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

Stable Identifier
Reaction [transition]
Homo sapiens
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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
10508780 Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue

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

Structure 1999
8550579 Molecular cloning, heterologous expression, and characterization of human glyoxalase II

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

J. Biol. Chem. 1996
15117945 The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II

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

J. Biol. Chem. 2004
Catalyst Activity

hydroxyacylglutathione hydrolase activity of HAGH-2:2xZn2+ [cytosol]

Orthologous Events
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