EC 188.8.131.52 - Nicotinate dehydrogenase
IntEnz Enzyme Nomenclature
nicotinic acid hydroxylase
12236 [IUBMB]H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)NADP+NADP(+)Name origin: UniProt - CHECKED (C)Formula: C21H25N7O17P3
Charge: -3ChEBI compound status: CHECKED (C)nicotinatenicotinateName origin: UniProt - CHECKED (C)Formula: C6H4NO2
Charge: -1ChEBI compound status: CHECKED (C)=6-hydroxynicotinate6-hydroxynicotinateName origin: UniProt - CHECKED (C)Formula: C6H4NO3
Charge: -1ChEBI compound status: CHECKED (C)H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)
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 184.108.40.206 (6-hydroxynicotinate reductase), EC 220.127.116.11 (enamidase), EC 18.104.22.1681 (2-hydroxymethylglutarate dehydrogenase), EC 22.214.171.124 (2-methyleneglutarate mutase), EC 126.96.36.199 (methylitaconate Δ-isomerase), EC 188.8.131.52 (dimethylmaleate hydratase) and EC 184.108.40.206 (2,3-dimethylmalate lyase).
Links to other databases
Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.J. Biol. Chem. 244: 1194-1203 (1969). [PMID: 4388026]
Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri.Biochemistry 35: 212-223 (1996). [PMID: 8555176]
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]
Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri.Arch. Biochem. Biophys. 221: 565-569 (1983). [PMID: 6838209]
Properties of the selenium-containing moiety of nicotinic-acid hydroxylase from Clostridium barkeri.Arch. Biochem. Biophys. 219: 30-38 (1983).
Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini.Arch. Microbiol. 154: 605-613 (1990).
[EC 220.127.116.11 created 1972 as EC 18.104.22.168, transferred 2004 to EC 22.214.171.124]