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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1974
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC388293/ https://ncbi.nlm.nih.gov/pubmed/4525454 |
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