Information on EC 4.1.3.27 - anthranilate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
4.1.3.27
-
RECOMMENDED NAME
GeneOntology No.
anthranilate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis
-
-
4-hydroxy-2(1H)-quinolone biosynthesis
-
-
acridone alkaloid biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-tryptophan biosynthesis
-
-
Metabolic pathways
-
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
-
tryptophan metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-59-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and 2 classes of mutants: one is defective in the chorismate-binding subunit E and is incapable of catalyzing the anthranilate synthetase reaction. The second class is defective in the G subunit but produces an active E subunit, this mutation results in a requirement for p-aminobenzoate in addition to anthranilate
-
-
Manually annotated by BRENDA team
two isoenzymes: AS-a and AS-b
-
-
Manually annotated by BRENDA team
L. cv. Shokan 1, induction with oligo-N-acetylchitooligosaccharide elicitors
-
-
Manually annotated by BRENDA team
strain Yu62
-
-
Manually annotated by BRENDA team
strain Yu62
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Pepty 695 and strain M5/95F
-
-
Manually annotated by BRENDA team
Claviceps sp.
Claviceps sp. SD58
strain SD58
-
-
Manually annotated by BRENDA team
H 16
-
-
Manually annotated by BRENDA team
H 16
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene trpED
-
-
Manually annotated by BRENDA team
Escherichia coli W3110 trpD9923
W3110 trpD9923
-
-
Manually annotated by BRENDA team
strain Z
-
-
Manually annotated by BRENDA team
strain Z
-
-
Manually annotated by BRENDA team
Hansenula henricii
ASA2 expressed in Astralagus sinicus
-
-
Manually annotated by BRENDA team
Oryza sativa Nipponbare
-
-
-
Manually annotated by BRENDA team
hybrid, clone INRA 7171-B4
-
-
Manually annotated by BRENDA team
strain HY150
-
-
Manually annotated by BRENDA team
strain 3022a
-
-
Manually annotated by BRENDA team
strain 3022a
-
-
Manually annotated by BRENDA team
strain MT4
-
-
Manually annotated by BRENDA team
Q06128: subunit TrpE, Q06129: subunit TrpG
Q06128 and Q06129
UniProt
Manually annotated by BRENDA team
independent expression of subunits in Escherichia coli
UniProt
Manually annotated by BRENDA team
genes trpE, trpGD, and trpG
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
P09785 and P09786, P20580
TrpE and PhnA sequences reveal the evolutionary relationships of each anthranilate synthase enzyme to those of other species, phylogenetic analysis and tree, overview. TrpEG are most closely related to anthranilate synthases from other members of the fluorescent pseudomonad family, while PhnAB are most closely related to anthranilate synthases from more distantly related organisms. The absence of a phnAB-like operon in other pseudomonads is evidence that PhnAB acquisition occurred after the family's diversification; TrpE and PhnA sequences reveal the evolutionary relationships of each anthranilate synthase enzyme to those of other species, phylogenetic analysis and tree, overview. TrpEG are most closely related to anthranilate synthases from other members of the fluorescent pseudomonad family, while PhnAB are most closely related to anthranilate synthases from more distantly related organisms. The absence of a phnAB-like operon in other pseudomonads is evidence that PhnAB acquisition occurred after the family's diversification
malfunction
metabolism
physiological function
additional information
-
the enzyme shows a mechanism of this tight activity regulation, catalytic Cys-His-Glu triad, molecular dynamics simulations, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + ammonia
anthranilate + pyruvate + H2O
show the reaction diagram
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + NH3
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
NH3 + phosphoribosyl diphosphate
phosphoribosyl amine
show the reaction diagram
-
mutant P362L
-
?
additional information
?
-
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
chorismate + ammonia
anthranilate + pyruvate + H2O
show the reaction diagram
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
feedback-insensitive enzyme
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
1 mM, can partially replace Mg2+ in activation
K+
Claviceps sp.
-
stimulates
Na+
Claviceps sp.
