The effect of the N-acyl moiety of the substrate on α-chymotrypsin binding and catalysis
Author:
Publisher
Elsevier BV
Subject
General Engineering
Reference48 articles.
1. Kinetic Evidence for the Formation of Acyl-Enzyme Intermediates in the α-Chymotrypsin-Catalyzed Hydrolyses of Specific Substrates
2. Chymotrypsin-catalyzed phenyl ester hydrolysis. Evidence for electrophilic assistance on carbonyl oxygen
3. Acylation of -Chymotrypsin by Oxygen and Sulfur Esters of Specific Substrates: Kinetic Evidence for a Tetrahedral Intermediate
4. Binding rates, oxygen-sulfur substitution effects, and the pH dependence of chymotrypsin reactions
5. Chymotrypsin catalysis. Evidence for a new intermediate. II
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1. Dynamics of ligand binding to .alpha.-chymotrypsin and to N-methyl-.alpha.-chymotrypsin;Biochemistry;1982-09-14
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