Acylation of α-Chymotrypsin by Oxygen and Sulfur Esters of Specific Substrates: Kinetic Evidence for a Tetrahedral Intermediate
The acylation step of the α-chymotrypsincatalyzed hydrolysis of N-acetyl-L (or DL)-tryptophan p-nitrophenyl, p-nitrothiophenyl, ethyl, and thiolethyl esters has been studied by the stopped-flow technique at 25°. The acylation rate constant, k(2), and the enzyme substrate dissociation constant, K(s),...
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| Publicat a: | Proc Natl Acad Sci U S A |
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| Autors principals: | , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
National Academy of Sciences
1974
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC388293/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/4525454/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.71.5.1643 |
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