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{{ | '''Hydroxyacylglutathione hydrolase, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''HAGH'' [[gene]].<ref name="pmid3025077">{{cite journal |vauthors=Mulley JC, Callen DF | title = New regional localisations for HAGH and PGP on human chromosome 16 | journal = Hum Genet | volume = 74 | issue = 4 | pages = 423–4 |date=Feb 1987 | pmid = 3025077 | pmc = | doi =10.1007/BF00280498 }}</ref><ref name="pmid7327557">{{cite journal |vauthors=Honey NK, Shows TB | title = Assignment of the glyoxalase II gene (HAGH) to human chromosome 16 | journal = Hum Genet | volume = 58 | issue = 4 | pages = 358–61 |date=Apr 1982 | pmid = 7327557 | pmc = | doi = 10.1007/bf00282815}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HAGH hydroxyacylglutathione hydrolase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3029| accessdate = }}</ref> | ||
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| summary_text = 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.<ref name="entrez" | | summary_text = 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.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=Kar NC, Pearson CM |title=Glyoxalase enzyme system in human muscular dystrophy |journal=Clin. Chim. Acta |volume=65 |issue= 1 |pages= 153–5 |year= 1976 |pmid= 1192606 |doi=10.1016/0009-8981(75)90348-4 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Hamilton DS, Creighton DJ |title=Inhibition of glyoxalase I by the enediol mimic S-(N-hydroxy-N-methylcarbamoyl)glutathione. The possible basis of a tumor-selective anticancer strategy |journal=J. Biol. Chem. |volume=267 |issue= 35 |pages= 24933–6 |year= 1993 |pmid= 1459997 |doi= }} | ||
*{{cite journal | | *{{cite journal |vauthors=Mulley JC, Barton N, Callen DF |title=Localisation of human PGP and HAGH genes to 16p13.3 |journal=Cytogenet. Cell Genet. |volume=53 |issue= 2–3 |pages= 175–6 |year= 1990 |pmid= 2164460 |doi=10.1159/000132923 }} | ||
*{{cite journal | author= | *{{cite journal | author=Talesa V |title=Demonstration of glyoxalase II in rat liver mitochondria. Partial purification and occurrence in multiple forms |journal=Biochim. Biophys. Acta |volume=955 |issue= 1 |pages= 103–10 |year= 1988 |pmid= 3382669 |doi=10.1016/0167-4838(88)90183-5 |name-list-format=vanc| author2=Uotila L | author3=Koivusalo M | display-authors=3 | last4=Principato | first4=G | last5=Giovannini | first5=E | last6=Rosi | first6=G }} | ||
*{{cite journal |vauthors=Thornalley PJ, Bellavite P |title=Modification of the glyoxalase system during the functional activation of human neutrophils |journal=Biochim. Biophys. Acta |volume=931 |issue= 2 |pages= 120–9 |year= 1987 |pmid= 3663711 |doi=10.1016/0167-4889(87)90198-4 }} | |||
*{{cite journal | | *{{cite journal |vauthors=Valentine WN, Paglia DE, Neerhout RC, Konrad PN |title=Erythrocyte glyoxalase II deficiency with coincidental hereditary elliptocytosis |journal=Blood |volume=36 |issue= 6 |pages= 797–808 |year= 1971 |pmid= 5485124 |doi= }} | ||
*{{cite journal | | *{{cite journal | author=Leoncini G |title=Platelet glyoxalases in thrombocytosis |journal=Scandinavian journal of haematology |volume=33 |issue= 1 |pages= 91–4 |year= 1984 |pmid= 6463589 |doi=10.1111/j.1600-0609.1984.tb02216.x |name-list-format=vanc| author2=Maresca M | author3=Balestrero F | display-authors=3 | last4=Armani | first4=U. | last5=Piana | first5=A. }} | ||
*{{cite journal | author=Leoncini G | *{{cite journal | author=Board PG |title=Genetic polymorphism of human erythrocyte glyoxalase II |journal=Am. J. Hum. Genet. |volume=32 |issue= 5 |pages= 690–4 |year= 1980 |pmid= 7424909 |doi= | pmc=1686103 }} | ||
*{{cite journal | author=Di Ilio C |title=Glyoxalase activities in tumor and non-tumor human urogenital tissues |journal=Cancer Lett. |volume=96 |issue= 2 |pages= 189–93 |year= 1995 |pmid= 7585456 |doi=10.1016/0304-3835(95)03928-P |name-list-format=vanc| author2=Angelucci S | author3=Pennelli A | display-authors=3 | last4=Zezza | first4=Andrea | last5=Tenaglia | first5=Raffaele | last6=Sacchetta | first6=Paolo }} | |||
