Nicotinate dehydrogenase
nicotinate dehydrogenase | |||||||||
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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 | ||||||||
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In enzymology, a nicotinate dehydrogenase (EC 1.17.1.5) is an enzyme that catalyzes the chemical reaction
![Nicotinate dehydrogenase.svg](http://upload.wikimedia.org/wikipedia/commons/thumb/e/ed/Nicotinate_dehydrogenase.svg/400px-Nicotinate_dehydrogenase.svg.png)
nicotinate + H2O + NADP+ 6-hydroxynicotinate + NADPH + H+
The 3 substrates of this enzyme are nicotinate, H2O, and NADP+, whereas its 3 products are , 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.
Categories:
- EC 1.17.1
- NADPH-dependent enzymes
- Flavin enzymes
- Iron enzymes
- Enzymes of unknown structure
- Oxidoreductase stubs