ADH5

From Wikipedia, the free encyclopedia


Alcohol dehydrogenase 5 (class III), chi polypeptide
PDB rendering based on 1m6h.
Available structures: 1m6h, 1m6w, 1ma0, 1mc5, 1mp0, 1teh, 2fze, 2fzw
Identifiers
Symbol(s) ADH5; ADH-3; ADHX; FDH
External IDs OMIM: 103710 MGI: 87929 HomoloGene: 68076
Orthologs
Human Mouse
Entrez 128 11532


Refseq NM_000671 (mRNA)
NP_000662 (protein)		 NM_007410 (mRNA)
NP_031436 (protein)
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide.

[edit] 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. 
 This protein-related article is a stub. You can help Wikipedia by expanding it.