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Information on EC 1.14.13.40 - anthraniloyl-CoA monooxygenase for references in articles please use BRENDA:EC1.14.13.40
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EC Tree
IUBMB Comments A flavoprotein (FAD). The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione.
The enzyme appears in viruses and cellular organisms
Synonyms
2-aminobenzoyl-coa monooxygenase/reductase, anthranoyl-coa monooxygenase/reductase,
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2-aminobenzoyl-CoA monooxygenase/reductase
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anthranoyl-CoA monooxygenase/reductase
-
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reductase, anthraniloyl coenzyme A
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anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
reaction mechanism
-
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
reaction mechanism
-
-
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
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2-aminobenzoyl-CoA,NAD(P)H:oxygen oxidoreductase (de-aromatizing)
A flavoprotein (FAD). The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione.
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2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
maleimide + NAD(P)H
succinimide + NAD(P)+
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
N-ethylmaleimide + NAD(P)H
succinimide + NAD(P)+
-
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
reaction mechanism
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
formation of 3 different products, the non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexadione
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
at least 2 different reaction products depending on the concentration of NADH
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
7 different products are formed, pattern is dependent on pH
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
product formed under physiological NADH concentration
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
i.e. anthraniloyl-CoA
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
pathway of aerobic breakdown of 2-aminobenzoate
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
7 different products are formed, pattern is dependent on pH
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
pathway of aerobic breakdown of 2-aminobenzoate
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
at least 2 different reaction products depending on the concentration of NADH
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
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-
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
i.e. anthraniloyl-CoA
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-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
-
7 different products are formed, pattern is dependent on pH
?
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
-
i.e. salicoyl-CoA, weak substrate, is probably monooxygenated but not hydrogenated
-
-
?
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
-
i.e. salicoyl-CoA, weak substrate, is probably monooxygenated but not hydrogenated
-
-
?
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
-
the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
-
-
?
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
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the enzyme catalyzes the monooxygenation of anthranoyl-CoA to 5-hydroxyl-2-aminobenzoyl-CoA and the subsequent reduction to the dearomatized product 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA. The two reactions occur in separate domains, termed the monooxygenase and reductase domain. Binding studies with 2-aminobenzoyl-CoA and p-hydroxybenzaldehyde as probes for the monooxygenase and reductase domain, respectively, indicate that two functionally distinct and independent active sites exist
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-
?
maleimide + NAD(P)H
succinimide + NAD(P)+
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-
-
-
?
maleimide + NAD(P)H
succinimide + NAD(P)+
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-
-
-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
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-
-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
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-
-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
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-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
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-
-
-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
-
-
-
?
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
-
-
-
-
?
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2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
-
the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
