Evidence for histidine in the active sites of ficin and stem-bromelain
- 1 November 1968
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 110 (1), 53-57
- https://doi.org/10.1042/bj1100053
Abstract
1. Ficin and stem-bromelain are irreversibly inhibited by 1,3-dibromoacetone, a reagent designed to react first with the active-site cysteine residue and subsequently with a second nucleophile. Evidence is presented that establishes that a histidine residue is within a 5Å locus of the active-site cysteine residue in both enzymes. The histidine residue in both enzymes is alkylated at N-1 by dibromoacetone. It is suggested that, as with papain, the thiol and imidazole groups act in concert in the hydrolysis of substrates by these enzymes. 2. The inhibition of thiol-subtilisin with 1,3-dibromoacetone is shown to be due to the alkylation of a cysteine residue only.This publication has 18 references indexed in Scilit:
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