Glyoxalase II: molecular characteristics, kinetics and mechanism

Biochem Soc Trans. 1993 May;21(2):522-7. doi: 10.1042/bst0210522.

Abstract

The mechanism that has been proposed for glyoxalase II [36] is summarized in Figure 3. It involves direct nucleophilic attack of an active-site histidine on the thiol ester substrate to form an acyl-imidazole intermediate which then rapidly hydrolyses. This is consistent with the known susceptibility of thiol esters to aminolysis and with the lability of acyl-imidazoles [47].

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Binding Sites / physiology
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Pyruvaldehyde / metabolism
  • Substrate Specificity
  • Thiolester Hydrolases / chemistry*
  • Thiolester Hydrolases / metabolism

Substances

  • Pyruvaldehyde
  • Thiolester Hydrolases
  • hydroxyacylglutathione hydrolase