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ADH5

{{Short description|Protein-coding gene in the species Homo sapiens}}

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{{Infobox_gene}}

Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.{{cite journal | vauthors = Hur MW, Edenberg HJ | title = Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase | journal = Gene | volume = 121 | issue = 2 | pages = 305–11 |date=Dec 1992| pmid = 1446828 | doi =10.1016/0378-1119(92)90135-C }}{{cite journal | vauthors = Adinolfi A, Adinolfi M, Hopkinson DA | title = Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme | journal = Ann Hum Genet | volume = 48 | issue = Pt 1 | pages = 1–10 |date=May 1984| pmid = 6424546 | doi =10.1111/j.1469-1809.1984.tb00828.x | s2cid = 85113864 }}{{cite web | title = Entrez Gene: ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=128}}

This gene encodes glutathione-dependent formaldehyde dehydrogenase or the class III alcohol dehydrogenase chi subunit, which is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class III alcohol dehydrogenase is a homodimer composed of 2 chi subunits. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione.

This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis.

Clinical significance

Mutations of the ADH5 gene and ALDH2 gene cause AMED syndrome, an autosomal recessive digenic multisystem disorder characterized by global developmental delay with impaired intellectual development, short stature, growth impairment and early development of myelodysplastic syndrome and bone marrow failure. The syndrome was first described in 2020.{{cite web|url=https://www.omim.org/entry/619151|title=AMED SYNDROME, DIGENIC; AMEDS|id=#619151|access-date=1 May 2024|last=Kniffin|first=Cassandra L.|date=27 November 2023|orig-date=Originally published on 13 January 2021|website=Online Mendelian Inheritance in Man|publisher=Johns Hopkins University}}

References

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Further reading

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  • {{cite journal | vauthors=Iborra FJ, Renau-Piqueras J, Portoles M |title=Immunocytochemical and biochemical demonstration of formaldhyde dehydrogenase (class III alcohol dehydrogenase) in the nucleus. |journal=J. Histochem. Cytochem. |volume=40 |issue= 12 |pages= 1865–78 |year= 1992 |pmid= 1453005 |doi= 10.1177/40.12.1453005|display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Giri PR, Krug JF, Kozak C |title=Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 1 |pages= 453–60 |year= 1989 |pmid= 2679557 |doi=10.1016/0006-291X(89)91741-5 |display-authors=etal|url=https://zenodo.org/record/1253802 }}
  • {{cite journal | vauthors=Sharma CP, Fox EA, Holmquist B |title=cDNA sequence of human class III alcohol dehydrogenase. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 2 |pages= 631–7 |year= 1989 |pmid= 2818582 |doi=10.1016/0006-291X(89)91507-6 |display-authors=etal}}
  • {{cite journal | vauthors=Beisswenger TB, Holmquist B, Vallee BL |title=chi-ADH is the sole alcohol dehydrogenase isozyme of mammalian brains: implications and inferences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 24 |pages= 8369–73 |year= 1986 |pmid= 2934732 |doi=10.1073/pnas.82.24.8369 | pmc=390917 |doi-access=free }}
  • {{cite journal | vauthors=Dafeldecker WP, Vallee BL |title=Organ-specific human alcohol dehydrogenase: isolation and characterization of isozymes from testis. |journal=Biochem. Biophys. Res. Commun. |volume=134 |issue= 3 |pages= 1056–63 |year= 1986 |pmid= 2936344 |doi=10.1016/0006-291X(86)90358-X }}
  • {{cite journal | vauthors=Kaiser R, Holmquist B, Hempel J |title=Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. |journal=Biochemistry |volume=27 |issue= 4 |pages= 1132–40 |year= 1988 |pmid= 3365377 |doi=10.1021/bi00404a009 |display-authors=etal}}
  • {{cite journal | vauthors=Khokha AM, Voronov PP, Zimatkin SM |title=[Immunoenzyme and immunohistochemical analysis of class III alcohol dehydrogenase from human testis] |journal=Biokhimiia |volume=59 |issue= 7 |pages= 997–1002 |year= 1994 |pmid= 7948423 }}
  • {{cite journal | vauthors=Engeland K, Höög JO, Holmquist B |title=Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 6 |pages= 2491–4 |year= 1993 |pmid= 8460164 |doi=10.1073/pnas.90.6.2491 | pmc=46113 |display-authors=etal|doi-access=free |bibcode=1993PNAS...90.2491E }}
  • {{cite journal | vauthors=Holmquist B, Moulis JM, Engeland K, Vallee BL |title=Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. |journal=Biochemistry |volume=32 |issue= 19 |pages= 5139–44 |year= 1993 |pmid= 8494891 |doi=10.1021/bi00070a024 }}
  • {{cite journal | vauthors=Engeland K, Maret W |title=Extrahepatic, differential expression of four classes of human alcohol dehydrogenase. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 1 |pages= 47–53 |year= 1993 |pmid= 8503936 |doi= 10.1006/bbrc.1993.1588 }}
  • {{cite journal | vauthors=Yang ZN, Bosron WF, Hurley TD |title=Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. |journal=J. Mol. Biol. |volume=265 |issue= 3 |pages= 330–43 |year= 1997 |pmid= 9018047 |doi= 10.1006/jmbi.1996.0731 }}
  • {{cite journal | vauthors=Mori O, Haseba T, Kameyama K |title=Histological distribution of class III alcohol dehydrogenase in human brain. |journal=Brain Res. |volume=852 |issue= 1 |pages= 186–90 |year= 2000 |pmid= 10661511 |doi=10.1016/S0006-8993(99)02201-5 |s2cid=23510523 |display-authors=etal}}
  • {{cite journal | vauthors=Sanghani PC, Stone CL, Ray BD |title=Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. |journal=Biochemistry |volume=39 |issue= 35 |pages= 10720–9 |year= 2000 |pmid= 10978156 |doi=10.1021/bi9929711 |display-authors=etal}}
  • {{cite journal | vauthors=Lee DK, Suh D, Edenberg HJ, Hur MW |title=POZ domain transcription factor, FBI-1, represses transcription of ADH5/FDH by interacting with the zinc finger and interfering with DNA binding activity of Sp1. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 26761–8 |year= 2002 |pmid= 12004059 |doi= 10.1074/jbc.M202078200 |doi-access= free }}
  • {{cite journal | vauthors=Jelski W, Chrostek L, Szmitkowski M, Laszewicz W |title=Activity of class I, II, III, and IV alcohol dehydrogenase isoenzymes in human gastric mucosa. |journal=Dig. Dis. Sci. |volume=47 |issue= 7 |pages= 1554–7 |year= 2002 |pmid= 12141816 |doi=10.1023/A:1015871219922 |s2cid=31197228 }}
  • {{cite journal | vauthors=Sanghani PC, Robinson H, Bosron WF, Hurley TD |title=Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes. |journal=Biochemistry |volume=41 |issue= 35 |pages= 10778–86 |year= 2002 |pmid= 12196016 |doi=10.1021/bi0257639 }}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Sanghani PC, Bosron WF, Hurley TD |title=Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation. |journal=Biochemistry |volume=41 |issue= 51 |pages= 15189–94 |year= 2003 |pmid= 12484756 |doi=10.1021/bi026705q }}

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External links

  • {{UCSC gene info|ADH5}}

{{PDB Gallery|geneid=128}}

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