KEGG   ENZYME: 1.17.1.5Help
Entry
EC 1.17.1.5                 Enzyme                                 

Name
nicotinate dehydrogenase;
nicotinic acid hydroxylase;
nicotinate hydroxylase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
nicotinate:NADP+ 6-oxidoreductase (hydroxylating)
Reaction(IUBMB)
nicotinate + H2O + NADP+ = 6-hydroxynicotinate + NADPH + H+ [RN:R01720]
Reaction(KEGG)
Substrate
nicotinate [CPD:C00253];
H2O [CPD:C00001];
NADP+ [CPD:C00006]
Product
6-hydroxynicotinate [CPD:C01020];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
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.
History
EC 1.17.1.5 created 1972 as EC 1.5.1.13, transferred 2004 to EC 1.17.1.5
Pathway
ec00760  Nicotinate and nicotinamide metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K20445  nicotinate dehydrogenase FAD-subunit
K20446  nicotinate dehydrogenase small FeS subunit
K20447  nicotinate dehydrogenase large molybdopterin subunit
K20448  nicotinate dehydrogenase medium molybdopterin subunit
Genes
DTI: Desti_0416 Desti_0691
GGH: GHH_c21850(pucD2)
GEA: GARCT_02058(pucD)
CPAT: CLPA_c02860(ndhF1) CLPA_c02870(ndhS1) CLPA_c02880(ndhL)
CPAE: CPAST_c02860(ndhF1) CPAST_c02870(ndhS1) CPAST_c02880(ndhL)
AMT: Amet_4569
AOE: Clos_0375 Clos_0377
DOR: Desor_0445 Desor_0446 Desor_1381
DAI: Desaci_2061 Desaci_2062 Desaci_2063
DMI: Desmer_1309 Desmer_1310
CHY: CHY_0690(coxM)
 » show all
Taxonomy
Reference
1  [PMID:4388026]
  Authors
Holcenberg JS, Stadtman ER.
  Title
Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase.
  Journal
J. Biol. Chem. 244 (1969) 1194-203.
Reference
2  [PMID:8555176]
  Authors
Gladyshev VN, Khangulov SV, Stadtman TC.
  Title
Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri.
  Journal
Biochemistry. 35 (1996) 212-23.
  Sequence
Reference
3  [PMID:8278371]
  Authors
Gladyshev VN, Khangulov SV, Stadtman TC.
  Title
Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 232-6.
Reference
4  [PMID:6838209]
  Authors
Dilworth GL.
  Title
Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri.
  Journal
Arch. Biochem. Biophys. 221 (1983) 565-9.
Reference
5  [PMID:7181513]
  Authors
Dilworth GL.
  Title
Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri.
  Journal
Arch. Biochem. Biophys. 219 (1982) 30-8.
Reference
6
  Authors
Nagel, M. and Andreesen, J.R.
  Title
Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini.
  Journal
Arch. Microbiol. 154 (1990) 605-613.
Other DBs
ExplorEnz - The Enzyme Database: 1.17.1.5
IUBMB Enzyme Nomenclature: 1.17.1.5
ExPASy - ENZYME nomenclature database: 1.17.1.5
BRENDA, the Enzyme Database: 1.17.1.5
CAS: 9059-03-4

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