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Information on EC 1.14.13.35 - anthranilate 3-monooxygenase (deaminating)
for references in articles please use BRENDA:EC1.14.13.35
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.35 anthranilate 3-monooxygenase (deaminating)
IUBMB Comments
The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD).
The enzyme appears in viruses and cellular organisms
- 1.14.13.35
- flavoproteins
- flavin
- niger
-
trichosporon
- catechols
- salicylate
- 2,3-dihydroxybenzoate
-
deaminate
- cutaneum
- hydroxylases
- imine
-
nonhydroxylated
- fmn
- p-hydroxybenzoate
-
half-reaction
-
massey
- flavodoxin
- l-kynurenine
-
ballou
-
flavoenzyme
-
d-amino
showSynonyms
anthranilate hydroxylase, anthranilate hydroxylase (deaminating), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anthranilate 2,3-dioxygenase (deaminating)
-
-
-
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anthranilate 2,3-hydroxylase (deaminating)
-
-
-
-
anthranilate hydroxylase
-
-
-
-
anthranilate hydroxylase (deaminating)
-
-
-
-
anthranilic hydroxylase
-
-
-
-
EC 1.14.12.2
-
-
formerly
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
mechanism
-
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
mechanism proposed involving imine formation and hydrolysis during the reaction with the flavin peroxide formed from reduced enzyme flavin and molecular oxygen
-
anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
possible involvement of superoxide anion (O2-) in the reaction
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anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
hydroxylation
-
-
-
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oxidation
-
-
-
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redox reaction
-
-
-
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reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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).
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CAS REGISTRY NUMBER
COMMENTARY
37256-68-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-fluoroanthranilate + NADPH + O2
4-fluoro-2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
5-fluoroanthranilate + NADPH + O2
5-fluoro-2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
N,N-dimethylanthranilate + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
N-methylanthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
3-hydroxyanthranilate + NADPH + O2
?
-
Substrates: no activity
Products: -
Products: -
?
3-hydroxyanthranilate + NADPH + O2
?
-
Substrates: -
Products: -
Products: -
?
3-methylanthranilate + NADPH + O2
? + NADP+ + NH3
-
Substrates: no activity
Products: -
Products: -
?
3-methylanthranilate + NADPH + O2
? + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
3-methylanthranilate + NADPH + O2
? + NADP+ + NH3
-
Substrates: -
Products: the proposed structure of the product contains a ketone function at the position 2
Products: the proposed structure of the product contains a ketone function at the position 2
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: metabolism of indole
Products: -
Products: -
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: -
Products: -
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: -
Products: 2,3-dihydroxybenzoate i.e. o-pyrocatechuate, oxygen atom at the 3-position of the product 2,3-dihydroxybenzoate originates from O2, that at the 2-position is derived from H2O
Products: 2,3-dihydroxybenzoate i.e. o-pyrocatechuate, oxygen atom at the 3-position of the product 2,3-dihydroxybenzoate originates from O2, that at the 2-position is derived from H2O
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: enzyme in degradation of L-tryptophan
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with: 3-hydroxyanthranilic acid, benzoic acid, salicylic acid, m-hydroxybenzoic acid, p-hydroxybenzoic acid, m-aminobenzoic acid, p-aminobenzoic acid, methylanthranilate or ethylanthranilate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with: 3-hydroxyanthranilic acid, benzoic acid, salicylic acid, m-hydroxybenzoic acid, p-hydroxybenzoic acid, m-aminobenzoic acid, p-aminobenzoic acid, methylanthranilate or ethylanthranilate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: metabolism of indole
Products: -
Products: -
?
