Alcohol dehydrogenase (nicotinoprotein)

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Alcohol dehydrogenase (nicotinoprotein)
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
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PubMed	articles
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

\rightleftharpoons

acetaldehyde + reduced acceptor

This enzyme contains Zn²⁺.

References

^ 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.
^ 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.
^ 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.
^ 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.
^ 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.

External links

Alcohol+dehydrogenase+(nicotinoprotein) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[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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v t e 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: 3β 3β-HSD NSDHL 11β 11β-HSD1 11β-HSD2 17β
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 Alcohol 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)