KEGG   ENZYME: 1.1.99.36Help
Entry
EC 1.1.99.36                Enzyme                                 

Name
alcohol dehydrogenase (nicotinoprotein);
NDMA-dependent alcohol dehydrogenase;
nicotinoprotein alcohol dehydrogenase;
np-ADH;
ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
ethanol:acceptor oxidoreductase
Reaction(IUBMB)
ethanol + acceptor = acetaldehyde + reduced acceptor [RN:R09552]
Reaction(KEGG)
Substrate
ethanol [CPD:C00469];
acceptor [CPD:C00028]
Product
acetaldehyde [CPD:C00084];
reduced acceptor [CPD:C00030]
Comment
Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro.
The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
History
EC 1.1.99.36 created 2010
Reference
1  [PMID:8385013]
  Authors
Van Ophem PW, Van Beeumen J, Duine JA
  Title
Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica.
  Journal
Eur. J. Biochem. 212 (1993) 819-26.
Reference
2  [PMID:9485460]
  Authors
Piersma SR, Visser AJ, de Vries S, Duine JA
  Title
Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis  methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.
  Journal
Biochemistry. 37 (1998) 3068-77.
Reference
3  [PMID:10784035]
  Authors
Schenkels P, Duine JA
  Title
Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.
  Journal
Microbiology. 146 ( Pt 4) (2000) 775-85.
Reference
4  [PMID:14690248]
  Authors
Piersma SR, Norin A, de Vries S, Jornvall H, Duine JA
  Title
Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site.
  Journal
J. Protein. Chem. 22 (2003) 457-61.
Reference
5  [PMID:12827287]
  Authors
Norin A, Piersma SR, Duine JA, Jornvall H
  Title
Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations.
  Journal
Cell. Mol. Life. Sci. 60 (2003) 999-1006.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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