-
stimulates
NH4+
Claviceps sp.
-
stimulates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3-[[(5S)-6-([2-[6-(3-amino-3-oxopropyl)dibenzo[b,d]furan-4-yl]ethyl]amino)-5-[[2-(4-nitrophenyl)propanoyl]amino]-6-oxohexyl]carbamoyl]phenoxy)acetic acid
-
-
(4R,5S,6S)-4-amino-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohex-1-enecarboxylate
-
-
(4R,5S,6S)-5-[(1-carboxyethenyl)oxy]-4,6-dihydroxycyclohex-1-enecarboxylate
-
-
(4S,5R,6R)-4-hydroxy-5-[(1-carboxyethenyl)oxy]-6-aminocyclohex-1-enecarboxylic acid
-
-
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
-
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
-
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
2-(1-carboxy-ethylamino)-isonicotinate
-
-
2-(3-(-(S)-5-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-4-(3-hydroxy-4-methyl-2-nitrobenzamido)-5-oxopentylcarbamoyl)-phenoxy)acetic acid
-
-
2-(3-(3-((R)-3-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-2-(3-hydroxy-4-methyl-2-nitrobenzamido)-3-oxopropylthio) propylcarbamoyl)phenoxy)acetic acid
-
-
2-(carboxymethyl-amino)-isonicotinate
-
-
2-oxoglutarate
-
reaction of component I with NH4+ as substrate
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
-
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
-
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
-
4-amino-3-(1-carboxyethoxy)benzoic acid
-
-
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
-
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
-
4-methylindole
-
inhibits at 0.3 mM
5-fluoro-DL-tryptophan
-
strong, 50% inhibition at 0.005 mM
5-methyl-DL-tryptophan
-
strong, 50% inhibition at 0.004 mM
5-Methyltryptophan
6-diazo-5-oxo-L-norleucine
6-fluoro-DL-tryptophan
-
strong, 50% inhibition at 0.009 mM
7-methyl-DL-tryptophan
-
inhibits at 0.3 mM
anthranilate
-
-
Bromopyruvate
-
inactivation prevented by chorismate and Trp
Ca2+
Claviceps sp.
-
-
Co2+
-
10 mM, 67% inhibition of enzyme from cell line R-15, 33% inhibition of enzyme from cell line R-20
Diethylamine
-
reaction of component I with NH4+ as substrate
Dimethylamine
-
reaction of component I with NH4+ as substrate
DL-4-methyltryptophan
-
-
DL-5-fluorotryptophan
DL-5-hydroxytryptophan
-
-
DL-5-Methyltryptophan
DL-6-Fluorotryptophan
-
-
elymoclavine
Claviceps sp.
-
i.e. (6-methyl-8,9-didehydroergolin-8yl)methanol
Fe2+
Claviceps sp.
-
-
Gln
-
reaction of component I with NH4+ as substrate
Glu
-
reaction of component I with NH4+ as substrate
iodoacetamide
L-2-Amino-4-oxo-5-chloropentanoic acid
-
irreversible, Gln protects
L-tryptophan
methylamine
-
reaction of component I with NH4+ as substrate
N-((S)-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxopropan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
-
N-((S)-6-amino-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxohexan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
-
N-Methylhydroxylamine
-
reaction of component I with NH4+ as substrate
N6-[3-(carboxymethoxy)benzoyl]-N2-(2,6-dimethoxybenzoyl)-L-lysyl-3-hydroxy-4-nitro-L-phenylalaninamide
-
-
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-3-chloro-L-phenylalaninamide
-
-
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-4-cyano-L-phenylalaninamide
-
-
NEM
-
reaction of component I with NH4+ as substrate
p-Hydroxybenzaldehyde
-
-
p-hydroxybenzoate
-
-
pyruvate
-
competitive with respect to chorismate, noncompetitive with respect to NH4+, reaction of component I with NH4+ as substrate
trimethylamine
-
reaction of component I with NH4+ as substrate
tryptamine
-
-
vanillate
-
-
[3-([(5S)-5-[[(3-benzoylpyridin-2-yl)carbonyl]amino]-6-[(1-carbamoylcyclohexyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
-
[3-([(5S)-6-[(1-carbamoylcyclohexyl)amino]-5-[(3,5-dihydroxybenzoyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
-
[3-([(5S)-6-[(4-carbamoyl-1,1-dioxidotetrahydro-2H-thiopyran-4-yl)amino]-6-oxo-5-[(4-phenoxybenzoyl)amino]hexyl]carbamoyl)phenoxy]acetic acid
-
-
additional information
-
not inhibitory: D-tryptophan
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chanoclavine
Claviceps sp.
