EC 1.17.1.5 - Nicotinate dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.17.1.5

Names

Accepted name:
nicotinate dehydrogenase
Other names:
nicotinate hydroxylase
nicotinic acid hydroxylase
Systematic name:
nicotinate:NADP+ 6-oxidoreductase (hydroxylating)

Reaction

Cofactors

Comments:

A flavoprotein containing non-heme iron. The enzyme is capable of acting on a variety of nicotinate analogues to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3-dicarboxylate, trigonelline and 6-methylnicotinate. The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide. Requires a cobamide coenzyme. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 3.5.2.18 (enamidase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050138
CAS Registry Number: 9059-03-4
UniProtKB/Swiss-Prot:

References

  1. Holcenberg, J.S. and Stadtman, E.R.
    Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.
    J. Biol. Chem. 244: 1194-1203 (1969). [PMID: 4388026]
  2. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C.
    Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri.
    Biochemistry 35: 212-223 (1996). [PMID: 8555176]
  3. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C.
    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. USA 91: 232-236 (1994). [PMID: 8278371]
  4. Dilworth, G.L.
    Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri.
    Arch. Biochem. Biophys. 221: 565-569 (1983). [PMID: 6838209]
  5. Dilworth, G.L.
    Properties of the selenium-containing moiety of nicotinic-acid hydroxylase from Clostridium barkeri.
    Arch. Biochem. Biophys. 219: 30-38 (1983).
  6. Nagel, M. and Andreesen, J.R.
    Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini.
    Arch. Microbiol. 154: 605-613 (1990).

[EC 1.17.1.5 created 1972 as EC 1.5.1.13, transferred 2004 to EC 1.17.1.5]