HAGH

HAGH

Identifiers

HAGH, GLO2, GLX2, GLXII, HAGH1, hydroxyacylglutathione hydrolase

External IDs

OMIM: 138760; MGI: 95745; GeneCards: HAGH

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1QH3, 1QH5

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
3.1.2.6	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 16 (human)

Band	16p13.3	Start	1,795,620 bp
Band	16p13.3	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
Band	17 A3.3\|17 12.53 cM	End	25,083,424 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

apex of heart

right lobe of liver

right adrenal gland

right adrenal cortex

left adrenal gland

gastrocnemius muscle

left adrenal cortex

prefrontal cortex

muscle of thigh

left testis

Top expressed in

spermatid

right kidney

spermatocyte

left lobe of liver

blood

proximal tubule

seminiferous tubule

human kidney

facial motor nucleus

tibiofemoral joint

More reference expression data


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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


3029


14651


ENSG00000063854


ENSMUSG00000024158


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

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.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000063854 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024158 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Mulley JC, Callen DF (Feb 1987). "New regional localisations for HAGH and PGP on human chromosome 16". Hum Genet. 74 (4): 423–4. doi:10.1007/BF00280498. PMID 3025077. S2CID 19620852.
↑ Honey NK, Shows TB (Apr 1982). "Assignment of the glyoxalase II gene (HAGH) to human chromosome 16". Hum Genet. 58 (4): 358–61. doi:10.1007/bf00282815. PMID 7327557. S2CID 10452468.
1 2 "Entrez Gene: HAGH hydroxyacylglutathione hydrolase".

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.

v t e PDB gallery
1qh3: HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE 1qh5: HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE

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