Nicotinate dehydrogenase

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

nicotinate + H2O + NADP+ 6-hydroxynicotinate + NADPH + H+
nicotinate dehydrogenase
Identifiers
EC number1.17.1.5
CAS number9059-03-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

Classification

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor.

Nomenclature

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.

Biological role

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.
    • 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; Andreesen JR (1990). "Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini". Arch. Microbiol. 154: 605–613. doi:10.1007/BF00248844.


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