Ligand anthranilate

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of anthranilate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C7H7NO2
anthranilate
RWZYAGGXGHYGMB-UHFFFAOYSA-N
Synonyms:
2-amino benzoate, 2-Aminobenzoate, 2-aminobenzoic acid, 2-Carboxy-1-phenylamine, anthranilic acid, o-aminobenzoate, o-aminobenzoic acid
Pathway Source
Pathways


Show all pahtways known for Show all BRENDA pathways known for anthranilate

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (18 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
anthranilate + NADPH + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = ?
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate
-
show the reaction diagram
acetyl-CoA + o-aminobenzoic acid = CoA + N-acetyl-o-aminobenzoic acid
-

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
2,3-dihydroxyindole + O2 = anthranilate + CO2
-
-
show the reaction diagram
2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H+ = anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD+
-
-
show the reaction diagram
2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA
-
show the reaction diagram
N-formylanthranilic acid + H2O = formate + anthranilic acid
-
-
show the reaction diagram
2-aminobenzonitrile + 2 H2O = 2-aminobenzoic acid + NH3
-

Substrate in Enzyme-catalyzed Reactions (66 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
anthranilate + NADH + 2 H+ + O2 = 2-aminophenol + NAD+ + H2O + CO2
-
show the reaction diagram
anthranilate + NADH + H+ + O2 = 5-hydroxyanthranilate + NAD+ + H2O
-
show the reaction diagram
anthranilate + NAD(P)H + O2 = 2-hydroxyaniline + NAD(P)+ + H2O2 + CO2
-
show the reaction diagram
anthranilate + NADPH + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3
-
show the reaction diagram
anthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilate + FAD + 2 H2O
-
show the reaction diagram
anthranilate + FADH2 + chloride + O2 + H+ = 5-chloro-anthranilate + FAD + 2 H2O
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate
-
show the reaction diagram
S-adenosyl-L-methionine + anthranilate = methyl anthranilate + S-adenosyl-L-homocysteine
-
show the reaction diagram
malonyl-CoA + anthranilate = CoA + N-malonylanthranilate
-
show the reaction diagram
acetyl-CoA + o-aminobenzoic acid = CoA + N-acetyl-o-aminobenzoic acid
-
show the reaction diagram
UDP-alpha-D-glucose + anthranilic acid = UDP + 1-O-anthraniloyl-beta-D-glucose
-
show the reaction diagram
2-aminobenzoate + UDPglucuronate = UDP + ?
-
show the reaction diagram
anthranilic acid + UDP-glucose = ?
-
show the reaction diagram
thiamine + o-aminobenzoic acid = 4-methyl-5-(2-hydroxyethyl)-thiazole + 2-[[(4-amino-2-methylpyrimidin-5-yl)methyl]amino]benzoic acid
-
show the reaction diagram
ATP + anthranilate = diphosphate + anthranylyl-adenylate
-
show the reaction diagram
ATP + anthranilate = ?
-
show the reaction diagram
2-Aminobenzoate = Aniline + CO2
-
show the reaction diagram
ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA
-
show the reaction diagram
ATP + 2-aminobenzoate + CoA = AMP + diphosphate + 2-aminobenzoyl-CoA
-

Product in Enzyme-catalyzed Reactions (45 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
2,3-dihydroxyindole + O2 = anthranilate + CO2
-
show the reaction diagram
methyl 2-aminobenzoate + H2O = methanol + 2-aminobenzoate
-
-
show the reaction diagram
2-aminobenzoyl-CoA + H2O = 2-aminobenzoate + CoA
-
-
show the reaction diagram
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O = anthranilate + 2-hydroxypenta-2,4-dienoate
-
-
show the reaction diagram
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O = 2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid
-

Activator in Enzyme-catalyzed Reactions (1 result)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
induces, the enzyme activity increases with an increase in the concentration of anthranilate in the growth medium, optimal amounts of the enzyme are synthesized when the concentration of anthranilate is 1 mg/ml, further increase in the concentration results in a considerable decrease in the growth of the organism as well in the enzyme activity
-

Inhibitor in Enzyme-catalyzed Reactions (59 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
competitive
-
competitive inhibition
-
22% inhibition at 2 mM and 11% inhibition at 0.2 mM
-
competitive inhibitor with benzoic acid as a substrate
-
LAO inhibitor, slightly inhibiting the degradation of fibrinogen
three and two binding sites in isoforms L1 and L2, respectively
competitive
about 35% inhibition at 0.2 mM
83.3% residual activity at 10 mM
75% activity left at 1.1 mM
-
weak
-
substrate inhibition above 0.008 mM
substrate inhibition
substrate inhibition above 0.008 mM
substrate inhibition. Concentrations above 0.004 mM result in reduced enzymatic activity
weak inhibition
-
Ki: 1.6 mM
-
9% inhibition at 0.5-1 mM
-
45% inhibition at 0.5 mM
-
29% inhibition at 1-2 mM
-
1 mM
-
competitive
-
i.e. ortho-aminobenzoate
-
competitive
-

