ExplorEnz: EC 1.17.1.5

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1.17.1.5

Accepted name:

nicotinate dehydrogenase

Reaction:

nicotinate + H₂O + NADP⁺ = 6-hydroxynicotinate + NADPH + H⁺

For diagram of nicotinate catabolism, click here

Other name(s):

nicotinic acid hydroxylase; nicotinate hydroxylase

Systematic name:

nicotinate:NADP⁺ 6-oxidoreductase (hydroxylating)

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.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9059-03-4

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 (1969) 1194–1203. [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 (1996) 212–223. [DOI] [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 (1994) 232–236. [DOI] [PMID: 8278371]
4.	Dilworth, G.L. Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 221 (1983) 565–569. [DOI] [PMID: 6838209]
5.	Dilworth, G.L. Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 219 (1982) 30–38. [DOI] [PMID: 7181513]
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 (1990) 605–613.

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