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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Detaylı Bibliyografya

Yayımlandı:	Proc Natl Acad Sci U S A
Asıl Yazarlar:	Hirohara, Hideo, Bender, Myron L., Stark, Richard S.
Materyal Türü:	Artigo
Dil:	Inglês
Baskı/Yayın Bilgisi:	National Academy of Sciences 1974
Konular:	Biological Sciences: Biochemistry
Online Erişim:	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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