Information on EC 6.2.1.32 - anthranilate-CoA ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.32
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RECOMMENDED NAME
GeneOntology No.
anthranilate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + anthranilate + CoA = AMP + diphosphate + anthraniloyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis
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4-hydroxy-2(1H)-quinolone biosynthesis
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Acridone alkaloid biosynthesis
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Aminobenzoate degradation
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anthranilate degradation II (aerobic)
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anthranilate degradation III (anaerobic)
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aurachin A, B, C and D biosynthesis
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aurachin RE biosynthesis
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Phenazine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
anthranilate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
112692-58-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KB740
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Manually annotated by BRENDA team
strain KB740
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Manually annotated by BRENDA team
strain PAO1, gene pqsA
UniProt
Manually annotated by BRENDA team
strain KB740
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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
ATP + 2-fluorobenzoate + CoA
AMP + 2-fluorobenzoyl-CoA + diphosphate
show the reaction diagram
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at the same reaction rate as 2-aminobenzoate
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-
?
ATP + 2-methylbenzoate + CoA
AMP + 2-methylbenzoyl-CoA + diphosphate
show the reaction diagram
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at less than 1/5 of the rate as 2-aminobenzoate
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-
?
ATP + 3-fluorobenzoate + CoA
AMP + 3-fluorobenzoyl-CoA + diphosphate
show the reaction diagram
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at half the reaction rate as 2-aminobenzoate
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?
ATP + 4-fluorobenzoate + CoA
AMP + 4-fluorobenzoyl-CoA + diphosphate
show the reaction diagram
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at the same reaction rate as 2-aminobenzoate
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?
ATP + anthranilate + CoA
AMP + diphosphate + anthranilyl-CoA
show the reaction diagram
ATP + benzoate + CoA
AMP + benzoyl-CoA + diphosphate
show the reaction diagram
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at the same reaction rate as 2-aminobenzoate
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-
?
ATP + CoA + anthranilate
AMP + diphosphate + anthranilyl-CoA
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
ATP + anthranilate + CoA
AMP + diphosphate + anthranilyl-CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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required, can replace Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-3-chlorobenzoate
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2-hydroxybenzoate salicylate
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3-fluoro-O-anisidine
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5,5'-dithiobis(2-nitrobenzoate)
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E2, no effect on isoenzyme E3
5-nitroanthranilonitrile
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anthranilonitrile
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Cu2+
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methylanthranilate
i.e. 2-aminobenzoate methyl ester
n-octylglucoside
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PCMB
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isoenzyme E3, no effect on E2
Tween 100
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Zn2+
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.02
2-Aminobenzoate
0.05 - 0.07
2-Fluorobenzoate
0.04 - 0.083
ATP
0.035 - 0.075
Benzoate
0.02 - 0.026
CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.7 - 267
2-Aminobenzoate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0129
2-amino-3-chlorobenzoate
pH 8.0, 37C
0.0183
2-hydroxybenzoate salicylate
pH 8.0, 37C
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0.0897
3-fluoro-O-anisidine
pH 8.0, 37C
0.037
5-nitroanthranilonitrile
pH 8.0, 37C
1.3
anthranilonitrile
pH 8.0, 37C
5.8
methylanthranilate
pH 8.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
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isoenzyme E3
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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isoenzyme E2, gel filtration
65000
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isoenzyme E3, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzymes not sensitive to oxygen
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713
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 0.05 mg/ml protein concentration, Tris-HCl buffer, pH 7.8, 50% loss of activity after 4 days
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frozen in liquid nitrogen for 3 months without remarkable loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PqsA 58fold from Escherichia coli by ammonium sulfate fractionation, metal affinity and hydrophobic interaction chromatography, and anion exchange chromatography
strain KB740, 2 forms, E2: MW 60000, induced anaerobically by 2-aminobenzoate and E3: MW 65000, induced aerobically by 2-aminobenzoate
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene pqsA is part of the pqsABCDE operon, sequence comparisons, expression of the His-tagged enzyme in Escherichia coli