*{{cite journal | author=Board PG |title=Genetic polymorphism of human erythrocyte glyoxalase II | *{{cite journal | author=Ridderström M |title=Molecular cloning, heterologous expression, and characterization of human glyoxalase II |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 319–23 |year= 1996 |pmid= 8550579 |doi=10.1074/jbc.271.1.319 |name-list-format=vanc| author2=Saccucci F | author3=Hellman U | display-authors=3 | last4=Bergman | first4=T | last5=Principato | first5=G | last6=Mannervik | first6=B }} | ||
*{{cite journal | author=Di Ilio C | *{{cite journal |vauthors=Cameron AD, Ridderström M, Olin B, Mannervik B |title=Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue |journal=Structure |volume=7 |issue= 9 |pages= 1067–78 |year= 1999 |pmid= 10508780 |doi=10.1016/S0969-2126(99)80174-9 }} | ||
*{{cite journal | author=Daniels RJ |title=Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16 |journal=Hum. Mol. Genet. |volume=10 |issue= 4 |pages= 339–52 |year= 2001 |pmid= 11157797 |doi=10.1093/hmg/10.4.339 |name-list-format=vanc| author2=Peden JF | author3=Lloyd C | display-authors=3 | last4=Horsley | first4=SW | last5=Clark | first5=K | last6=Tufarelli | first6=C | last7=Kearney | first7=L | last8=Buckle | first8=VJ | last9=Doggett | first9=NA }} | |||
*{{cite journal | author= | *{{cite journal | author=Rulli A |title=Expression of glyoxalase I and II in normal and breast cancer tissues |journal=Breast Cancer Res. Treat. |volume=66 |issue= 1 |pages= 67–72 |year= 2001 |pmid= 11368412 |doi=10.1023/A:1010632919129 |name-list-format=vanc| author2=Carli L | author3=Romani R | display-authors=3 | last4=Baroni | first4=Tiziano | last5=Giovannini | first5=Elvio | last6=Rosi | first6=Gabriella | last7=Talesa | first7=Vincenzo }} | ||
*{{cite journal | author=Scirè A |title=Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II |journal=Proteins |volume=48 |issue= 1 |pages= 126–33 |year= 2002 |pmid= 12012344 |doi= 10.1002/prot.10149 |name-list-format=vanc| author2=Saccucci F | author3=Bertoli E | display-authors=3 | last4=Cambria | first4=Maria Teresa | last5=Principato | first5=Giovanni | last6=d'Auria | first6=Sabato | last7=Tanfani | first7=Fabio }} | |||
*{{cite journal | | *{{cite journal | author=Mearini E |title=Differing expression of enzymes of the glyoxalase system in superficial and invasive bladder carcinomas |journal=Eur. J. Cancer |volume=38 |issue= 14 |pages= 1946–50 |year= 2002 |pmid= 12204678 |doi=10.1016/S0959-8049(02)00236-8 |name-list-format=vanc| author2=Romani R | author3=Mearini L | display-authors=3 | last4=Antognelli | first4=C | last5=Zucchi | first5=A | last6=Baroni | first6=T | last7=Porena | first7=M | last8=Talesa | first8=VN }} | ||
*{{cite journal | author= | *{{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }} | ||
*{{cite journal |vauthors=Cordell PA, Futers TS, Grant PJ, Pease RJ |title=The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28653–61 |year= 2004 |pmid= 15117945 |doi= 10.1074/jbc.M403470200 }} | |||
*{{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }} | |||
*{{cite journal | author= | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=3029}} | |||
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{{ | {{gene-16-stub}} | ||
Latest revision as of 13:27, 31 August 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| RefSeq (mRNA) |
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| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| Wikidata | |||||||
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Hydroxyacylglutathione hydrolase, mitochondrial is an enzyme that in humans is encoded by the HAGH gene.[1][2][3]
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.[3]
References
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "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. 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. 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.
- 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.
- 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. 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.
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