Information on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.114
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RECOMMENDED NAME
GeneOntology No.
6-hydroxynicotinate 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nicotinate degradation I
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Nicotinate and nicotinamide metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
6-hydroxynicotinate,NADH:oxygen oxidoreductase (3-hydroxylating, decarboxylating)
A flavoprotein (FAD) [1]. The reaction is involved in the aerobic catabolism of nicotinic acid.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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Manually annotated by BRENDA team
Bordetella bronchiseptica ATCC BAA-588 / NCTC 13252 / RB50
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
modeling of substrate 6-hydroxynicotinate into the active site, substrate binding site structure, overview. The nicC gene in Pseudomonas putida strain KT2440 has been misidentified as salicylate hydroxylase, nahG
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
show the reaction diagram
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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riboflavin or FMN do not serve as enzyme cofactors
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
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1 mM, complete inhibition
6-hydroxynicotinaldehyde
competitive inhibition with respect to 6-hydroxynicotinate is weak
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Ag2SO4
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1 mM, complete inhibition
CuCl2
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1 mM, complete inhibition
HgCl2
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1 mM, complete inhibition
methylmethanethiosulfonate
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N-ethylmaleimide
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1 mM, 69% inhibition
nicotinate
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potent competitive inhibitor
p-chloromercuribenzoate
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1 mM, complete inhibition
additional information
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no significant effect on enzyme activity is found with metal-chelating agents such o-phenanthroline, 8-hydroxyquinoline, EDTA, disodium 4,5-dihydroxy-m-benzenedisulfonate, fluoride and azide, and other compounds such as KCl, LiCl, NaCl, BaCl2, CaCl2, MnCl2, MgCl2, PbCl2, ZnCl2, CoCl2, SnCl2, FeSO4, FeCl3, NiCl2, CdCl2, AlCl3, iodoacetic acid, hydroxylamine, phenylhydrazine, semicarbazide, cysteamine, alpha,alpha'-dipyridyl and urea
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
4-hydroxybenzoate
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pH 7.0, 30C
0.085 - 0.098
6-Hydroxynicotinate
0.003 - 0.006
NADH
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 4.2
6-Hydroxynicotinate
2.2 - 4.2
NADH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.6 - 49.4
6-Hydroxynicotinate
700 - 733.3
NADH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.98
6-hydroxynicotinaldehyde
pH 7.5, 25C, recombinant enzyme
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0.49
nicotinate
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additional information
additional information
inhibition kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH-dependence of the enzyme fitting to a double-bell curve pH-rate profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
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x * 42000, SDS-PAGE
42886
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1 * 42886, including the starting methionine, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
structure of the PpNicC monomer, modeling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged selenomethionine-labeled enzyme, hanging drop vapor diffusion method, mixing of 0.0015 ml of protein solution with 0.0015 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.7-8.3, 27-30% PEG 4000, and 0.2 M magnesium chloride hexahydrate, 18C, 2-3 days, method optimization, X-ray diffraction structure determination and analysis using SAD phasing at 2.1 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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35C, 10 min, stable between pH 6.0 and pH 9.0
697700
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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pH 7.0, 10 min, in the absence of FAD, apoenzyme is stable below
40
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pH 7.0, 10 min, in the presence of 0.5 mM FAD, holoenzyme is stable below
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene Bb1770, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strains MachI and BL21(DE3)
gene nicC, DNA and amino acid sequence determination and analysis, sequence comparisons
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gene nicC, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strains MachI and BL21(DE3)
the nicC gene is cloned and expressed in Pseudomonas fluorescens (plasmid pIZNicC)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
Show AA Sequence (272 entries)
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