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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
forming of carbon sulfur bonds
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-
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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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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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Phenazine biosynthesis
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Aminobenzoate degradation
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Acridone alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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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
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Manually annotated by BRENDA team
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
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 + anthraniloyl-CoA
show the reaction diagram
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
additional information
?
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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 + anthraniloyl-CoA
show the reaction diagram
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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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, 37°C
0.0897
3-fluoro-O-anisidine
pH 8.0, 37°C
0.037
5-nitroanthranilonitrile
pH 8.0, 37°C
1.3
anthranilonitrile
pH 8.0, 37°C
5.8
methylanthranilate
pH 8.0, 37°C
0.0183
salicylate
pH 8.0, 37°C
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
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
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified isolated N-terminal domain of anthranilate-CoA ligase PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP, sitting drop vapor diffusion technique, mixing of 200 nl of protein solution with 200 nl of reservoir solution containing 0.1 M Na3 citrate, pH 5.8-6.3, 22-28% w/v PEG 3350, and 0.2-0.5 M NH4OAc. Crystals can only be obtained in the presence of substrates, leading to complexes with anthraniloyl-AMP or 6-fluoroanthraniloyl-AMP, 20°C, X-ray diffraction structure determination and analysis at 1.43-1.90 A resolution, molecular replacement using the structure of the benzoate-CoA ligase from Bacillus xenoverans LB400, PDB ID 2V7B, as a search model, modeling
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzymes not sensitive to oxygen
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713
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development