Issue 11, 1975

The carboxypeptidase Y-catalysed hydrolysis of aryl trimethylacetates: the nature of the deacylation reaction of trimethylacetylcarboxypeptidase Y

Abstract

The identical kcat values obtained for the trimethylacetyl esters of 4-nitrophenol, 2,4-dinitrophenol, and 2-chloro-4-nitrophenol support the intermediacy of a trimethylacetyl enzyme in the esterase action of yeast carboxypeptidase Y, the deacylation of which depends on the ionization of an acidic species (pKapp= 5·1) with limiting kcat values of 0·9 × 10–2 s–1 and 2·2 × 10–2 s–1 in acidic and basic solutions, respectively.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1975, 429-430

The carboxypeptidase Y-catalysed hydrolysis of aryl trimethylacetates: the nature of the deacylation reaction of trimethylacetylcarboxypeptidase Y

K. T. Douglas, Y. Nakagawa and E. T. Kaiser, J. Chem. Soc., Chem. Commun., 1975, 429 DOI: 10.1039/C39750000429

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