ADH5

ADH5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1M6H, 1M6W, 1MA0, 1MC5, 1MP0, 1TEH, 2FZE, 2FZW, 3QJ5
Identifiers
Aliases	ADH5, ADH-3, ADHX, FALDH, FDH, GSH-FDH, GSNOR, HEL-S-60p, alcohol dehydrogenase 5 (class III), chi polypeptide
External IDs	MGI: 87929 HomoloGene: 68076 GeneCards: ADH5
Gene ontology Molecular function • protein homodimerization activity • zinc ion binding • metal ion binding • fatty acid binding • formaldehyde dehydrogenase activity • electron carrier activity • oxidoreductase activity • S-(hydroxymethyl)glutathione dehydrogenase activity • alcohol dehydrogenase (NAD) activity Cellular component • cytoplasm • cytosol • mitochondrion • extracellular exosome Biological process • respiratory system process • retinoid metabolic process • response to redox state • positive regulation of blood pressure • response to lipopolysaccharide • peptidyl-cysteine S-nitrosylation • response to nitrosative stress • formaldehyde catabolic process • oxidation-reduction process • ethanol oxidation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	128	11532
Ensembl	ENSG00000197894	ENSMUSG00000028138
UniProt	P11766	P28474
RefSeq (mRNA)	NM_000671	NM_001288578 NM_007410
RefSeq (protein)	NP_000662.3	NP_001275507.1 NP_031436.2
Location (UCSC)	Chr 4: 99.07 – 99.09 Mb	Chr 3: 138.44 – 138.46 Mb
PubMed search	[1]	[2]
Wikidata

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Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.^[3][4][5]

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.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Hur MW, Edenberg HJ (Dec 1992). "Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase". Gene. 121 (2): 305–11. doi:10.1016/0378-1119(92)90135-C. PMID 1446828.
4. Adinolfi A, Adinolfi M, Hopkinson DA (May 1984). "Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme". Ann Hum Genet. 48 (Pt 1): 1–10. doi:10.1111/j.1469-1809.1984.tb00828.x. PMID 6424546.
5. "Entrez Gene: ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide".

External links

• Human ADH5 genome location and ADH5 gene details page in the UCSC Genome Browser.

Further reading

• 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. doi:10.1177/40.12.1453005. 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. doi:10.1016/0006-291X(89)91741-5. 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. doi:10.1016/0006-291X(89)91507-6. 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. doi:10.1073/pnas.82.24.8369. PMC 390917. 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. doi:10.1016/0006-291X(86)90358-X. 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. doi:10.1021/bi00404a009. PMID 3365377.
• 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. doi:10.1073/pnas.90.6.2491. PMC 46113. 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. doi:10.1021/bi00070a024. 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. doi:10.1016/S0006-8993(99)02201-5. PMID 10661511.
• Sanghani PC, Stone CL, Ray BD, et al. (2000). "Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase.". Biochemistry. 39 (35): 10720–9. doi:10.1021/bi9929711. 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. doi:10.1023/A:1015871219922. 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. doi:10.1021/bi0257639. 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. PMC 139241. 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. doi:10.1021/bi026705q. PMID 12484756.