Alcohol dehydrogenase (nicotinoprotein)

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

\rightleftharpoons

acetaldehyde + reduced acceptor

This enzyme contains Zn²⁺.

References

↑ Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A. (1993). "Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica". Eur. J. Biochem. 212 (3): 819–826. doi:10.1111/j.1432-1033.1993.tb17723.x. PMID 8385013.
↑ Piersma, S.R.; Visser, A.J.; de Vries, S.; Duine, J.A. (1998). "Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase". Biochemistry. 37 (9): 3068–3077. doi:10.1021/bi972115u. PMID 9485460.
↑ Schenkels, P.; Duine, J.A. (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: 775–785. doi:10.1099/00221287-146-4-775. PMID 10784035.
↑ Piersma, S.R.; Norin, A.; de Vries, S.; Jornvall, H.; Duine, J.A. (2003). "Inhibition of nicotinoprotein (NAD⁺-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site". J. Protein Chem. 22 (5): 457–461. doi:10.1023/b:jopc.0000005461.53788.ee. PMID 14690248.
↑ Norin, A.; Piersma, S.R.; Duine, J.A.; Jornvall, H. (2003). "Nicotinoprotein (NAD⁺ -containing) alcohol dehydrogenase: structural relationships and functional interpretations". Cell. Mol. Life Sci. 60 (5): 999–1006. doi:10.1007/s00018-003-3105-9. PMID 12827287.

External links

Alcohol dehydrogenase (nicotinoprotein) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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