www.ncbi.nlm.nih.gov/pubmed/27792325
http://dx.doi.org/10.1021/jacs.6b09936

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