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

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

Stable Identifier

R-HSA-6783221

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

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

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 D-lactate (D-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