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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)+
anthraniloyl-CoA + NADH + H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+
maleimide + NAD(P)H
succinimide + NAD(P)+
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + 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)+
-
-
-
-
?
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)+
-
-
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)+
-
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
-
-
?
anthraniloyl-CoA + NADH + H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+
-
-
-
-
r
anthraniloyl-CoA + NADH + H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+
-
-
-
-
r
maleimide + NAD(P)H
succinimide + NAD(P)+
-
-
-
-
?
maleimide + NAD(P)H
succinimide + NAD(P)+
-
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
-
?
N-ethylmaleimide + NAD(P)H + H+
N-ethylsuccinimide + NAD(P)+
-
-
-
?
N-ethylmaleimide + NAD(P)H + 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)+
-
-
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
-
-
?
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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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
-
dimer
-
alpha2 homodimer
-
dimer
-
three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
-
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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
Aromatoleum evansii, Aromatoleum 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
Aromatoleum 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
Aromatoleum evansii
brenda
1.14.13.40 anthraniloyl-CoA monooxygenase
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