HAGH

HAGH
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1QH3, 1QH5
Identifiers
Aliases	HAGH, GLO2, GLX2, GLXII, HAGH1, hydroxyacylglutathione hydrolase
External IDs	OMIM: 138760 MGI: 95745 HomoloGene: 3890 GeneCards: HAGH
Gene location (Human) Chr. Chromosome 16 (human) Band 16p13.3 Start 1,795,620 bp End 1,827,157 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17 A3.3|17 12.53 cM Start 25,059,117 bp End 25,083,424 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver right adrenal gland left adrenal gland gastrocnemius muscle prefrontal cortex left ventricle Brodmann area 9 anterior pituitary nucleus accumbens frontal pole Top expressed in spermatid spermatocyte left lobe of liver blood proximal tubule seminiferous tubule kidney facial motor nucleus brown adipose tissue cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function hydroxyacylglutathione hydrolase activity protein binding hydrolase activity metal ion binding Cellular component cytoplasm cytosol mitochondrial matrix mitochondrion Biological process methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione glutathione biosynthetic process pyruvate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3029 14651 Ensembl ENSG00000063854 ENSMUSG00000024158 UniProt Q16775 Q99KB8 RefSeq (mRNA) NM_001040427 NM_001286249 NM_005326 NM_001363912 NM_001363914 NM_001159626 NM_024284 RefSeq (protein) NP_001035517 NP_001273178 NP_005317 NP_001350841 NP_001350843 NP_001153098 NP_077246 Location (UCSC) Chr 16: 1.8 – 1.83 Mb Chr 17: 25.06 – 25.08 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Hydroxyacylglutathione hydrolase, mitochondrial is an enzyme that in humans is encoded by the HAGH gene.

The enzyme encoded by this gene is classified as a thiolesterase and is responsible for the hydrolysis of S-lactoyl-glutathione to reduced glutathione and D-lactate.

Further reading

• Kar NC, Pearson CM (1976). "Glyoxalase enzyme system in human muscular dystrophy". Clin. Chim. Acta. 65 (1): 153–5. doi:10.1016/0009-8981(75)90348-4. PMID 1192606.
• Hamilton DS, Creighton DJ (1993). "Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy". J. Biol. Chem. 267 (35): 24933–6. doi:10.1016/S0021-9258(19)73986-6. PMID 1459997.
• Mulley JC, Barton N, Callen DF (1990). "Localisation of human PGP and HAGH genes to 16p13.3". Cytogenet. Cell Genet. 53 (2–3): 175–6. doi:10.1159/000132923. PMID 2164460.
• Talesa V, Uotila L, Koivusalo M, et al. (1988). "Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms". Biochim. Biophys. Acta. 955 (1): 103–10. doi:10.1016/0167-4838(88)90183-5. PMID 3382669.
• Thornalley PJ, Bellavite P (1987). "Modification of the glyoxalase system during the functional activation of human neutrophils". Biochim. Biophys. Acta. 931 (2): 120–9. doi:10.1016/0167-4889(87)90198-4. PMID 3663711.
• Valentine WN, Paglia DE, Neerhout RC, Konrad PN (1971). "Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis". Blood. 36 (6): 797–808. doi:10.1182/blood.V36.6.797.797. PMID 5485124.
• Leoncini G, Maresca M, Balestrero F, et al. (1984). "Platelet glyoxalases in thrombocytosis". Scandinavian Journal of Haematology. 33 (1): 91–4. doi:10.1111/j.1600-0609.1984.tb02216.x. PMID 6463589.
• Board PG (1980). "Genetic polymorphism of human erythrocyte glyoxalase II". Am. J. Hum. Genet. 32 (5): 690–4. PMC 1686103. PMID 7424909.
• Di Ilio C, Angelucci S, Pennelli A, et al. (1995). "Glyoxalase activities in tumor and non-tumor human urogenital tissues". Cancer Lett. 96 (2): 189–93. doi:10.1016/0304-3835(95)03928-P. PMID 7585456.
• Ridderström M, Saccucci F, Hellman U, et al. (1996). "Molecular cloning, heterologous expression, and characterization of human glyoxalase II". J. Biol. Chem. 271 (1): 319–23. doi:10.1074/jbc.271.1.319. PMID 8550579.
• Cameron AD, Ridderström M, Olin B, Mannervik B (1999). "Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue". Structure. 7 (9): 1067–78. doi:10.1016/S0969-2126(99)80174-9. PMID 10508780.
• Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16". Hum. Mol. Genet. 10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID 11157797.
• Rulli A, Carli L, Romani R, et al. (2001). "Expression of glyoxalase I and II in normal and breast cancer tissues". Breast Cancer Res. Treat. 66 (1): 67–72. doi:10.1023/A:1010632919129. PMID 11368412. S2CID 10225506.
• Scirè A, Saccucci F, Bertoli E, et al. (2002). "Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II". Proteins. 48 (1): 126–33. doi:10.1002/prot.10149. PMID 12012344. S2CID 25251778.
• Mearini E, Romani R, Mearini L, et al. (2002). "Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas". Eur. J. Cancer. 38 (14): 1946–50. doi:10.1016/S0959-8049(02)00236-8. PMID 12204678.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cordell PA, Futers TS, Grant PJ, Pease RJ (2004). "The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II". J. Biol. Chem. 279 (27): 28653–61. doi:10.1074/jbc.M403470200. PMID 15117945.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.