Protein Family Models

This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (Pfam:PF00753) [1-3]. [1]. 10508780. Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Cameron AD, Ridderstrom M, Olin B, Mannervik B;. Structure. 1999;7:1067-1078. [2]. 14529289. Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Schilling O, Wenzel N, Naylor M, Vogel A, Crowder M, Makaroff C, Meyer-Klaucke W;. Biochemistry. 2003;42:11777-11786. [3]. 17764159. Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity. Campos-Bermudez VA, Leite NR, Krog R, Costa-Filho AJ, Soncini FC, Oliva G, Vila AJ;. Biochemistry. 2007;46:11069-11079. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

hydroxyacylglutathione hydrolase is a type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione

Date:

2017-05-09

Catalyzes the hydrolysis of S-D-lactoylglutathione to D-lactic acid and reduced glutathione; plays an important role in cellular detoxification using glutathione

Gene:

gloB

Date:

2021-10-13

Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (PF00753).

Gene:

gloB

Date:

2021-04-27