-
slight activation in presence of His
elymoclavine
Claviceps sp.
-
slight activation in presence of His
indoleacrylic acid
Claviceps sp.
-
slight activation in presence of His
prephenic acid
Claviceps sp.
-
slight activation in presence of His
additional information
-
activation mechanism of anthranilate synthase, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 3.1
chorismate
0.05 - 10
Gln
0.36
glutamine
-
-
0.0193 - 7
L-Gln
0.088 - 3.6
L-glutamine
0.0093 - 46
NH4+
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0061 - 383
chorismate
0.25
L-Gln
Archaeoglobus fulgidus
-
pH 8.0, 60C, with or without 2 M KCl and 25% glycerol
138 - 152
L-glutamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 2.6
(3-carbamoylphenoxy)acetic acid
0.11 - 0.25
(3-[[(5S)-6-([2-[6-(3-amino-3-oxopropyl)dibenzo[b,d]furan-4-yl]ethyl]amino)-5-[[2-(4-nitrophenyl)propanoyl]amino]-6-oxohexyl]carbamoyl]phenoxy)acetic acid
0.0036
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.0019
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.041
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25C
0.0053
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
0.059
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25C
0.12
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
0.1
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
0.05
2-(1-carboxy-ethylamino)-isonicotinate
-
pH 7.0, 25C
0.041
2-(3-(-(S)-5-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-4-(3-hydroxy-4-methyl-2-nitrobenzamido)-5-oxopentylcarbamoyl)-phenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.096
2-(3-(3-((R)-3-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-2-(3-hydroxy-4-methyl-2-nitrobenzamido)-3-oxopropylthio) propylcarbamoyl)phenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.094
2-(carboxymethyl-amino)-isonicotinate
-
pH 7.0, 25C
0.024
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
pH 7.0, 25C
0.021
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
pH 7.0, 25C
0.026
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
pH 7.0, 25C
0.0029
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
pH 7.0, 25C
0.025
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
pH 7.0, 25C
0.21 - 0.55
3-(carboxymethoxy)benzoic acid
0.4
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
pH 7.5
0.043
4-amino-3-(1-carboxyethoxy)benzoic acid
-
pH 7.0, 25C
0.023
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
pH 7.0, 25C
0.021
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.0054
DL-5-Methyltryptophan
-
-
0.00028 - 0.135
L-Trp
0.004 - 0.074
L-tryptophan
0.2
N-((S)-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxopropan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.11
N-((S)-6-amino-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxohexan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.08
N6-[3-(carboxymethoxy)benzoyl]-N2-(2,6-dimethoxybenzoyl)-L-lysyl-3-hydroxy-4-nitro-L-phenylalaninamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.02 - 0.054
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-3-chloro-L-phenylalaninamide
0.028 - 0.081
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-4-cyano-L-phenylalaninamide
0.33
p-Hydroxybenzaldehyde
-
pH 7.5
0.002
p-hydroxybenzoate
-
pH 7.5
0.26
vanillate
-
pH 7.5
0.49 - 1.081
[3-([(5S)-5-[[(3-benzoylpyridin-2-yl)carbonyl]amino]-6-[(1-carbamoylcyclohexyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
0.16 - 0.389
[3-([(5S)-6-[(1-carbamoylcyclohexyl)amino]-5-[(3,5-dihydroxybenzoyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
0.57 - 1.02
[3-([(5S)-6-[(4-carbamoyl-1,1-dioxidotetrahydro-2H-thiopyran-4-yl)amino]-6-oxo-5-[(4-phenoxybenzoyl)amino]hexyl]carbamoyl)phenoxy]acetic acid
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0063
L-Trp
Oryza sativa
-
feedback-inhibition, IC50: 0.0063 mM for wild-type enzyme, 0.0933 mM for mutant S126F, 0.0316 mM for mutant Y367A, 0.0749 mM for mutant A369L, 0.101 mM for mutant Y367A/L530D and 0.0583 mM for mutant A369L/L530D
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00077
original activity, un-induced state
0.0017
original activity, induced state
0.0022
activity after 5 years, un-induced state
0.0262
activity after 5 years, induced state
0.585
Claviceps sp.
