Information on EC 1.14.13.40 - anthraniloyl-CoA monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.40
-
RECOMMENDED NAME
GeneOntology No.
anthraniloyl-CoA monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthraniloyl-CoA + 2 NAD(P)H + 2 H+ + O2 = 2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + 2 NAD(P)+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anthranilate degradation II (aerobic)
-
-
Aminobenzoate degradation
-
-
Microbial metabolism in diverse environments
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
112692-57-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KB740
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-
Manually annotated by BRENDA team
strain K172 and K 740
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
show the reaction diagram
2-hydroxybenzoyl-CoA + NAD(P)H + O2
?
show the reaction diagram
maleimide + NAD(P)H
succinimide + NAD(P)+
show the reaction diagram
N-ethylmaleimide + NAD(P)H
N-ethylsuccinimide + NAD(P)+
show the reaction diagram
N-ethylmaleimide + NAD(P)H
succinimide + NAD(P)+
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-CoA + NAD(P)H + O2
2-amino-5-oxocyclohex-1-enecarboxyl-CoA + H2O + NAD(P)+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
requirement
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-aminobenzoyl-CoA
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substrate inhibition above 0.15 mM
4-hydroxymercuribenzoate
-
at least 90% inhibition at 0.2 mM
5,5'-dithiobis(2-nitrobenzoate)
-
at least 90% inhibition at 0.2 mM
AgNO3
-
at least 90% inhibition at 0.01 mM
HgSO4
-
at least 90% inhibition at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.025
2-aminobenzoyl-CoA
0.25 - 0.47
N-ethylmaleimide
0.026 - 0.042
NADH
0.5
NADPH
-
-
0.005
O2
-
value below
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70.8
2-aminobenzoyl-CoA
Pseudomonas sp.
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.015
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cell extract
additional information
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specific activity of isolated and reconstituted enzyme in different fractions after purification
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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2-aminobenzoyl-CoA + NADH
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
-
SDS-PAGE
87000
-
calculated from deduced amino acid sequence
170000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
25
-
50% loss of activity in 2 days when stored highly concentrated
40
-
unstable above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C stable
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-196°C stable for at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apparent homogeneity
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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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