Abstract
2H 2O effects on the hydrolyses of nonactivated alkyl and the corresponding activated alkyl thiol and p- nitrophenyl esters by subtilisin. Type Carlsberg, were investigated. Similar effects were obtained with the activated and nonactivated esters of acetic and cinnamic acids. This rules out the formation of a transient acyl-imidazole intermediate in the catalysis by serine proteases proposed by Hubbard, C. D. and Kirsch, J. F. (1972) Biochemistry 11, 2483–2493, for nonspecific-activated ester substrates. Stereochemical considerations based on model building of the active site of subtilisin offer further evidence against nucleophilic catalysis by the histidine residue.
Published Version
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