Structure–Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase

[Image: see text] Kinetic parameters are reported for the reactions of whole substrates (k(cat)/K(m), M(–1) s(–1)) (R)-glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP) and for the substrate pieces [(k(cat)/K(m))(E·HP(i))/K(d), M(–2) s(–1)] glycolaldehyde (GA) and phosphite dian...

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Detalles Bibliográficos
Autores principales: Richard, John P., Amyes, Tina L., Malabanan, M. Merced, Zhai, Xiang, Kim, Kalvin J., Reinhardt, Christopher J., Wierenga, Rik K., Drake, Eric J., Gulick, Andrew M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4934371/
https://www.ncbi.nlm.nih.gov/pubmed/27149328
http://dx.doi.org/10.1021/acs.biochem.6b00311

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4934371/
https://www.ncbi.nlm.nih.gov/pubmed/27149328
http://dx.doi.org/10.1021/acs.biochem.6b00311

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