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{{ | '''Alcohol dehydrogenase class-3''' is an [[enzyme]] that in humans is encoded by the ''ADH5'' [[gene]].<ref name="pmid1446828">{{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 | pmc = | doi =10.1016/0378-1119(92)90135-C }}</ref><ref name="pmid6424546">{{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 | pmc = | doi =10.1111/j.1469-1809.1984.tb00828.x }}</ref><ref name="entrez">{{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| accessdate = }}</ref> | ||
}} | |||
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| section_title = | | section_title = | ||
| summary_text = 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.<ref name="entrez" | | summary_text = 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.<ref name="entrez"/> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|ADH5}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
*{{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 | | *{{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 | | *{{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 |doi= }} | ||
*{{cite journal | | *{{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}} | ||
*{{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 | | *{{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 | | *{{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 | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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 | | *{{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 }} | ||
*{{cite journal | | *{{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 }} | ||
*{{cite journal | | *{{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 | | *{{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 |display-authors=etal}} | ||
*{{cite journal | | *{{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 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=128}} | |||
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Revision as of 17:51, 29 August 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Ensembl |
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| UniProt |
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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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Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.[1][2][3]
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.[3]
References
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "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.
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