On the Question of an Acyl-enzyme Intermediate in the Chymotrypsin- Catalyzed Hydrolysis of Hydroxamic Acids.
نویسندگان
چکیده
منابع مشابه
Comparison of the Relative Rates of the Chymotrypsin-catalyzed and Nonenzymic Reactions of Esters with Hydroxylamine and Water.
The formation of an acyl-enzyme intermediate in the chymotrypsin-catalyzed reactions of esters (l-3) is widely held to be established, although some data do not quantitatively fit the theory (4, 5) and there is some dissent from this view. One of the simplest and most convincing ways of demonstrating the formation of an acyl-enzyme intermediate is to show that the chymotrypsin-catalyzed solvoly...
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Enzyme-substrate binding constants, K’e, for chymotrypsin and specific amide (N-acetyl-Mryptophanamide and Nacetyl-L-phenylalaninamide) and ester (N-acetyl-L-tryptophan ethyl ester) substrates have been measured by a proflavin-displacement method. Also, the rate constant for the formation of one intermediate in the chymotrypsincatalyzed hydrolysis of the ester has been determined at selected pH...
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The pH dependence of the steady state kinetic parameters K,(app) and $,t of the a-, acetylated 6-, and ar-chymotrypsincatalyzed hydrolysis of the specific amide substrate N-acetylr.-tryptophanamide, has been investigated in the neutral and alkaline pH regions. A completely automatic technique for measuring the hydrolysis of amides was used. New results and important aspects of the chymotrypsin-...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 238 شماره
صفحات -
تاریخ انتشار 1963