ExplorEnz: EC 1.1.1.1

Your query returned 1 entry. Printable version

1.1.1.1

Accepted name:

alcohol dehydrogenase

Reaction:

(1) a primary alcohol + NAD⁺ = an aldehyde + NADH + H⁺
(2) a secondary alcohol + NAD⁺ = a ketone + NADH + H⁺

For diagram of mevalonate biosynthesis, click here

Other name(s):

aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase

Systematic name:

alcohol:NAD⁺ oxidoreductase

Comments:

A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.

Links to other databases:

BRENDA, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9031-72-5

References:

1.	Brändén, G.-I., Jörnvall, H., Eklund, H. and Furugren, B. Alcohol dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 103–190.
2.	Jörnvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443–452. [DOI] [PMID: 320001]
3.	Negelein, E. and Wulff, H.-J. Diphosphopyridinproteid, Alkohol, Acetaldehyd. Biochem. Z. 293 (1937) 351–389.
4.	Sund, H. and Theorell, H. Alcohol dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 25–83.
5.	Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31–49. [PMID: 13605979]

[EC 1.1.1.1 created 1961, modified 2011]