Alcohol dehydrogenase (acceptor)

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In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction

a primary alcohol + acceptor $\rightleftharpoons$ an aldehyde + reduced acceptor

Thus, the two substrates of this enzyme are primary alcohol and acceptor, whereas its two products are aldehyde and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is alcohol:acceptor oxidoreductase. Other names in common use include primary alcohol dehydrogenase, MDH, quinohemoprotein alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase, and alcohol:(acceptor) oxidoreductase. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, 1,2-dichloroethane degradation, propanoate metabolism, butanoate metabolism, and methane metabolism. It employs one cofactor, PQQ.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1G72, 1H4I, 1H4J, 1LRW, 1W6S, 2AD6, 2AD7, 2AD8, 2D0V, 4AAH, and 8ADH.

[edit] References

IUBMB entry for 1.1.99.8
BRENDA references for 1.1.99.8 (Recommended.)
PubMed references for 1.1.99.8
PubMed Central references for 1.1.99.8
Google Scholar references for 1.1.99.8
Ameyama M and Adachi O (1982). "Alcohol dehydrogenase from acetic acid bacteria, membrane-bound". Methods Enzymol. 89: 450–457.
Anthony C, Zatman LJ (1967). "The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27". Biochem. J. 104: 953–9. PMID 6058112.
Duine JA, Frank J, van Zeeland JK (1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS. Lett. 108: 443–6. doi:10.1016/0014-5793(79)80584-0. PMID 520586.
Duine JA, Frank J, Verwiel PE (1980). "Structure and activity of the prosthetic group of methanol dehydrogenase". Eur. J. Biochem. 108: 187–92. doi:10.1111/j.1432-1033.1980.tb04711.x. PMID 6250827.
Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). "A novel coenzyme from bacterial primary alcohol dehydrogenases". Nature. 280: 843–4. doi:10.1038/280843a0. PMID 471057.