Nicotine dehydrogenase

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nicotine dehydrogenase
nicotine dehydrogenase
Identifiers
EC no.	1.5.99.4
CAS no.	37256-31-8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
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PubMed	articles
NCBI	proteins

Last updated August 27, 2023

In enzymology, a nicotine dehydrogenase (EC 1.5.99.4) is an enzyme that catalyzes the chemical reaction

(S)-nicotine + acceptor + H₂O

\rightleftharpoons

(S)-6-hydroxynicotine + reduced acceptor

The 3 substrates of this enzyme are (S)-nicotine, acceptor, and H₂O, whereas its two products are (S)-6-hydroxynicotine and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is nicotine:acceptor 6-oxidoreductase (hydroxylating). Other names in common use include nicotine oxidase, D-nicotine oxidase, nicotine:(acceptor) 6-oxidoreductase (hydroxylating), and L-nicotine oxidase. It has 2 cofactors: metal, and FMN.

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In enzymology, a (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction

References

BEHRMAN EJ, STANIER RY (1957). "The bacterial oxidation of nicotinic acid". J. Biol. Chem. 228 (2): 923–45. PMID 13475371.
Decker K, Bleeg H (1965). "Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans". Biochim. Biophys. Acta. 105 (2): 313–24. doi:10.1016/s0926-6593(65)80155-2. PMID 5849820.
Hochstein LI, Dalton BP (1967). "The purification and properties of nicotine oxidase". Biochim. Biophys. Acta. 139 (1): 56–68. doi:10.1016/0005-2744(67)90113-1. PMID 4962139.
HOCHSTEIN LI, RITTENBERG SC (1959). "The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (1)-6-hydroxynicotine". J. Biol. Chem. 234 (1): 156–60. PMID 13610912.

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v t e Oxidoreductases: CH-NH (EC 1.5)
1.5.1: NAD or NADP acceptor	Dihydrofolate reductase Saccharopine dehydrogenase Methylenetetrahydrofolate reductase
1.5.3: oxygen acceptor	Dihydrobenzophenanthridine oxidase Sarcosine oxidase Proline oxidase
1.5.5: quinone acceptor	Electron-transferring-flavoprotein dehydrogenase
1.5.99	Sarcosine dehydrogenase Cytokinin dehydrogenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme 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)