ADH5

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Alcohol dehydrogenase 5 (class III), chi polypeptide
PDB rendering based on 1m6h.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols ADH5 ; ADH-3; ADHX; FDH
External IDs Template:OMIM5 Template:MGI HomoloGene68076
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Alcohol dehydrogenase 5 (class III), chi polypeptide, also known as ADH5, is a human gene.[1]

This gene encodes glutathione-dependent formaldehyde dehydrogenase or 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.[1]

References

  1. 1.0 1.1 "Entrez Gene: ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide".

Further reading

  • Hur MW, Edenberg HJ (1992). "Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase". Gene. 121 (2): 305–11. PMID 1446828.
  • Iborra FJ, Renau-Piqueras J, Portoles M; et al. (1992). "Immunocytochemical and biochemical demonstration of formaldhyde dehydrogenase (class III alcohol dehydrogenase) in the nucleus". J. Histochem. Cytochem. 40 (12): 1865–78. PMID 1453005.
  • Giri PR, Krug JF, Kozak C; et al. (1989). "Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA". Biochem. Biophys. Res. Commun. 164 (1): 453–60. PMID 2679557.
  • Sharma CP, Fox EA, Holmquist B; et al. (1989). "cDNA sequence of human class III alcohol dehydrogenase". Biochem. Biophys. Res. Commun. 164 (2): 631–7. PMID 2818582.
  • Beisswenger TB, Holmquist B, Vallee BL (1986). "chi-ADH is the sole alcohol dehydrogenase isozyme of mammalian brains: implications and inferences". Proc. Natl. Acad. Sci. U.S.A. 82 (24): 8369–73. PMID 2934732.
  • Dafeldecker WP, Vallee BL (1986). "Organ-specific human alcohol dehydrogenase: isolation and characterization of isozymes from testis". Biochem. Biophys. Res. Commun. 134 (3): 1056–63. PMID 2936344.
  • Kaiser R, Holmquist B, Hempel J; et al. (1988). "Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes". Biochemistry. 27 (4): 1132–40. PMID 3365377.
  • Adinolfi A, Adinolfi M, Hopkinson DA (1984). "Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme". Ann. Hum. Genet. 48 (Pt 1): 1–10. PMID 6424546.
  • Khokha AM, Voronov PP, Zimatkin SM (1994). "[Immunoenzyme and immunohistochemical analysis of class III alcohol dehydrogenase from human testis]". Biokhimiia. 59 (7): 997–1002. PMID 7948423.
  • Engeland K, Höög JO, Holmquist B; et al. (1993). "Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation". Proc. Natl. Acad. Sci. U.S.A. 90 (6): 2491–4. PMID 8460164.
  • Holmquist B, Moulis JM, Engeland K, Vallee BL (1993). "Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase". Biochemistry. 32 (19): 5139–44. PMID 8494891.
  • Engeland K, Maret W (1993). "Extrahepatic, differential expression of four classes of human alcohol dehydrogenase". Biochem. Biophys. Res. Commun. 193 (1): 47–53. doi:10.1006/bbrc.1993.1588. PMID 8503936.
  • Yang ZN, Bosron WF, Hurley TD (1997). "Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase". J. Mol. Biol. 265 (3): 330–43. doi:10.1006/jmbi.1996.0731. PMID 9018047.
  • Mori O, Haseba T, Kameyama K; et al. (2000). "Histological distribution of class III alcohol dehydrogenase in human brain". Brain Res. 852 (1): 186–90. PMID 10661511.
  • Sanghani PC, Stone CL, Ray BD; et al. (2000). "Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase". Biochemistry. 39 (35): 10720–9. PMID 10978156.
  • Lee DK, Suh D, Edenberg HJ, Hur MW (2002). "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". J. Biol. Chem. 277 (30): 26761–8. doi:10.1074/jbc.M202078200. PMID 12004059.
  • Jelski W, Chrostek L, Szmitkowski M, Laszewicz W (2002). "Activity of class I, II, III, and IV alcohol dehydrogenase isoenzymes in human gastric mucosa". Dig. Dis. Sci. 47 (7): 1554–7. PMID 12141816.
  • Sanghani PC, Robinson H, Bosron WF, Hurley TD (2002). "Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes". Biochemistry. 41 (35): 10778–86. PMID 12196016.
  • 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. PMID 12477932.
  • Sanghani PC, Bosron WF, Hurley TD (2003). "Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation". Biochemistry. 41 (51): 15189–94. PMID 12484756.

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