Nicotinate dehydrogenase

nicotinate dehydrogenase
Identifiers
EC no.	1.17.1.5
CAS no.	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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

nicotinate + H₂O + NADP⁺${\displaystyle \rightleftharpoons }$ 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⁺.

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. doi: 10.1016/S0021-9258(18)91829-6 . 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 (6): 605–613. doi:10.1007/BF00248844. S2CID   21544639.