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product formed under physiological NADH concentration
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
pathway of aerobic breakdown of 2-aminobenzoate
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-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
-
pathway of aerobic breakdown of 2-aminobenzoate
-
-
?
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FMN
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the reductase domain utilizes FMN for the reduction of the intermediate 5-hydroxyl-2-aminobenzoyl-CoA
FAD
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approximately 2 mol noncovalently bound FAD per mol of enzyme; flavoprotein
FAD
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the three dimeric forms alphaalpha, alpha'alpha' and alphaalpha' differ in their mode of binding FAD
FAD
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the monooxygenase domain contains FAD
NADPH
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enzyme is less active with NADPH than with NADH
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2-aminobenzoyl-CoA
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substrate inhibition above 0.15 mM
4-hydroxymercuribenzoate
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at least 90% inhibition at 0.2 mM
5,5'-dithiobis(2-nitrobenzoate)
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at least 90% inhibition at 0.2 mM
AgNO3
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at least 90% inhibition at 0.01 mM
HgSO4
-
at least 90% inhibition at 0.1 mM
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0.02 - 0.025
2-aminobenzoyl-CoA
0.25 - 0.47
N-ethylmaleimide
0.02
2-aminobenzoyl-CoA
-
value below, cell extract
0.025
2-aminobenzoyl-CoA
-
value below
0.25
N-ethylmaleimide
-
-
0.47
N-ethylmaleimide
-
-
0.026
NADH
-
-
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70.8
2-aminobenzoyl-CoA
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-
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additional information
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specific activity of isolated and reconstituted enzyme in different fractions after purification
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8
-
2-aminobenzoyl-CoA + NADH
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-
-
brenda
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-
-
brenda
and strain K 740
-
-
brenda
-
-
-
brenda
-
-
-
brenda
and strain K 740
-
-
brenda
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metabolism
-
the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
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C1ACU1_GEMAT
Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505)
787
0
88212
TrEMBL
A0A0H4L4E7_9RHOB
764
0
85128
TrEMBL
E3HWN3_ACHXA
Achromobacter xylosoxidans (strain A8)
783
0
86951
TrEMBL
A0A2H1KWT2_9MICO
797
0
87562
TrEMBL
A0A0N8K607_9RHOB
766
0
86209
TrEMBL
A9DF02_HOEPD
Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43)
764
0
85799
TrEMBL
A0A3B0RNQ3_9ZZZZ
767
0
86074
TrEMBL
Q2KUR1_BORA1
Bordetella avium (strain 197N)
781
0
86786
TrEMBL
A0A1A0DBT6_ACEPA
363
0
39637
TrEMBL
A0A017HT97_9RHOB
258
0
29346
TrEMBL
V9WCS4_9RHOB
764
0
85023
TrEMBL
A0A0S4P6W0_9BURK
790
0
87336
TrEMBL
Q93FB8_AZOEV
773
0
87096
TrEMBL
A0A017HRM9_9RHOB
96
0
10936
TrEMBL
A0A291QH52_9ACTN
777
0
84696
TrEMBL
A0A0P8BPZ1_9RHIZ
790
1
88757
TrEMBL
A0A017HDZ1_9RHOB
764
0
84903
TrEMBL
A0A1Y0XV34_ACEPA
363
0
39645
TrEMBL
Q93FC6_AZOEV
773
0
86889
TrEMBL
A0A0K8P2L4_IDESA
Ideonella sakaiensis (strain 201-F6)
779
0
86785
TrEMBL
A0A1Q8LQI2_9PSEU
411
0
45229
TrEMBL
Q0K8X1_CUPNH
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
784
0
87253
TrEMBL
A0A0K3BHS5_9PSEU
773
0
85089
TrEMBL
A0A1Q8JI43_9PSEU
516
0
56849
TrEMBL
A0A1Y0UUA8_9PROT
363
0
39576
TrEMBL
G0F164_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1)
784
0
87135
TrEMBL
A0A1R3US12_9ACTN
807
0
88609
TrEMBL
A0A0T5ZU69_9BACT
515
0
58213
TrEMBL
A0A1E1V9L3_9BRAD
774
0
86486
TrEMBL
A0A3B0SE29_9ZZZZ
787
0
88248
TrEMBL
A0A1Q8L4A0_9PSEU
733
0
81078
TrEMBL
A0A292YVQ9_9PSEU
520
0
56259
TrEMBL
Q5LKH4_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
764
0
85484
TrEMBL
D5RRD9_9PROT
768
0
84721
TrEMBL
A0A0J5QGA3_9RHOB
762
0
84579
TrEMBL
A0A160TSB7_9ZZZZ
775
0
86825
TrEMBL
A0A160TPP9_9ZZZZ
760
0
83620
TrEMBL
F5SFH4_9BACL
340
0
37431
TrEMBL
B8KT99_9GAMM
302
0
34298
TrEMBL
A0A017HRI2_9RHOB
291
0
31884
TrEMBL
A0A024KAH1_9RHIZ
781
0
88204
TrEMBL
A0A1Q8LV31_9PSEU
733
0
81052
TrEMBL
A0A0J9E6F5_9RHOB
767
0
85580
TrEMBL
A1K6U6_AZOSB
Azoarcus sp. (strain BH72)
771
0
86905
TrEMBL
A0A109YL79_9SPHN
766
0
86046
TrEMBL
A0A0H5CJR1_9PSEU
690
0
74283
TrEMBL
A0A1Q8KZE8_9PSEU
411
0
45229
TrEMBL
A0A292YMH8_9PSEU
743
0
78878
TrEMBL
U2ERC6_9GAMM
434
0
47607
TrEMBL
A0A1Q8KPB6_9PSEU
433
0
47613
TrEMBL
B8KTA0_9GAMM
439
0
49081
TrEMBL
A0A1E3L0R3_9BACL
374
0
41683
TrEMBL
A9I1N7_BORPD
