Any feedback?
Information on EC 4.1.3.27 - anthranilate synthase
for references in articles please use BRENDA:EC4.1.3.27Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.3.27 anthranilate synthaseIUBMB Comments
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.
Specify your search results
Word Map
- 4.1.3.27
-
amidotransferase
-
feedback-insensitive
-
trpeg
- l-tryptophan
- p-aminobenzoate
- isochorismate
- catharanthus
- roseus
-
glutamine-dependent
- 5-methyltryptophan
-
feedback-resistant
-
chorismate-utilizing
- tryptamine
- paba
- buchnera
- prephenate
-
indole-3-glycerol
- 4-amino-4-deoxychorismate
-
indoleglycerol
-
5-phosphoribosylpyrophosphate
-
aminodeoxychorismate
- biotechnology
- synthesis
- molecular biology
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
anthranilate synthase, anthranilate synthetase, oasa1d, oasa1, oasa2, phnab, anthranilate synthase component i, trped, hvasa2, anthranilate synthase-phosphoribosyltransferase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ANTA synthase
anthranilate synthase
anthranilate synthase component I
anthranilate synthase-phosphoribosyltransferase
-
tryptophan biosynthetic enzyme complex
anthranilate synthetase
-
-
-
-
AS-I
ASA
ASA1
ASA2
ASalpha
ASalphabeta
ASB
chorismate lyase
-
-
-
-
Glutamine amido-transferase
-
-
-
-
Glutamine amidotransferase
-
-
-
-
OASA1D
OASA2
synthase, anthranilate
-
-
-
-
synthetase, anthranilate
-
-
-
-
TrpE
TrpED
anthranilate synthase
-
-
-
-
OASA1D
-
feedback-insensitive alpha-subunit OASA1D (OASA1 with point mutation N323D)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
mechanism
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
mechanism
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
sequential mechanism
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
sequential mechanism
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
trans-6-amino-5-[(2-carboxyethenyl)-oxy]-1,3-cyclohexadiene-1-carboxylic acid is an enzyme-bound inhibitor
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
thermodynamics
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
mechanism
-
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9031-59-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chorismate + NH3
anthranilate + pyruvate + H2O
-
-
-
-
?
NH3 + phosphoribosyl diphosphate
phosphoribosyl amine
-
mutant P362L
-
?
chorismate + ammonia
anthranilate + pyruvate + H2O
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
feedback-insensitive enzyme
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
anthranilate synthase activity of mutant plants resistant to growth inhition by 5-methyltryptophan is 2.2fold to 3fold higher than that of the control. OASE2 is one of the key-regulating enzyme subunits in the tryptophan biosynthetic pathway
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
component I is inactive with L-Gln
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
one subunit of the enzyme contains a chorismate binding site and catalyzes the formation of anthranilate via 2-amino-2-deoxyisochorismate. After the first step, the intermediate remains bound to the enzyme, where it is subsequently converted to anthranilate through the elimination of pyruvate
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
?
chorismate + NH4+
?
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
?
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
feedback-insensitive enzyme
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
alpha-subunits (OASA1 or OASA2) alone possess anthranilate synthase activity with NH4+
-
-
?
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of avenanthramides
-
?
additional information
?
-
-
first enzyme in the branch pathway in Trp biosynthesis
-
-
?
additional information
?
-
-
active site residue that forms the covalent gamma-glutamyl-AS II intermediate is Cys
-
-
?
additional information
?
-
-
subunit ASalpha requires an ASbeta-subunit for Gln-dependent activity
-
-
?
additional information
?
-
-
ASI, is encoded by the gene TrpE and catalyzes the formation of anthranilate from chorismate and NH4+ as an independent subunit and from chorismate and Gln, when complexed with ASII. ASII consists of a glutamine amidotransferase domain, TrpG, which enables the complex to utilize Gln as an NH4+ source and an N-(5'-phosphoribosyl)anthranilate synthase domain, which catalyzes the production of N-(5'-phosphoribosyl)anthranilate from anthranilate and (5-phosphoribosyl)anthranilate
-
-
?
additional information
?
-
-
does not possess chorismate mutase promiscuous activity
-
-
?
additional information
?
-
-
regulation of the gene by attenuation
-
-
?
additional information
?
-
-
the 72000 Da subunit converts chorismate to anthranilate using NH4+. The 28000 Da subunit confers the enzyme the ability to use Gln instead of NH4+ as substrate
-
-
?
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
?
additional information
?
-
-
the 72000 Da subunit converts chorismate to anthranilate using NH4+. The 28000 Da subunit confers the enzyme the ability to use Gln instead of NH4+ as substrate
-
-
?
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
?
additional information
?
-
-
the enzyme does not utilize ammonia as a substrate
-
-
?
additional information
?
-
no substrate: asparagine
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chorismate + NH4+
anthranilate + pyruvate + H2O
-
feedback-insensitive enzyme
-
-
?
chorismate + ammonia
anthranilate + pyruvate + H2O
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
feedback-insensitive enzyme
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
-
anthranilate synthase activity of mutant plants resistant to growth inhition by 5-methyltryptophan is 2.2fold to 3fold higher than that of the control. OASE2 is one of the key-regulating enzyme subunits in the tryptophan biosynthetic pathway
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
one subunit of the enzyme contains a chorismate binding site and catalyzes the formation of anthranilate via 2-amino-2-deoxyisochorismate. After the first step, the intermediate remains bound to the enzyme, where it is subsequently converted to anthranilate through the elimination of pyruvate
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
-
-
-
-
?
