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
1.14.13.114
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RECOMMENDED NAME
GeneOntology No.
6-hydroxynicotinate 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
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-
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PATHWAY
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6-hydroxynicotinic acid 3-monooxygenase
-
-
6-hydroxynicotinic acid 3-monooxygenase
Pseudomonas fluorescens TN5
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-
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6HNA monooxygenase
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Pseudomonas fluorescens TN5
strain TN5
-
-
Manually annotated by BRENDA team
strain KT2440
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens TN5
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6.0% relative activity compared with 6-hydroxynicotinate
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH, NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
Pseudomonas fluorescens TN5
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH, NADH is 5times more effective than NADPH
-
-
?
additional information
?
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Pseudomonas fluorescens, Pseudomonas fluorescens TN5
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3-hydroxybenzoate (0.49% relative activity compared with 6-hydroxynicotinate), 2-hydroxybenzoate (0.18% compared with 6-hydroxynicotinate), 2-hydroxynicotinate (0.31% relative activity compared with 6-hydroxynicotinate) and 6-hydroxypyrazine carboxylate (0.19% relative activity compared with 6-hydroxynicotinate) are less effecive substrates or, in the case of nicotinate, 6-methylnicotinate and benzoate, not substrates at all
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
-
-
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens TN5
-
aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADH
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the enzyme activity is NADH-dependent and FAD-dependent. NADH is 5times more effective than NADPH
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 ACCESSION NO.
COMMENTARY
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
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
HgCl2
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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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.15
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4-hydroxybenzoate
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pH 7.0, 30°C
0.098
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6-Hydroxynicotinate
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pH 7.0, 30°C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.49
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nicotinate
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas fluorescens TN5
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bound to
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 42000, SDS-PAGE
monomer
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1 * 40000-42000, SDS-PAGE; 1 * 42886, including the starting methionine, calculated from sequence
monomer
Pseudomonas fluorescens TN5
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1 * 40000-42000, SDS-PAGE; 1 * 42886, including the starting methionine, calculated from sequence
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pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
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35°C, 10 min, stable between pH 6.0 and pH 9.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
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the isolated enzyme is used for the synthesis of 2,5-dihydroxypyridine, a precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
synthesis
Pseudomonas fluorescens TN5
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the isolated enzyme is used for the synthesis of 2,5-dihydroxypyridine, a precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
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