Glyoxalase II: Molecular characteristics, kinetics and mechanism

Autor:	D L Vander Jagt
Rok vydání:	1993
Předmět:	chemistry.chemical_classification Binding Sites Lability Stereochemistry Kinetics Substrate (chemistry) Hydrogen-Ion Concentration Pyruvaldehyde Biochemistry Hydroxyacylglutathione hydrolase Substrate Specificity Aminolysis chemistry Nucleophile Thiol Animals Humans Thiolester Hydrolases Histidine
Zdroj:	Biochemical Society Transactions. 21:522-527
ISSN:	1470-8752 0300-5127
Popis:	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].
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e5cacef658ff5366ac9e958dcccdd6 https://doi.org/10.1042/bst0210522 Zobrazit plný text záznamu