Alcohol dehydrogenase (acceptor)
| alcohol dehydrogenase (acceptor) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.99.8 | ||||||||
| CAS no. | 37205-43-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction
- a primary alcohol + acceptor 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.
Structural studies
[edit]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.
See also
[edit]References
[edit]- Ameyama M; Adachi O (1982). "Alcohol dehydrogenase from acetic acid bacteria, membrane-bound". Carbohydrate Metabolism - Part D. Methods in Enzymology. Vol. 89. pp. 450–457. doi:10.1016/S0076-6879(82)89078-2. ISBN 978-0-12-181989-7.
- Anthony C, Zatman LJ (1967). "The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27". Biochem. J. 104 (3): 953–9. doi:10.1042/bj1040953. PMC 1271237. PMID 6058112.
- Duine JA, Frank J, van Zeeland JK (1979). "Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein'". FEBS Lett. 108 (2): 443–6. Bibcode:1979FEBSL.108..443D. doi:10.1016/0014-5793(79)80584-0. PMID 520586. S2CID 45206403.
- Duine JA, Frank J, Verwiel PE (1980). "Structure and activity of the prosthetic group of methanol dehydrogenase". Eur. J. Biochem. 108 (1): 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 (5725): 843–4. Bibcode:1979Natur.280..843S. doi:10.1038/280843a0. PMID 471057. S2CID 3094647.
