Information on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase

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The expected taxonomic range for this enzyme is: Pseudomonas

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
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Nicotinate and nicotinamide metabolism
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nicotinate degradation I
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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
strain TN5
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Manually annotated by BRENDA team
strain TN5
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Manually annotated by BRENDA team
strain KT2440
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Manually annotated by BRENDA team
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
FAD
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the enzyme activity is NADH-dependent and FAD-dependent. The holoenzyme contains 1 M of FAD per 1 M of enzyme. FAD gradually dissociates from the enzyme during purification. Without FAD, no pure enzyme activity is observed, but after the addition of FAD, the apoenzyme is activated immediately
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
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
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, 30°C
0.098
6-Hydroxynicotinate
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pH 7.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.49
nicotinate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 42000, SDS-PAGE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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35°C, 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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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the nicC gene is cloned and expressed in Pseudomonas fluorescens (plasmid pIZNicC)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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