“Alcohol dehydrogenase (acceptor)”的意思、由来-开放百科全书

词条

Alcohol dehydrogenase (acceptor)

释义

Structural studies
See also
References

{{enzyme
| Name = alcohol dehydrogenase (acceptor)
| EC_number = 1.1.99.8
| CAS_number = 37205-43-9
| IUBMB_EC_number = 1/1/99/8
| GO_code = 0018468
| image =
| width =
| caption =
}}

In enzymology, an alcohol dehydrogenase (acceptor) ({{EC number|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

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

References

{{cite journal |author1 = Ameyama M |author2 =Adachi O | date = 1982 | title = Alcohol dehydrogenase from acetic acid bacteria, membrane-bound | journal = Methods in Enzymology | volume = 89 | pages = 450–457 | doi = 10.1016/S0076-6879(82)89078-2 | isbn = 978-0-12-181989-7 }}
{{cite journal | vauthors = Anthony C, Zatman LJ | date = 1967 | title = The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27 | journal = Biochem. J. | volume = 104 | pages = 953–9 | pmid = 6058112 | issue = 3 | pmc = 1271237 }}
{{cite journal | vauthors = Duine JA, Frank J, van Zeeland JK | date = 1979 | title = Glucose dehydrogenase from Acinetobacter calcoaceticus: a 'quinoprotein' | journal = FEBS Lett. | volume = 108 | pages = 443–6 | pmid = 520586 | doi = 10.1016/0014-5793(79)80584-0 | issue = 2 }}
{{cite journal | vauthors = Duine JA, Frank J, Verwiel PE | date = 1980 | title = Structure and activity of the prosthetic group of methanol dehydrogenase | journal = Eur. J. Biochem. | volume = 108 | pages = 187–92 | pmid = 6250827 | doi = 10.1111/j.1432-1033.1980.tb04711.x | issue = 1 }}
{{cite journal | vauthors = Salisbury SA, Forrest HS, Cruse WB, Kennard O | date = 1979 | title = A novel coenzyme from bacterial primary alcohol dehydrogenases | journal = Nature | volume = 280 | pages = 843–4 | pmid = 471057 | doi = 10.1038/280843a0 | issue = 5725 }}

3 : EC 1.1.99|Pyrroloquinoline quinone enzymes|Enzymes of known structure

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Structural studies

See also

References