ADH7

From Wikipedia, the free encyclopedia

Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide

PDB rendering based on 1agn.

Available structures: 1agn, 1d1s, 1d1t

Identifiers

Symbol(s)

ADH7; ADH-4

External IDs

OMIM: 600086 MGI: 87926 HomoloGene: 37333

Gene ontology
Molecular Function:	• alcohol dehydrogenase activity, zinc-dependent • retinol dehydrogenase activity • zinc ion binding • oxidoreductase activity • metal ion binding
Biological Process:	• ethanol oxidation • electron transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000673 (mRNA)
NP_000664 (protein)

NM_009626 (mRNA)
NP_033756 (protein)

Location

Chr 4: 100.55 - 100.58 Mb

Chr 3: 138.16 - 138.17 Mb

Pubmed search

[1]

[2]

Alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide, also known as ADH7, is a human gene.^[1]

This gene encodes class IV alcohol dehydrogenase 7 mu or sigma 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. The enzyme encoded by this gene is inefficient in ethanol oxidation, but is the most active as a retinol dehydrogenase; thus it may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. The expression of this gene is much more abundant in stomach than liver, thus differing from the other known gene family members.^[1]

[edit] References

^ ^a ^b Entrez Gene: ADH7 alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide.

[edit] Further reading

Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Xie P, Parsons SH, Speckhard DC, et al. (1997). "X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity.". J. Biol. Chem. 272 (30): 18558–63. PMID 9228021.
Yokoyama H, Baraona E, Lieber CS (1997). "Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH.". Genomics 31 (2): 243–5. doi:10.1006/geno.1996.0040. PMID 8824810.
Satre MA, Zgombić-Knight M, Duester G (1994). "The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene.". J. Biol. Chem. 269 (22): 15606–12. PMID 8195208.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R (1994). "Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7).". FEBS Lett. 351 (3): 411–5. PMID 8082805.
Yokoyama H, Baraona E, Lieber CS (1994). "Molecular cloning of human class IV alcohol dehydrogenase cDNA.". Biochem. Biophys. Res. Commun. 203 (1): 219–24. doi:10.1006/bbrc.1994.2170. PMID 8074657.
Farrés J, Moreno A, Crosas B, et al. (1994). "Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships.". Eur. J. Biochem. 224 (2): 549–57. PMID 7925371.
Zgombić-Knight M, Foglio MH, Duester G (1995). "Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro.". J. Biol. Chem. 270 (9): 4305–11. PMID 7876191.
Kedishvili NY, Bosron WF, Stone CL, et al. (1995). "Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes.". J. Biol. Chem. 270 (8): 3625–30. PMID 7876099.
Cheung B, Anderson JK, Holmes RS, Beacham IR (1995). "Human stomach class IV alcohol dehydrogenase: molecular genetic analysis.". Alcohol. Clin. Exp. Res. 19 (1): 185–6. PMID 7771649.
Parés X, Cederlund E, Moreno A, et al. (1992). "Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class.". FEBS Lett. 303 (1): 69–72. PMID 1592118.