Open AccessTHE MECHANISM OF CHYMOTRYPSIN-CATALYZED REACTIONS
Author(s) -
H. Gutfreund,
Julian M. Sturtevant
Publication year - 1956
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.42.10.719
Subject(s) - symmetry (geometry) , interpretation (philosophy) , quantum , physics , theoretical physics , mechanism (biology) , quantum mechanics , t symmetry , classical mechanics , statistical physics , mathematics , computer science , geometry , programming language , superconductivity
In two recent papers" 2 it has been suggested that the reaction of chymotrypsin with its substrates proceeds by way of three kinetically distinct steps. First there occurs a rapid initial "adsorption" of the substrate on the specificity site of the enzyme. The second step involves the acylation of a group on the enzyme by the acidic part of the substrate, with concomitant liberation of the nonacyl moiety. Finally the acylated enzyme is hydrolyzed to regenerate the free enzyme and liberate the acidic part of the substrate. The following extension of the Michaelis-Menten scheme is both necessary and sufficient to account for all the experimental evidence concerning chymotrypsincatalyzed reactions, except that pertaining to the effect of inhibitors other than hydrogen ions:
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