InterPro domain: IPR035680

Hydroxyacylglutathione hydrolase is also known as glyoxalase II, S-2-hydroxylacylglutathione hydrolase, hydroxyacylglutathione hydrolase, or acetoacetylglutathione hydrolase. In the second step of the glyoxalase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione [ 1 , 2 ].

Glyoxalase II belongs to the metallo-beta-lactamase (MBL)-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions [ 3 ]. The enzyme consists of two domains. The first domain folds into a four-layered beta sandwich, similar to that seen in the metallo-beta-lactamases. The second domain is predominantly alpha-helical. The active site contains a binuclear zinc-binding site and a substrate-binding site extending over the domain interface [ 4 ].

1. Glyoxalase II: molecular characteristics, kinetics and mechanism. Biochem. Soc. Trans. 21, 522-7
2. Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure 7, 1067-78
3. Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. FEBS Lett. 503, 1-6