EC 1.1.1.1 - Alcohol dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.1

Names

Accepted name:
alcohol dehydrogenase
Other names:
ADH
NAD-dependent alcohol dehydrogenase
NAD-specific aromatic alcohol dehydrogenase
NADH-alcohol dehydrogenase
NADH-aldehyde dehydrogenase
alcohol dehydrogenase (NAD)
aldehyde reductase
aliphatic alcohol dehydrogenase
ethanol dehydrogenase
primary alcohol dehydrogenase
yeast alcohol dehydrogenase
Systematic name:
alcohol:NAD+ oxidoreductase

Reactions

Cofactor

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00058 , PROSITE:PDOC00059 , PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004022
CAS Registry Number: 9031-72-5
UniProtKB/Swiss-Prot: (245) [show] [UniProt]

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, 103-190
  2. Jörnvall, H.
    Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects.
    Eur. J. Biochem. 72: 443-452 (1977). [PMID: 320001]
  3. Negelein, E. and Wulff, H.-J.
    Diphosphopyridinproteid ackohol, acetaldehyd.
    Biochem. Z. 293: 351-389 (1937).
  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, 25-83
  5. Theorell, H.
    Kinetics and equilibria in the liver alcohol dehydrogenase system.
    Adv. Enzymol. Relat. Subj. Biochem. 20: 31-49 (1958).

[EC 1.1.1.1 created 1961]