Nicotinate dehydrogenase

nicotinate dehydrogenase
Identifiers
EC number	1.17.1.5
CAS number	9059-03-4
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 / EGO
Search PMC articles PubMed articles

In enzymology, a nicotinate dehydrogenase (EC 1.17.1.5) is an enzyme that catalyzes the chemical reaction

nicotinate + H₂O + NADP⁺ $\rightleftharpoons$ 6-hydroxynicotinate + NADPH + H⁺

The 3 substrates of this enzyme are nicotinate, H₂O, and NADP⁺, whereas its 3 products are 6-hydroxynicotinate, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 group with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is nicotinate:NADP+ 6-oxidoreductase (hydroxylating). Other names in common use include nicotinic acid hydroxylase, and nicotinate hydroxylase. This enzyme participates in nicotinate and nicotinamide metabolism. It has 2 cofactors: FAD, and Iron.

References

• Holcenberg JS, Stadtman ER (1969). "Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase". J. Biol. Chem. 244 (5): 1194–203. PMID 4388026. 
• Gladyshev VN, Khangulov SV, Stadtman TC (1996). "Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri". Biochemistry. 35 (1): 212–23. doi:10.1021/bi951793i. PMID 8555176. 
• Gladyshev VN, Khangulov SV, Stadtman TC (1994). "Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme". Proc. Natl. Acad. Sci. U. S. A. 91 (1): 232–6. doi:10.1073/pnas.91.1.232. PMC 42921. PMID 8278371. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42921. 
• Dilworth GL (1983). "Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri". Arch. Biochem. Biophys. 221 (2): 565–9. doi:10.1016/0003-9861(83)90176-5. PMID 6838209. 
• Dilworth GL (1983). "Properties of the selenium-containing moiety of nicotinic-acid hydroxylase from Clostridium barkeri". Arch. Biochem. Biophys. 219 (1): 30–38. doi:10.1016/0003-9861(82)90130-8. PMID 7181513. 
• Nagel M and Andreesen JR (1990). "Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini". Arch. Microbiol. 154: 605–613. 

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