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Information on EC 1.14.13.40 - anthraniloyl-CoA monooxygenase
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1.14.13.40 anthraniloyl-CoA monooxygenaseIUBMB Comments
A flavoprotein (FAD). The non-aromatic product is unstable and releases CO2 and NH3, forming 1,4-cyclohexanedione.
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Word Map
- 1.14.13.40
- flavoproteins
-
flavoenzyme
-
denitrifying
- 2-aminobenzoate
- evansii
- thioesters
-
azoarcus
-
monooxygenation
-
dearomatized
- flavin
-
non-aromatic
-
alicyclic
- yellow
- borohydride
- n-ethylmaleimide
- salicylate
-
fuchs
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
2
+
=
+
+
2
Synonyms
2-aminobenzoyl-CoA monooxygenase/reductase, ACMR, anthranoyl-CoA monooxygenase/reductase, reductase, anthraniloyl coenzyme A, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-aminobenzoyl-CoA monooxygenase/reductase
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-
-
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reductase, anthraniloyl coenzyme A
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
reaction mechanism
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anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
112692-57-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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)+
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
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reaction mechanism
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-
?
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)+
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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)+
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-
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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-
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)+
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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)+
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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)+
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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)+
-
-
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)+
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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
-
-
?
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
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-
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)+
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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)+
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7 different products are formed, pattern is dependent on pH
?
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
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i.e. salicoyl-CoA, weak substrate, is probably monooxygenated but not hydrogenated
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?
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
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i.e. salicoyl-CoA, weak substrate, is probably monooxygenated but not hydrogenated
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?
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 participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
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-
?
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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-
?
anthraniloyl-CoA + NADH + H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+
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r
anthraniloyl-CoA + NADH + H+ + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD+
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r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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the three dimeric forms alphaalpha, alpha'alpha' and alphaalpha' differ in their mode of binding FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
additional information
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specific activity of isolated and reconstituted enzyme in different fractions after purification
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
Show AA Sequence and Transmembrane Helices (236 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
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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
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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
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three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
dimer
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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
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dimer
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three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is a fusion protein of a monooxygenase and a reductase, plasmid also encodes enzymes of beta-oxidation
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plasmid encodes 2 enzymes: 2-aminobenzoate CoA ligase and 2-aminobenzoyl CoA monooxygenase/reductase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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