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Alcohol dehydrogenase (nicotinoprotein)
Identifiers
EC no. 1.1.99.36
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
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NCBI proteins

Alcohol dehydrogenase (nicotinoprotein) ( EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

ethanol + acceptor acetaldehyde + reduced acceptor

This enzyme contains Zn2+.

References

  1. ^ Van Ophem PW, Van Beeumen J, Duine JA (March 1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica". European Journal of Biochemistry. 212 (3): 819–26. doi: 10.1111/j.1432-1033.1993.tb17723.x. PMID  8385013.
  2. ^ Piersma SR, Visser AJ, de Vries S, Duine JA (March 1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase". Biochemistry. 37 (9): 3068–77. doi: 10.1021/bi972115u. PMID  9485460.
  3. ^ Schenkels P, Duine JA (April 2000). "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". Microbiology. 146 ( Pt 4) (4): 775–85. doi: 10.1099/00221287-146-4-775. PMID  10784035.
  4. ^ Piersma SR, Norin A, de Vries S, Jörnvall H, Duine JA (July 2003). "Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site". Journal of Protein Chemistry. 22 (5): 457–61. doi: 10.1023/b:jopc.0000005461.53788.ee. PMID  14690248.
  5. ^ Norin A, Piersma SR, Duine JA, Jörnvall H (May 2003). "Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations". Cellular and Molecular Life Sciences. 60 (5): 999–1006. doi: 10.1007/s00018-003-3105-9. PMC  11138879. PMID  12827287.

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