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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...
| Autores principales: | , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
American
Chemical Society
2016
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| 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 |