Reaction: (1) a primary alcohol + NAD+ = an aldehyde + NADH + H+
(2) a secondary alcohol + NAD+ = a ketone + NADH + H+
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, 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 ed., vol. 11, Academic Press, New York, 1975, p. 103-190.
2. Jörnvall, H. Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects. Eur. J. Biochem. 72 (1977) 443-452. [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. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 25-83.
5. Theorell, H. Kinetics and equilibria in the liver alcohol dehydrogenase system. Adv. Enzymol. Relat. Subj. Biochem. 20 (1958) 31-49.