anthranilate + NADPH + O2
2,3-dihydroxybenzoate + NADP+ + NH3
-
Substrates: enzyme in degradation of L-tryptophan
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
2% of the activity when NADPH is replaced by NADH, no effect: FAD, FMN
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additional information
-
2% of the activity when NADPH is replaced by NADH, no effect: FAD, FMN
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
-
the partially purified enzyme is not activated by any metal ion but a considerable decrease in anthranilate hydroxylase activity occurs when the organism is grown on a medium deprived of iron
Iron
-
enzyme-bound iron, participation of Fe in reaction, omission of Fe in the growth medium yields inactive preparation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
50% inhibition at 0.25 mM, 80% inhibition at 0.5 mM and 95% inhibition at 1 mM
1,10-phenanthroline
-
46% inhibition at 0.5 mM , 60% inhibition at 1 mM, 80% inhibition at 3 mM, anthranilic acid protects the enzyme from inhibition
additional information
-
reversal of 1,10-phenanthroline inhibition by ferric-EDTA, ferrous-EDTA, ferric citrate and cytochrome c
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additional information
-
complete inhibition when superoxide dismutase is included in the reaction mixture for the assay of the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
anthranilate
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0507
0.28
-
organism grown on iron-deficient medium, no addition of other constituents
2.2
-
organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 5 min
4.2
-
organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 10 min
4.6
-
organism grown on iron-deficient medium, addition of 1 mM ferric-EDTA
4.9
-
organism grown on iron-deficient medium, addition of 1 mM ferric citrate, preincubation time: 15, 20 or 30 min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9.8
-
less than 1% of maximal activity at pH 5.5 and pH 9.8
7.5 - 9.5
7.5 - 9.5
-
pH 7.5: about 80% of activity maximum, pH 9.5: about 55% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in the dark, Na+/K+ phosphate buffer, pH 7.4, 0.1 mM EDTA, stable for at least 6 months
-
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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
-
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
-
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
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, J.J.; Dagley, S.
Catabolism of tryptophan, anthranilate, and 2,3-dihydroxybenzoate in Trichosporon cutaneum
J. Bacteriol.
146
291-297
1981
Cutaneotrichosporon cutaneum
brenda
Kamath, A.V.; Vaidyanathan, C.S.
New pathway for the biodegradation of indole in Aspergillus niger
Appl. Environ. Microbiol.
56
275-280
1990
Aspergillus niger
brenda
Manstein, D.J.; Pai, E.F.
Absolute stereochemistry of flavins in enzyme-catalyzed reactions
Biochemistry
25
6807-6816
1986
Cutaneotrichosporon cutaneum
brenda
Powlowski, J.B.; Dagley, S.; Massey, V.; Ballou, D.P.
Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum
J. Biol. Chem.
262
69-74
1987
Cutaneotrichosporon cutaneum
brenda
Subramanian, V.; Vaidyanathan, C.S.
Anthranilate hydroxylase from Aspergillus niger: new type of NADPH-linked nonheme iron monooxygenase
J. Bacteriol.
160
651-655
1984
Aspergillus niger
brenda
Powlowski, J.; Ballou, D.P.; Massey, V.
Studies of the oxidative half-reaction of anthranilate hydroxylase (deaminating) with native and modified substrates
J. Biol. Chem.
265
4969-4975
1990
Cutaneotrichosporon cutaneum
brenda
Powlowski, J.; Massey, V.; Ballou, D.P.
Reactions of anthranilate hydroxylase with salicylate, a nonhydroxylated substrate analogue. Steady state and rapid reaction kinetics
J. Biol. Chem.
264
5606-5612
1989
Cutaneotrichosporon cutaneum
brenda
Kumar, R.P.; Sreeleela, N.S.; Rao, P.V.S.; Vaidyanathan, C.S.
Anthranilate hydroxylase from Aspergillus niger: evidence for the participation of iron in the double hydroxylation reaction
J. Bacteriol.
113
1213-1216
1973
Aspergillus niger, Aspergillus niger UBC 814
brenda
Kumar, R.P.; Ravindranath, S.D.; Vaidyanathan, C.S.; Rao, N.A.
Mechanism of hydroxylation of aromatic compounds. II. Evidence for the involvement of superoxide anions in enzymatic hydroxylations
Biochem. Biophys. Res. Commun.
49
1422-1426
1972
Aspergillus niger
brenda
Rao, P.V.S.; Sreeleela, N.S.; Kumar, R.P.; Vaidyanathan, C.S.
Anthranilic acid hydroxylase (Aspergillus niger)
Methods Enzymol.
17A
510-513
1970
Aspergillus niger
-
brenda
Rao, P.V.S.; Sreeleela, N.S.; Premakumar, R.; Vaidyanathan, C.S.
Regulation of the pathway for the degradation of anthranilate in Aspergillus niger
J. Bacteriol.
107
100-105
1971
Aspergillus niger, Aspergillus niger UBC 814
brenda
Sreeleela, N.S.; SubraRao, P.V.; Premkumar, R.; Vaidyanathan, C.S.
A new anthranilic acid hydroxylase from Aspergillus niger. Purification and properties
J. Biol. Chem.
244
2293-2298
1969
Aspergillus niger
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.13.35)
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