Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Ball, J.C.; vander Jagt, D.L.
    S-2-Hydroxyacylglutathione hydrolase (glyoxalase II): active-site mapping of a nonserine thiolesterase (1981), Biochemistry, 20, 899-905.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.2.6 diethyldicarbonate
-
 Rattus norvegicus
3.1.2.6 methylene blue photoinactivation Rattus norvegicus
3.1.2.6 Trinitrobenzenesulfonate
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.6 0.014
-
 S-mandeloylglutathione
-
 Rattus norvegicus
3.1.2.6 0.18
-
 S-Lactoylglutathione
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.6 Rattus norvegicus
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
3.1.2.6 photoinactivation by methylene blue Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.2.6 S-(2-hydroxyacyl)glutathione + H2O = glutathione + a 2-hydroxy carboxylate mechanism Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.2.6 erythrocyte
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.6 lactoylglutathione + H2O
-
 Rattus norvegicus D-lactate + glutathione
-
 ?
3.1.2.6 S-mandeloylglutathione + H2O
-
 Rattus norvegicus mandelate + glutathione
-
 ?