Information on EC 1.14.13.35 - anthranilate 3-monooxygenase (deaminating)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.35
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RECOMMENDED NAME
GeneOntology No.
anthranilate 3-monooxygenase (deaminating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
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hydroxylation
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oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminobenzoate degradation
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SYSTEMATIC NAME
IUBMB Comments
anthranilate,NADPH:oxygen oxidoreductase (3-hydroxylating, deaminating)
The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-68-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydrazinebenzoate + NADH + O2
?
show the reaction diagram
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?
2-thiobenzoate + NADPH + O2
?
show the reaction diagram
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?
3-hydroxyanthranilate + NADPH + O2
?
show the reaction diagram
3-methylanthranilate + NADPH + O2
? + NADP+ + NH3
show the reaction diagram
4-fluoroanthranilate + NADPH + O2
4-fluoro-2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
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-
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?
5-fluoroanthranilate + NADPH + O2
5-fluoro-2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
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?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
N,N-dimethylanthranilate + NADPH + O2
?
show the reaction diagram
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?
N-methylanthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
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?
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
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
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2% of the activity when NADPH is replaced by NADH, no effect: FAD, FMN
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-dipyridyl
3-hydroxyanthranilic acid
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3-Hydroxybenzoic acid
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8-hydroxyquinoline
cycloheximide
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inhibits the enzyme induction
diethyldithiocarbamate
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EDTA
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7% inhibition at 1 mM
Heavy metal ions
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N-ethylmaleimide
p-chloromercuribenzoate
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p-hydroxymercuribenzoate
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96% inhibition at 0.5 mM
Salicylaldoxime
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aminonicotinate
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activates
3-Hydroxyanthranilate
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induces
anthranilate
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induces, the enzyme activity increases with an increase in the concentration of anthranilate in the growth medium, optimal amounts of the enzyme are synthesized when the concentration of anthranilate is 1 mg/ml, further increase in the concentration results in a considerable decrease in the growth of the organism as well in the enzyme activity
indole
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0.02% induces the enzyme 516fold
kynurenine
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induces
L-tryptophan
N-Formyl anthranilate
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activates
salicylate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
anthranilic acid
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0.16
NADPH
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Trichosporon cutaneum
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0026
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organism grown on the standard medium with kynurenine
0.0032
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organism grown on the standard medium with tryptophan
0.0056
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organism grown on the standard medium with 3-hydroxyanthranilate
0.0058
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organism grown on the standard medium with anthranilate
0.041
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extracts of tryptophan-grown cells
0.05
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in cell extracts grown on glucose
0.0507
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; partially purified enzyme
0.28
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organism grown on iron-deficient medium, no addition of other constituents
1.02
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partially purified enzyme
2.2
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organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 5 min
4.2
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organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 10 min
4.6
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organism grown on iron-deficient medium, addition of 1 mM ferric-EDTA
4.9
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organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 15, 20 or 30 min
5.6
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organism grown on standard iron-sufficient medium
25.8
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in cell extracts grown on glucose plus indole
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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for optimal induction
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.8
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less than 1% of maximal activity at pH 5.5 and pH 9.8
7.5 - 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
89000
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gel filtration
95000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9 - 9.1
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4C, stable for at least 3 days
438866
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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half-life: 14 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glutathione stabilizes
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the enzyme is inactivated by treatment with ammonium sulfate or by adsorption on DEAE-cellulose or CM-cellulose, filtration through Sephadex G-25 or dialysis against 0.025 M sodium phosphate buffer, pH 7, containing 1 mM GSH irreversibly inactivates the enzyme
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
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inactivates the enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% inactivation of the purified enzyme after 2 days
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-20C, ammonium sulfate precipitate, stable for at least 3 months
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-20C, in the dark, Na+/K+ phosphate buffer, pH 7.4, 0.1 mM EDTA, stable for at least 6 months
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frozen, mycelium, no appreciable loss of activity after 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial, using centrifugation, protamine sulfate treatment, treatment with diethylaminoethyl-cellulose and filtration through a Buchner funnel
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partial, using heat treatment, DEAE-cellulose column chromatography and elution with a linear gradient of 0 to 0.1 M KCl in phosphate buffer
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partial, using protamine sulfate treatment, DEAE-cellulose treatment, alumina C-gamma treatment and hydroxylapatite treatment
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using ammonium sulfate precipitation, column chromatography on DE23-cellulose, phenyl-Sepharose and S-300 Sephacryl
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using protamine sulfate treatment, DEAE-cellulose treatment and alumina C-gamma treatment
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using protamine sulfate treatment, DEAE-cellulose treatment, ammonium sulfate precipitation, fractionation on Biogel P-100 column, successive negative adsorption on alumina-gel, tricalcium phosphate gel and DEAE-cellulose column, and positive adsorption on a DEAE-Sephadex A-50 column
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