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
786
0
87074
TrEMBL
A0A1K0INU0_CUPNE
784
0
87252
TrEMBL
A0A3B0SHE6_9ZZZZ
445
0
50789
TrEMBL
A0A0B8N7Y8_9NOCA
554
0
60275
TrEMBL
A0A157QGC3_9BORD
783
0
86675
TrEMBL
Q5P5U0_AROAE
Aromatoleum aromaticum (strain EbN1)
771
0
86775
TrEMBL
A0A3B0S3B6_9ZZZZ
770
0
86569
TrEMBL
A0A0P7ZY36_9RHOB
762
0
86137
TrEMBL
A0A2R4BQF3_THAAR
772
0
85916
TrEMBL
E3HTY3_ACHXA
Achromobacter xylosoxidans (strain A8)
370
0
39983
TrEMBL
A0A1Y1IW13_COMTE
589
6
62707
TrEMBL
Q1LL95_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
791
0
87373
TrEMBL
A0A0F7PG56_9RHIZ
764
0
85847
TrEMBL
A0A1R4EV20_9ACTO
797
0
87464
TrEMBL
A0A1V1PN58_9PROT
760
0
84361
TrEMBL
J7M0H1_9MICC
796
0
87515
TrEMBL
A0A0P7Y6N5_9RHOB
762
0
85962
TrEMBL
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87000
-
calculated from deduced amino acid sequence
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homodimer
-
it is proposed that the monooxygenase and reductase domain of opposite peptide chains are involved in the transformation of anthranoyl-CoA to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA
dimer
-
2 * 85000 SDS-PAGE, probably alpha2 dimer, may exist in three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha', where alpha' may be a subunit with a different conformation
dimer
-
three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
dimer
-
2 * 85000 SDS-PAGE, probably alpha2 dimer, may exist in three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha', where alpha' may be a subunit with a different conformation; alpha2 homodimer; three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
-
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0
-
50% loss of activity in 2 days when stored highly concentrated, in dilute solutions it loses 50% of activity in 2 min, NADH, FAD and 2-aminobenzoyl CoA enhance stability
25
-
50% loss of activity in 2 days when stored highly concentrated
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-196°C stable for at least 6 months
-
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-
-
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enzyme is a fusion protein of a monooxygenase and a reductase, plasmid also encodes enzymes of beta-oxidation
-
expression in Escherichia coli BL21
-
plasmid encodes 2 enzymes: 2-aminobenzoate CoA ligase and 2-aminobenzoyl CoA monooxygenase/reductase
-
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Buder, R.; Fuchs, G.
2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Purification and some properties of the enzyme
Eur. J. Biochem.
185
629-635
1989
Pseudomonas sp., Pseudomonas sp. KB740
brenda
Buder, R.; Ziegler, K.; Fuchs, G.; Langkau, B.; Ghisla, S.
2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Studies on the stoichiometry and the course of the reaction
Eur. J. Biochem.
185
637-643
1989
Pseudomonas sp., Pseudomonas sp. KB740
brenda
Langkau, B.; Ghisla, S.; Buder, R.; Ziegler, K.; Fuchs, G.
2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme. Identification of the reaction products
Eur. J. Biochem.
191
365-371
1990
Pseudomonas sp.
brenda
Altenschmidt, U.; Eckerskorn, C.; Fuchs, G.
Evidence that enzymes of a novel aerobic 2-amino-benzoate metabolism in denitrifying Pseudomonas are coded on a small plasmid
Eur. J. Biochem.
194
647-653
1990
Pseudomonas sp., Pseudomonas sp. KB740
brenda
Schuhle, K.; Jahn, M.; Ghisla, S.; Fuchs, G.
Two similar gene clusters coding for enzymes of a new type of aerobic 2-aminobenzoate (anthranilate) metabolism in the bacterium Azoarcus evansii
J. Bacteriol.
183
5268-5278
2001
Azoarcus evansii, Azoarcus evansii KB740
brenda
Torres, R.A.; Bruice, T.C.
Theoretical investigation of the [1,2]-sigmatropic hydrogen migration in the mechanism of oxidation of 2-aminobenzoyl-CoA by 2-aminobenzoyl-CoA monooxygenase/reductase
Proc. Natl. Acad. Sci. USA
96
14748-14752
1999
Azoarcus evansii
brenda
Langkau, B.; Vock, P.; Massey, V.; Fuchs, G.; Ghisla, S.
2-Aminobenzoyl-CoA monooxygenase/reductase. Evidence for two distinct loci catalyzing substrate monooxygenation and hydrogenation
Eur. J. Biochem.
230
676-685
1995
Pseudomonas sp., Pseudomonas sp. KB740
brenda
Lochmeyer, C.; Koch, J.; Fuchs, G.
Anaerobic degradation of 2-aminobenzoic acid (anthranilic acid) via benzoyl-coenzyme A (CoA) and cyclohex-1-enecarboxyl-CoA in a denitrifying bacterium
J. Bacteriol.
174
3621-3628
1992
Pseudomonas sp., Pseudomonas sp. K172
brenda
Bergner, T.; Pavkov-Keller, T.; Kreuzer, K.; Kowaliuk, J.; Plank, M.; Runggatscher, K.; Turrini, N.G.; Zucol, B.; Wallner, S.; Faber, K.; Gruber, K.; Macheroux, P.
Anthranoyl-CoA monooxygenase/reductase from Azoarcus evansii possesses both FMN and FAD in two distinct and independent active sites
Biochim. Biophys. Acta
1854
890-896
2015
Azoarcus evansii
brenda
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1.14.13.40 anthraniloyl-CoA monooxygenase
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