-
-
2.16
crude supernatant
4.44
purification step Ni-NTA column
5.2
after concentration step
43
Hansenula henricii
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
Hansenula henricii
-
Gln-dependent reaction
7.2 - 7.6
-
Gln-dependent activity
7.3 - 8
-
isoenzyme AS-b
7.3
Hansenula henricii
-
NH4+-dependent enzyme
7.5 - 8.3
-
Gln-dependent activity
7.8
Claviceps sp.
-
Gln-dependent activity
8.1
-
L-Gln-dependent reaction, with 25% glycerol and 2 M KCl
8.6
Claviceps sp.
-
NH4+-dependent activity
additional information
-
NH4+-dependent activity increases linearly through pH 9.0 without reaching a maximum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
about 75% of maximal activity, Gln-dependent activity
6.5 - 9
-
pH 6.5: about 20% of maximal activity, pH 9.0: optimum
7 - 10
pH 7 20% relative activity, pH 10 60% relative activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37 - 40
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
-
25C: about 70% of maximal activity, 45C: about 85% of maximal activity
30 - 37
incubation at temperatures higher than 37C results in a significant reduction of activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.72
calculation from nucleotide sequence
8.38
calculation from nucleotide sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
normal cells and cells resistant to growth inhibition by DL-5-methyltryptophan
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
high activity in vascular region of yound stem, weak activity in older stem
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is synthesized as a higher MW precursor and then imported into chloroplasts and processed into the mature form
Manually annotated by BRENDA team
-
Trp-resistant form
Manually annotated by BRENDA team
-
,subunit Asalpha is synthesized as a cytosolic precursor, the active subunit is localized in the stroma of plastids
Manually annotated by BRENDA team
additional information
-
the Trp-sensitive form is localized in particulate fraction
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21050
calculated, beta, PabA subunit
47930
calculated, probable anthranilate synthase ORF CV0568
50000
Hansenula henricii
-
NH4-dependent enzyme, i.e. component I, gel filtration
54020
calculated, alpha, TrpE subunit
60000
gel filtration
62300
recombinant fusion protein, determined by SDS-PAGE
62350
determined by mass spectrometry
80000
-
gel filtration
86000
-
gel filtration or sucrose density gradient centrifugation in presence of 30% glycerol
94000 - 117000
-
gel filtration
122000
-
gel filtration
126000
-
sucrose density gradient centrifugation
139300
-
deduced from amino acid sequence
140000
-
sucrose density gradient centrifugation
141000
-
sucrose density gradient centrifugation
143000
-
gel filtration
150000
158000
-
gel filtration
160000
200000
220000
-
gel filtration
400000
Claviceps sp.
