Deuterium isotope effects on acylation of subtilisin

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Abstract

2H2O 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.

Original languageEnglish
Pages (from-to)639-642
Number of pages4
JournalBBA - Enzymology
Volume321
Issue number2
DOIs
Publication statusPublished - Oct 10 1973

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Subtilisin
Acylation
Deuterium
Catalysis
Isotopes
Esters
Serine Proteases
Histidine
Sulfhydryl Compounds
Biochemistry
Catalytic Domain
Acetates
imidazole

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Deuterium isotope effects on acylation of subtilisin. / Polgár, L.

In: BBA - Enzymology, Vol. 321, No. 2, 10.10.1973, p. 639-642.

Research output: Contribution to journalArticle

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