HOME
login
history
all enzymes
BRENDA home
History
Information on EC 1.14.13.40 - anthraniloyl-CoA monooxygenase
for references in articles please use BRENDA:EC1.14.13.40Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Word Map
- 1.14.13.40
-
flavoenzyme
-
denitrifying
- flavoproteins
- thioesters
-
azoarcus
- 2-aminobenzoate
-
monooxygenation
- evansii
- ligase
-
non-aromatic
-
dearomatized
- flavin
- yellow
-
fuchs
-
alicyclic
- n-ethylmaleimide
- borohydride
- salicylate
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
2
+
=
+
+
2
Synonyms
2-aminobenzoyl-coa monooxygenase/reductase, anthranoyl-coa monooxygenase/reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
112692-57-6
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
the reductase domain utilizes FMN for the reduction of the intermediate 5-hydroxyl-2-aminobenzoyl-CoA
FAD
-
approximately 2 mol noncovalently bound FAD per mol of enzyme; flavoprotein
FAD
-
the three dimeric forms alphaalpha, alpha'alpha' and alphaalpha' differ in their mode of binding FAD
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
specific activity of isolated and reconstituted enzyme in different fractions after purification
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme participates in a pathway for the degradation of aromatic compounds in Azoarcus evansii
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A9I1N7_BORPD
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
786
0
87074
TrEMBL
A0A017HRM9_9RHOB
96
0
10936
TrEMBL
A0A0N8K607_9RHOB
766
0
86209
TrEMBL
A0A0J9E6F5_9RHOB
767
0
85580
TrEMBL
A0A017HT97_9RHOB
258
0
29346
TrEMBL
A0A0P0RGQ6_9BURK
790
0
88391
TrEMBL
A0A017HDZ1_9RHOB
764
0
84903
TrEMBL
A0A1Y0XV34_ACEPA
363
0
39645
TrEMBL
A0A0P7ZY36_9RHOB
762
0
86137
TrEMBL
G0F164_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / N-1)
784
0
87135
TrEMBL
A0A0K8P2L4_IDESA
Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6)
779
0
86785
TrEMBL
A9DF02_HOEPD
Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43)
764
0
85799
TrEMBL
A0A0P8BPZ1_9RHIZ
790
1
88757
TrEMBL
A0A0P7Y6N5_9RHOB
762
0
85962
TrEMBL
A0A5E8GUW2_LABAD
Labrenzia alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11)
773
0
86177
TrEMBL
Q5LKH4_RUEPO
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
764
0
85484
TrEMBL
C1ACU1_GEMAT
Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505)
787
0
88212
TrEMBL
Q0K8X1_CUPNH
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
784
0
87253
TrEMBL
A0A017HRI2_9RHOB
291
0
31884
TrEMBL
A0A0T5ZU69_9BACT
515
0
58213
TrEMBL
Q1LL95_CUPMC
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
791
0
87373
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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; alpha2 homodimer; three dimeric forms: 1. alpha,alpha, 2. alpha',alpha', 3. alpha,alpha'
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.13.40)
Transporter Classification Database (TCDB):
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
