HAGH

HAGH

Target · Mitochondrial thiolesterase

HAGH Hydroxyacylglutathione hydrolase · glyoxalase II

HAGH (hydroxyacylglutathione hydrolase, also known as GLO2, GLXII and HAGH1) is a thiolesterase that hydrolyses S-D-lactoyl-glutathione to glutathione and D-lactic acid. It belongs to the glyoxalase II family of the metallo-beta-lactamase superfamily. Browse Assay Genie's current range of HAGH research reagents below, or read on for the biology behind the target.

Mitochondrial matrix and cytoplasmGlyoxalase II thiolesteraseThree transcript variants
308 aa
Protein length
~34 kDa
Molecular weight
16p13.3
Gene locus
EC 3.1.2.6
Enzyme class
Target information

What is HAGH (hydroxyacylglutathione hydrolase)?

HAGH is a thiolesterase that catalyses the hydrolysis of S-D-lactoyl-glutathione, releasing reduced glutathione and D-lactic acid. The reaction is assigned EC 3.1.2.6, and the enzyme is the second of the two glyoxalase activities, which is why it is commonly called glyoxalase II (GLO2 or GLXII). Because the reaction returns glutathione as a product, HAGH is of interest wherever glutathione handling and thioester turnover are studied.

The HAGH gene encodes a protein that belongs to the metallo-beta-lactamase superfamily and the glyoxalase II family. HGNC places it in the MBL domain containing glyoxalase 2 subfamily and in the thioester hydrolases gene group. UniProt records the protein in the mitochondrial matrix and in the cytoplasm. Mouse and rat both carry a Hagh ortholog, which allows the enzyme to be studied in common model systems.

NCBI Gene (RefSeq) reports three transcript variants of the HAGH gene that encode different isoforms. Alongside the approved symbol, the gene has appeared as HAGH1, and the earlier name was hydroxyacyl glutathione hydrolase. Researchers working on HAGH typically consider these aliases together when searching the literature, and may look for an HAGH antibody or HAGH ELISA kit when measuring the protein.

Glutathione metabolism

HAGH releases reduced glutathione and D-lactate from S-D-lactoyl-glutathione, making it a relevant enzyme for studies of glutathione recycling.

Glyoxalase pathway research

As glyoxalase II, HAGH acts on S-lactoyl-glutathione, so it is studied as a defined step in glyoxalase-related biochemistry.

Mitochondrial enzymology

UniProt places HAGH in the mitochondrial matrix as well as the cytoplasm, which suits work on compartment-specific enzyme activity.

Metallo-beta-lactamase family studies

HAGH is a member of the metallo-beta-lactamase superfamily, making it a useful reference for comparing thioester hydrolases within this fold.

Background

HAGH frequently asked questions

What does HAGH do?

HAGH is a thiolesterase that catalyses the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. It is classified as EC 3.1.2.6 and is also known as glyoxalase II, reflecting its role in the glyoxalase system.

What other names and isoforms does HAGH have?

HAGH is also called GLO2, GLXII and HAGH1, and was previously named hydroxyacyl glutathione hydrolase. NCBI Gene reports three transcript variants that encode different isoforms, so it is worth checking which isoform a given reagent recognises.

Is HAGH conserved across species?

Mouse and rat both have an ortholog named Hagh, so the enzyme can be studied in standard rodent models. The protein belongs to the glyoxalase II family of the metallo-beta-lactamase superfamily. Check the datasheet of any product for its validated reactivity.

Explore

Related targets

Other glyoxalase pathway enzymes, glutathione-related proteins and thioester hydrolases with products at Assay Genie.

Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16775; product specifications from Assay Genie datasheets.

HAGH Product listing