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Information on EC 1.14.13.40 - anthraniloyl-CoA monooxygenase
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EC Tree
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
-
azoarcus
- thioesters
-
monooxygenation
-
non-aromatic
- flavin
-
dearomatized
- n-ethylmaleimide
- yellow
-
alicyclic
- salicylate
- borohydride
-
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
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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
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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)+
-
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
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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
-
the reductase domain utilizes FMN for the reduction of the intermediate 5-hydroxyl-2-aminobenzoyl-CoA
FAD
-
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
-
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
-
the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). C1ACU1_GEMAT
Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505)
787
0
88212
TrEMBL
-
A0A6J4XCP2_9DELT
769
0
86245
TrEMBL
-
A9DF02_HOEPD
Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43)
764
0
85799
TrEMBL
-
A0A160TSB7_9ZZZZ
775
0
86825
TrEMBL
other Location (Reliability: 5)
A0A3B0SE29_9ZZZZ
787
0
88248
TrEMBL
other Location (Reliability: 2)
A0A6J4NL45_9RHOB
uncultured Rubellimicrobium sp
761
0
86474
TrEMBL
-
E3HTY3_ACHXA
Achromobacter xylosoxidans (strain A8)
370
0
39983
TrEMBL
-
A0A0P8BPZ1_9RHIZ
790
1
88757
TrEMBL
-
A0A0J9E6F5_9RHOB
767
0
85580
TrEMBL
-
A0A6J4M433_9BACT
772
1
85566
TrEMBL
-
A0A6J4I540_9PROT
285
0
30452
TrEMBL
-
A0A5E8GUW2_LABAD
Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11)
773
0
86177
TrEMBL
-
A0A0K8P2L4_IDESA
Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6)
779
0
86785
TrEMBL
-
A0A1Y0XV34_ACEPA
363
0
39645
TrEMBL
-
A0A6J4S9W4_9SPHN
91
0
10015
TrEMBL
-
A0A0J5QGA3_9RHOB
762
0
84579
TrEMBL
-
G0F164_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
784
0
87135
TrEMBL
-
A0A6J4XQI3_9DELT
769
0
86101
TrEMBL
-
A0A0T5ZU69_9BACT
515
0
58213
TrEMBL
-
A0A017HT97_9RHOB
258
0
29346
TrEMBL
-
A9I1N7_BORPD
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
786
0
87074
TrEMBL
-
A0A017HRM9_9RHOB
96
0
10936
TrEMBL
-
A0A6J4PKM9_9ACTN
764
0
86331
TrEMBL
-
Q5LKH4_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
764
0
85484
TrEMBL
-
A0A0P7Y6N5_9RHOB
762
0
85962
TrEMBL
-
A0A0N8K607_9RHOB
766
0
86209
TrEMBL
-
A0A6J4IWT7_9PROT
778
0
85956
TrEMBL
-
A0A0K3BHS5_9PSEU
773
0
85089
TrEMBL
-
A0A017HDZ1_9RHOB
764
0
84903
TrEMBL
-
A0A160TPP9_9ZZZZ
760
0
83620
TrEMBL
other Location (Reliability: 4)
Q0K8X1_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
784
0
87253
TrEMBL
-
A0A3B0S3B6_9ZZZZ
770
0
86569
TrEMBL
other Location (Reliability: 2)
Q1LL95_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
791
0
87373
TrEMBL
-
A0A017HRI2_9RHOB
291
0
31884
TrEMBL
-
A0A0P0RGQ6_9BURK
790
0
88391
TrEMBL
-
A0A1B2GPB0_STRNR
810
0
88123
TrEMBL
-
A0A3B0SHE6_9ZZZZ
445
0
50789
TrEMBL
other Location (Reliability: 3)
E3HWN3_ACHXA
Achromobacter xylosoxidans (strain A8)
783
0
86951
TrEMBL
-
A0A3B0RNQ3_9ZZZZ
767
0
86074
TrEMBL
other Location (Reliability: 3)
A0A0P7ZY36_9RHOB
762
0
86137
TrEMBL
-
A0A1R4EV20_9ACTO
797
0
87464
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
-
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
-
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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