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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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Autores principales: Hirohara, Hideo, Bender, Myron L., Stark, Richard S.
Formato: Artigo
Lenguaje:Inglês
Publicado: 1974
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC388293/
https://ncbi.nlm.nih.gov/pubmed/4525454
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