HAGH hydrolyses (R)-S-LGSH to GSH and LACT

Stable Identifier
R-HSA-6783221
Type
Reaction
Species
Homo sapiens
Compartment
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In the second step of the glyoxalase system, hydroxyacylglutathione hydrolase (HAGH) catalyses the hydrolysis of (R)-S-lactoylglutathione ((R)-S-LGSH) to glutathione (GSH) and lactic acid (LACT) (Ridderstrom et al. 1996). The HAGH gene can produce two forms of the protein, form 1 is mitochondrial whereas form 2 is cytosolic (Cordell et al. 2004). HAGH is monomeric but requires two Zn2+ ions for activity (Cameron et al. 1999). This reaction completes the detoxification of methylglyoxal, a reactive byproduct of pyruvate metabolism.

Literature References
PubMed ID Title Journal Year
8550579 Molecular cloning, heterologous expression, and characterization of human glyoxalase II

Ridderström, M, Saccucci, F, Hellman, U, Bergman, T, Principato, G, Mannervik, B

J. Biol. Chem. 1996
10508780 Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue

Cameron, AD, Ridderström, M, Olin, B, Mannervik, B

Structure 1999
15117945 The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II

Cordell, PA, Futers, TS, Grant, PJ, Pease, RJ

J. Biol. Chem. 2004
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
hydroxyacylglutathione hydrolase activity of HAGH-2:2xZn2+ [cytosol]
Physical Entity
Activity
Orthologous Events
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