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotetramer
monomer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with its product 4-hydroxybenzoate
-
in complex with allosteric inhibitor L-tryptophan
-
in complex with chorismate, glutamine and glutamate and in complex with L-tryptophan
P00897 and P00500
in the absence of physiological ligands
Q06128 and Q06129
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 85
-
activity steadily increases with the rising of temperature in the range 25C to 85C, the enzyme is fully active above 85C
35
-
5 min, about 25% loss of activity
40
-
5 min, about 50% loss of activity
45
-
5 min, about 80% loss of activity
50
-
5 min, about 90% loss of activity
75
-
half-life in presence of 25% glycerol without KCl: 4.6 min, in 25% glycerol with 2 M KCl activity is constant for over 4 h after initial drop in activity to 83%
80
-
half-life in presence of 25% glycerol without KCl: 1.2 min, half-life in presence of 25% glycerol and 2 M KCl: 200 min
85
-
half-life in presence of 25% glycerol without KCl: 0.9 min, half-life in presence of 25% glycerol and 2 M KCl: 50 min
90
-
half-life in presence of 25% glycerol and 2 M KCl: 12 min
95
-
half-life in presence of 25% glycerol and 2 M KCl: 4.1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM dithiothreitol and 50 mM L-glutamine have a stabilizing effect each
-
anthranilate synthetase activity of the enzyme complex is quite unstable unless Gln, MgCl2, Tris and glycerol are included in the extraction buffer
Claviceps sp.
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, activity of partially purified enzyme declines during storage
-
-20C, in a 1:1 mixture of glycerol, 50 mM tricine, pH 7.5,1 mM DTT, 0.1 mM EDTA, additional protein bands appear upon storage, after an initial 10 15% drop in activity, little or no loss of enzyme activity is observed over a period of several weeks
-
-20C, unstable
-
-80C, 20 mM KH2PO4 buffer, 50 mM KCl, 1 mM DTT, pH 7.5
-
-80C, indefinitely stable
-
2C or -10C, activity declines to 3400 or 4000 units per mg and remains constant for several months
-
4C, TEA-sulfuric acid buffer, PH 7.2, stable for at least 2 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange chromatography
-
anthranilate synthase I, from a plasmid bearing Escherichia coli
-
immobilized metal ion affinity chromatography (Ni2+)
-
isoenzyme As-b
-
L-Trp-agarose in the purification of the anthranilate synthetase complex
-
partial
partial, from a high rutacridone producing cell line R-20 and from a low rutacrinone producing cell line R-15
-
recombinant wild-type and mutant His-tagged enzymes from Escherichia coli by nickel affinity and anion exchange chromatography
-
using Ni-NTA His-binding resin, the 6xHis-tag is removed by digestion with enterokinase
wild-type and mutant purified by hydroxyapatite chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha subunit (with a point mutation to confer feedback resistance to tryptophan) expressed in hairy root of Catharanthus roseus
-
cDNA(OASA1D) and the promoter of the maize ubiquitin gene is subcloned into pYT8C-Hm to generate pUASA1D, which also contains hpt as a selectable marker gene. For potato transformation, the vector p35SASA1D is constructed from pIG121-Hm, which contains the selectable marker genes hpt and nptII controlled by the 35S promoter of cauliflower mosaic virus, by replacing the beta-glucuronidase gene with the OASA1D cDNA
-
cloning of the genes phnA and phnB of the anthranilate synthase that participates in the synthesis of pyocyanin
-
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain JM109
-
expressed in Glycine max
-
expressed in Vigna angularis
-
expression in Escherichia coli
expression in Nicotiana tabacum; expression in Nicotiana tabacum
expression in Saccharomyces cerevisiae
-
expression of gene trpE in Escherichia coli strain BL21(DE3)RIPL and of wild-type and mutant genes trpGD and trpG in Escherichia coli strain BL21(DE3)Rosetta, all as N- and C-terminally His6-tagged proteins
-
expression of OASA1D/N323 in Solanum tuberosum induces a 2fold to 20fold increase in the amount of Trp
-
gene phnAB, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview; gene trpE, phylogenetic analysis, cloning in Escherichia coli strain Dh5alpha, enzyme expression in an enzyme-deficient Pseudomonas aeruginosa strain. Overexpression of anthranilate synthase genes trpE and phnAB results in pathway crosstalk, overview
P09785 and P09786, P20580
gene trpED
-
His-tagged veresion expressed in Escherichia coli C41(DE3)
-
into the BSMVm:gamma vector, the UbiNos_2-3 vector is used to express HvASa2. Into the hairpin vector pIPKTA30, hairpin construct co-bombarded with a Ubi:GUS expression vector into barley epidermal cells
into the pGEM-T Easy vector for expression in Escherichia coli cells
-
into the vector pET30a for expression in Escherichia coli BL21DE3 cells
