| 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 | ||||||||
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In enzymology, a nicotinate dehydrogenase (EC 1.17.1.5) is an enzyme that catalyzes the chemical reaction
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.
| Other oxidoreductases (EC 1.15–1.21) | |
|---|---|
| 1.15: Acting on superoxide as acceptor | |
| 1.16: Oxidizing metal ions | |
| 1.17: Acting on CH or CH2 groups | |
| 1.18: Acting on iron–sulfur proteins as donors | |
| 1.19: Acting on reduced flavodoxin as donor | |
| 1.20: Acting on phosphorus or arsenic in donors | |
| 1.21: Acting on X-H and Y-H to form an X-Y bond | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
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