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Information on EC 1.14.12.1 - anthranilate 1,2-dioxygenase (deaminating, decarboxylating) for references in articles please use BRENDA:EC1.14.12.1
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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
antdo, two-component anthranilate 1,2-dioxygenase,
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anthranilate hydroxylase
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anthranilic acid hydroxylase
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anthranilic hydroxylase
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two-component anthranilate 1,2-dioxygenase
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anthranilate + NAD(P)H + 2 H+ + O2 = catechol + CO2 + NAD(P)+ + NH3
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anthranilate,NAD(P)H:oxygen oxidoreductase (1,2-hydroxylating, deaminating, decarboxylating)
Requires Fe2+.
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2,3-dihydroxybenzoic acid + NAD(P)H + O2 + H2O
?
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?
anthranilate + NADPH + H+ + O2
catechol + CO2 + NADP+ + NH3
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?
anthranilic acid + alanine + O2
?
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
anthranilic acid + NADH + O2 + H2O
catechol + CO2 + NAD+ + NH3
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?
benzoate + NAD(P)H + O2 + H2O
benzoate dihydrodiol + ?
catechol + O2 + NAD(P)H + H2O
?
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?
protocatechuic acid + NAD(P)H + O2 + H2O
?
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?
salicylic acid + NAD(P)H + O2 + H2O
?
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?
additional information
?
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salicylic acid and o-aminophenol are no substrates
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anthranilic acid + alanine + O2
?
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?
anthranilic acid + alanine + O2
?
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?
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
involved in the tryptophan degradation pathway
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?
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds, enables growth on anthranilate as sole carbon source
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
benzoate + NAD(P)H + O2 + H2O
benzoate dihydrodiol + ?
poor substrate
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?
benzoate + NAD(P)H + O2 + H2O
benzoate dihydrodiol + ?
poor substrate
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?
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anthranilate + NADPH + H+ + O2
catechol + CO2 + NADP+ + NH3
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?
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
Q84BZ2, Q84BZ3
involved in the tryptophan degradation pathway
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?
anthranilic acid + alanine + O2
catechol + CO2 + NH3 + ?
Q84BZ2, Q84BZ3
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds, enables growth on anthranilate as sole carbon source
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
Q84BZ2, Q84BZ3
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
Q84BZ2, Q84BZ3
involved in the tryptophan degradation pathway
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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initial step in aerobic degradation of aromatic compounds
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?
anthranilic acid + NAD(P)H + O2 + H2O
catechol + CO2 + NAD(P)+ + NH3
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?
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iron-sulfur centre
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proximal Rieske [2Fe-2S] center
iron-sulfur centre
proximal Rieske [2Fe-2S] center; proximal Rieske [2Fe-2S] center
iron-sulfur centre
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proximal Rieske [2Fe-2S] center
NADH
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NADPH
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NAD+ + NADP+ do not replace NADH or NADPH
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p-chloromercuribenzoate
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additional information
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oxygenase component completely inactive at pH 9
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brenda
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brenda
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brenda
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brenda
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brenda
wild-type ATCC 15926, ATCC 29574
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brenda
No.23 (ATCC 11250)
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brenda
two component type of enzyme
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brenda
two component type of enzyme
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brenda
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brenda
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brenda
derived from BD413
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brenda
large subunit; three component type of enzyme
SwissProt
brenda
small subunit; three component type of enzyme
SwissProt
brenda
large subunit; three component type of enzyme
SwissProt
brenda
small subunit; three component type of enzyme
SwissProt
brenda
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18900
AndAd, product of ORF4, calculated from deduced amino acid sequence; AndAd, product of ORF4, calculated from deduced amino acid sequence
19000
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1 * 19000 + 1 * 39000 + 1 * 54000, DNA-sequence
24000
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apha, beta, 3 * 52000 + 3 * 24000, SDS-PAGE, native mass by gel filtration
39000
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1 * 19000 + 1 * 39000 + 1 * 54000, DNA-sequence
48000
AndAc, product of ORF3, calculated from deduced amino acid sequence; AndAc, product of ORF3, calculated from deduced amino acid sequence
52000
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apha, beta, 3 * 52000 + 3 * 24000, SDS-PAGE, native mass by gel filtration
54000
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1 * 19000 + 1 * 39000 + 1 * 54000, DNA-sequence
220000
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gel filtration, wild type and mutant enzymes
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hexamer
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apha, beta, 3 * 52000 + 3 * 24000, SDS-PAGE, native mass by gel filtration
trimer
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1 * 19000 + 1 * 39000 + 1 * 54000, DNA-sequence
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recombinant protein, expressed in Escherichia coli
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wild type and mutant enzymes
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clustered antABC genes from ADP1 chromosome encodes anthranilate dioxygenase
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clustered antABC genes from ADP1 chromosome encodes anthranilate dioxygenase; expressed in Escherichia coli
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expressed in Escherichia coli TOP10F'; expressed in Escherichia coli TOP10F'
expressed in Escherichia coli W3110 trpD9923 cells
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expression of mutant enzymes in Escherichia coli BL21-Codon Plus
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Bundy, B.M.; Campbell, A.L.; Neidle, E.L.
Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1
J. Bacteriol.
180
4466-4474
1998
Acinetobacter sp., Pseudomonas sp.
brenda
Taniuchi, H.; Hatanaka, M.; Kuno, S.; Hayaishi, O.; Nakajima, M.; Kurihara, N.
Enzymatic formation of catechol from anthranilic acid
J. Biol. Chem.
239
2204-2211
1964
Pseudomonas fluorescens
brenda
Roenberg, S.L.; Hegeman, G.D.
Genetics of the mandelate pathway in Pseudomonas aeruginosa
J. Bacteriol.
108
1270-1276
1971
Pseudomonas aeruginosa
brenda
Wheels, M.L.
Regulation of the synthesis of enzymes of tryptophan dissimilation in Acinetobacter calcoaceticus
Arch. Mikrobiol.
87
1-9
1972
Acinetobacter calcoaceticus
brenda
Salcher, O.; Lingens, F.
Metabolism of tryptophan by Pseudomonas aureofaciens and its relationship to pyrrolnitrin biosynthesis
J. Gen. Microbiol.
121
465-471
1980
Pseudomonas chlororaphis subsp. aureofaciens
brenda
Macheroux, Peter; Kojiro, C.L.; Schopfer, L.M.; Chakraborty, S.; Massey, V.
F NMR studies on fluoroflavins and 8-fluoroflavoproteins
Biochemistry
29
2670-2679
1990
Cutaneotrichosporon cutaneum
brenda
Eby, D.M.; Beharry, Z.M.; Coulter, E.D.; Kurtz, D.M., Jr.; Neidle, E.L.
Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1
J. Bacteriol.
183
109-118
2001
Acinetobacter sp., Pseudomonas sp.
brenda
Beharry, Z.M.; Eby, D.M.; Coulter, E.D.; Viswanathan, R.; Neidle, E.L.; Phillips, R.S.; Kurtz, D.M., Jr.
Histidine ligand protonation and redox potential in the Rieske dioxygenases: Role of a conserved aspartate in anthranilate 1,2-Dioxygenase
Biochemistry
42
13625-13636
2003
Acinetobacter sp.
brenda
Chang, H.K.; Mohseni, P.; Zylstra, G.J.
Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1
J. Bacteriol.
185
5871-5881
2003
Burkholderia cepacia, Burkholderia cepacia (Q84BZ2), Burkholderia cepacia (Q84BZ3), Burkholderia cepacia DBO1 / ATCC 29424 (Q84BZ2), Burkholderia cepacia DBO1 / ATCC 29424 (Q84BZ3)
brenda
Urata, M.; Miyakoshi, M.; Kai, S.; Maeda, K.; Habe, H.; Omori, T.; Yamane, H.; Nojiri, H.
Transcriptional regulation of the ant operon, encoding two-component anthranilate 1,2-dioxygenase, on the carbazole-degradative plasmid pCAR1 of Pseudomonas resinovorans strain CA10
J. Bacteriol.
186
6815-6823
2004
Pseudomonas resinovorans, Pseudomonas resinovorans CA10
brenda
Iwaki, H.; Hasegawa, Y.
Degradation of 2-nitrobenzoate by Burkholderia terrae strain KU-15
Biosci. Biotechnol. Biochem.
71
145-151
2007
Paraburkholderia terrae, Paraburkholderia terrae KU-15
brenda
Balderas-Hernandez, V.; Trevino-Quintanilla, L.; Hernandez-Chavez, G.; Martinez, A.; Bolivar, F.; Gosset, G.
Catechol biosynthesis from glucose in Escherichia coli anthranilate-overproducer strains by heterologous expression of anthranilate 1,2-dioxygenase from Pseudomonas aeruginosa PAO1
Microb. Cell Fact.
13
136
2014
Pseudomonas aeruginosa
brenda
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1.14.12.1 anthranilate 1,2-dioxygenase (deaminating, decarboxylating)
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