into vector pAST-IV containing a 1671 bp long modified version of the ASA2 gene without a putative transit peptide and with an ASA2 3'-non-coding region (204 bp) as the termination sequence. Expression cassette containing Prrn-ASA2 integrated into the region between accD and ycf4 of the tobacco plastome
-
isolation of beta-subunit genes OASB1 and OASB2 and synthesis of each anthranilate synthase alpha-subunit (IASA1 and OASA2) and beta-subunit (OASB1 and OASB2) in wheat germ cell-free system
-
mutant anthanilate synthase Pro21Ser that is insensitive to feedback inhibition by Trp
-
partial complex anthranilate synthase expressed in Escherichia coli CB694
-
phylogenetic analysis, Agrobacterium-mediated co-overexpression of OsTDC, a putative tryptophan decarboxylase gene from rice, with OASA1D, the feedback-resistant anthranilate synthase alpha-subunit mutant in Oryza sativa calli, real-time quantitative reverse-transcription PCR expression analysis
-
quantitative real-time PCR enzyme expression analysis
transformation of Nicotiana tabacum with the ASA2 cDNA clone from Nicotiana tabacum driven by the CaMV 35S promoter and selected with kanamycin to obtain transformants that might be expressing ASA2
-
TrpE subunit
P00897 and P00500
wild-type and mutant overexpressed in Escherichia coli cells (strain CB694) harboring the pSTC25 plasmid
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-glutamine induces the enzyme transcription and translation through the regulation of auxin biosynthesis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R321H
-
Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R358H
-
Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R429H
-
similar Km value to the wild-type enzyme and a slightly larger turnover number
R452H
-
less than 0.05% of the activity of the wild-type enzyme
C14S
-
increase of Km value by 50%, improved behaviour in solution and crystallization
C81S
-
increase of Km value by 50%, improved behaviour in solution and crystallization
P21S
-
insensitive to feedback inhibition by Trp
A369L
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
A380S
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
A532Y
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
G518A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
G521A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
G522A
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
G522Y
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
L520F
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
L530D
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
N351A
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
N351D
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
N363A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
N363D
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P364A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P364L
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P366A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
S126A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
S356A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
Y349A
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y349F
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y367A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
Y367A/L530D
-
accumulation of free Trp in cells expressing the mutant OASA2 is 2.3fold of that of cells expressing wild-type D126F /L530D
Y516A
-
nonfunctional protein, anthranilate synthase alpha-subunit OASA2
P362L
-
TrpD subunit, enzyme is able to generate phosphoribosyl amine from ammonia and phosphoribosyl diphosphate
Q147K
-
does not exhibit anthranilate synthase activity. Using (NH4)2SO4, 29% of the wild-type activity is restored to the mutant, with anthranilate representing 97% of all products. Employs water as a nucleophile to a small extent
L126G
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme
L126G/V127Y/T129Y/Y131V
-
site-directed mutagenesis of anthranilate synthase glutaminase subunit TrpG residues, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme
T129A
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme
T129F
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme
T129Y
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant constitutively hydrolyzes glutamine in the absence of TrpE in contrast to the wild-type enzyme
V127Y
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme
Y131V
-
site-directed mutagenesis of a residue of the glutaminase subunit TrpG from anthranilate synthase, the mutant shows no activity with glutamine in absence of TrpE like the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
medicine
molecular biology
-
use of the feedback-insensitive alpha-subunit OASA1D (N323D) of anthranilate synthase as a selectable marker for transformation of rice and potato, the selection system will prove applicable to a wide range of plant species and culture procedures
synthesis
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