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.
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]
Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C. Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri. Biochemistry35 (1996) 212–223. [PMID: 8555176]
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. USA91 (1994) 232–236. [PMID: 8278371]
Dilworth, G.L. Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys.221 (1983) 565–569. [PMID: 6838209]
Dilworth, G.L. Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys.219 (1982) 30–38. [PMID: 7181513]
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 188.8.131.52 created 1972 as EC 184.108.40.206, transferred 2004 to EC 220.127.116.11]