3D Structure of Enzyme-Ligand-Complex (PDB) (94 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (46 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
25°C, pH not specified in the publication, isoenzyme AAMT1
0.45
-
25°C, pH not specified in the publication, isoenzyme AAMT2
0.37
-
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
3.5
-
at 60°C
0.105
-
at 87°C
0.4
-
cosubstrate: 5-phospho-alpha-D-ribose 1-diphosphate
I36E/M47D double mutant, kcat/KM: 4.8 1/s*microM
-999
-
mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
2
-
mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
4.4
-
mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
13.3
-
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
3.4
-
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
2.7
-
at 50°C
0.067
-
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
3.9
-
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
0.78
-
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
1.3
-
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.046
-
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
1.2
-
mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
1.2
-
wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.33
-
wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.24
-
wild-type, kcat/KM: 4.8 1/s*microM
-999
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A
2
-
+/-0.04, wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration
0.41
-
+/-0.06, I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
0.28
-
25°C
0.014
-
40°C
0.035
-
50°C
0.067
-
60°C
0.105
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
5.1
-
-
4.4
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
0.62
-
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
4.2
-
60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A
0.73
-
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.48
-
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
1.1
-
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N
6
-
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q
5.6
-
87°C
0.4
-
at 25°C
0.014
-
at 40°C
0.035
-
pH 8.0, 31°C, recombinant wild-type enzyme
3.9
-
28°C, isoenzyme E3
21.7
-
28°C, isoenzyme E2
267
-

KM Value (59 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
0.12
-
30°C, pH 7.0
0.028
-
N298E mutant
0.024
-
wild-type
0.007
-
25°C, pH not specified in the publication, isoenzyme AAMT2
0.311
-
25°C, pH not specified in the publication, isoenzyme AAMT1
0.641
-
pH 7, temperature not specified in the publication
3.4
-
-
13
-
pH 8.0, 21°C
2.74
-
mutant enzyme I36E/M47D/D83G/N109S/F149S, pH 7.2, 37°C
0.06
-
I36E/M47D double mutant, pH 7.2, 37°C, 0.01 microM subunit concentration
0.000058
-
mutant D83G, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.00012
-
mutant D83G/F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.0036
-
mutant D83G/F149S, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.0031
-
mutant enzyme I36E/M47D/D83G/F149S, pH 7.2, 37°C
0.011
-
mutant enzyme I36E/M47D/D83G/F149S/F193S, pH 7.2, 37°C
0.029
-
mutant enzyme I36E/M47D/D83G/F149S/I169T, pH 7.2, 37°C
0.007
-
mutant enzyme I36E/M47D/D83G/F149S/L320M, pH 7.2, 37°C
0.008
-
TAX6trpR782
0.003
-
mutant enzyme I36E/M47D/T77I/D83G/F149S, pH 7.2, 37°C
0.037
-
mutant enzyme I36E/M47D/T77I/D83G/F149S/I169T/F193S/L320M, pH 7.2, 37°C
0.082
-
mutant enzyme I36E/M47D/T77I/D83G/F149S/N109S/I169T/F193S/L320M, pH 7.2, 37°C
0.051
-
mutant F149S, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.0012
-
wild-type, in the presence of 2 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.00002
-
wild-type, in the presence of 0.05 mM MgCl2, 50 mM Tris-HCl, pH 7.2, at 37°C
0.000018
-
wild-type, pH 7.2, 37°C, 0.01 microM subunit concentration
0.000085
-
trpAB1653trpR782
0.004
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme R164A
0.297
-
25°C
0.002
-
40°C
0.0026
-
50°C
0.0032
-
60°C
0.0035
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A
0.00053
-
60°C, pH 7.5, 0.05 mM Mg2+, mutant enzyme H107A/P178A
0.0125
-
at pH 8.5 and 55°C
0.0022
-
60°C, pH 7.5, 0.05 mM Mg2+, wild-type enzyme
0.00004
-
60°C, pH 7.5, 0.05 mM Mg2+,mutant enzyme R164A/H154A
0.149
-
60°C, pH 7.5, 2 mM Mg2+, mutant enzyme K106Q
0.00075
-
60°C, pH 7.5, 2 mM Mg2+, wild-type enzyme
0.00007
-
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme D223N
0.00016
-
60°C, pH 7.5, 2 mM Mg2+,mutant enzyme E224Q
0.00091
-
87°C
0.005
-
at 87°C, Km decreases at lower temperatures
0.000005
-
-
37
-
37°C
0.15
-
pH 8.0, 31°C, recombinant wild-type enzyme
0.021
-
in Tris-HCl at pH 8.0
0.25
-
isoenzyme E3
0.015
-
isoenzyme E2

Ki Value (10 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
for the pI 4.98 enzyme
for the pI 5.6 enzyme
6.5
-
20 mM Tris-HCl, pH 8.0, 25°C
0.87
-
isoform L2, enzyme-substrate complex
0.02544
-
isoform L2, free enzyme
0.01189
-
in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C
1.6
-
-
0.03
-

References & Links

Links to other databases for anthranilate

ChEBI
PubChem
-
PubChem