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Enzyme Nomenclature
Information on EC 1.14.13.114 - 6-hydroxynicotinate 3-monooxygenase
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The expected taxonomic range for this enzyme is: Pseudomonas
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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
LITERATURE
6-hydroxynicotinate + NADH + H+ + O2 = 2,5-dihydroxypyridine + NAD+ + H2O + CO2
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
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6.0% relative activity compared with 6-hydroxynicotinate
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-
?
4-hydroxybenzoate + NADH + H+ + O2
hydroquinone + NAD+ + H2O + CO2
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6.0% relative activity compared with 6-hydroxynicotinate
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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NADH is 5times more effective than NADPH
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-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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-
-
-
?
additional information
?
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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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additional information
?
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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aerobic catabolism of nicotinic acid. NADH is 5times more effective than NADPH
-
-
?
6-hydroxynicotinate + NADH + H+ + O2
2,5-dihydroxypyridine + NAD+ + H2O + CO2
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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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NADH
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the enzyme activity is NADH-dependent and FAD-dependent. NADH is 5times more effective than NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42886
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1 * 42886, including the starting methionine, calculated from sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
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1 * 40000-42000, SDS-PAGE; 1 * 42886, including the starting methionine, calculated from sequence
monomer
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1 * 40000-42000, SDS-PAGE; 1 * 42886, including the starting methionine, calculated from sequence
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the nicC gene is cloned and expressed in Pseudomonas fluorescens (plasmid pIZNicC)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.114)
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