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of avenanthramides
-
?
additional information
?
-
-
first enzyme in the branch pathway in Trp biosynthesis
-
-
?
additional information
?
-
-
regulation of the gene by attenuation
-
-
?
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
?
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Mg2+
-
Km for the mutant enzyme: 0.036 mM, Km for the wild-type enzyme: 0.101 mM
Mg2+
-
reaction of component I with NH4+ as substrate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,4R,5S,6S)-4-[(1-carboxyethenyl)oxy]-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-ene-2-carboxylic acid
-
-
(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
-
-
(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxy-6-methylidenecyclohex-1-ene-1-carboxylic acid
-
-
(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1R)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1S)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(2-carboxyprop-2-en-1-yl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic 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
-
-
1-(2-carboxyprop-2-en-1-yl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
-
1-(2-carboxyprop-2-en-1-yl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
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-oxoglutarate
-
reaction of component I with NH4+ as substrate
2-[[(1R,6R)-3-bromo-6-hydroxycyclohexa-2,4-dien-1-yl]oxy]prop-2-enoic acid
-
-
3-[[(1E)-1-carboxylatobut-1-en-1-yl]oxy]-2-hydroxybenzoate
-
3-[[(1E)-1-carboxylatoprop-1-en-1-yl]oxy]-2-hydroxybenzoate
-
3-[[(E)-1-carboxylato-2-phenylethenyl]oxy]-2-hydroxybenzoate
-
Bromopyruvate
-
inactivation prevented by chorismate and Trp
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
Gln
-
reaction of component I with NH4+ as substrate
Glu
-
reaction of component I with NH4+ as substrate
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
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
[(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-dien-1-yl]phosphonate
-
-
[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
-
-
5-Methyltryptophan
-
less effective inhibitor than 4-methylindole or 7-methyl-DL-tryptophan
6-diazo-5-oxo-L-norleucine
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
DL-5-fluorotryptophan
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
DL-5-Methyltryptophan
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
iodoacetamide
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
L-Trp
-
isoenzyme AS-b is inhibited 97% by 0.020 mM, isoenzyme AS-a is inhibited 66% by 0.020 mM
L-Trp
-
noncompetitive with respect to L-Gln, inhibitory effect increases with rising pH
L-Trp
-
strain with a anthanilate synthase that is insensitive to feedback inhibition by Trp, the 61st nucleotide, C to A substitution, that changes Pro21 to Ser is the cause of the desensitization to feedback inhibition by Trp
L-Trp
-
competitive with respect to chorismate; noncompetitive with respect to NH4+ and Gln
L-Trp
-
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
L-Trp
-
competitive with chorismate, noncompetitive with NH4+, reaction of component I with NH4+ as substrate
L-Trp
-
binding of a single inhibitor molecule to one TrpE subunit of the TrpE2-TrpD2 complex is sufficient for the propagation of a conformational change that affects the active site of the companion subunit; feedback inhibition
PCMB
-
reaction of component I with NH4+ as substrate
tryptophan
-
the enzyme is competitively but non-cooperatively inhibited by tryptophan
additional information
-
subunit ASA2 is insensitive to tryptophan feedback inhibition
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activation mechanism of anthranilate synthase, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Foot-and-Mouth Disease
Translational fusions with fragments of the trpE gene improve the expression of a poorly expressed heterologous gene in Escherichia coli.
Infections
Induction of serotonin biosynthesis is uncoupled from the coordinated induction of tryptophan biosynthesis in pepper fruits (Capsicum annuum) upon pathogen infection.
Infections
Isolation and genetic characterization of the nitA mutants of Escherichia coli affecting the termination factor rho.
Mouth Diseases
Translational fusions with fragments of the trpE gene improve the expression of a poorly expressed heterologous gene in Escherichia coli.
Protein Deficiency
Manipulation of amino acid composition in soybean seeds by the combination of deregulated tryptophan biosynthesis and storage protein deficiency.
Starvation
Regulation of tryptophan biosynthesis in Methanobacterium thermoautotrophicum Marburg.
Tuberculosis
Gut Microbiota Metabolite Indole Propionic Acid Targets Tryptophan Biosynthesis in Mycobacterium tuberculosis.
Tuberculosis
Mechanism of Fluorinated Anthranilate-Induced Growth Inhibition in Mycobacterium tuberculosis.
Tuberculosis
Purification and characterization of anthranilate synthase component I (TrpE) from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Resistance of Mycobacterium tuberculosis to indole 4-carboxamides occurs through alterations in drug metabolism and tryptophan biosynthesis.
Tuberculosis
Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
chorismate
-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60°C
0.0039
chorismate
-
saturating Mg2+, pH 7.0, 25°C
0.023
chorismate
-
Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2)
0.039
chorismate
-
pH 8.3, 32°C, A369L/L530D mutant anthranilate synthase alpha-subunit OASA2
0.043
chorismate
-
pH 8.3, 32°C, A369L mutant anthranilate synthase alpha-subunit OASA2
0.043
chorismate
-
pH 8.3, 32°C, wild-type enzyme, anthranilate synthase alpha-subunit OASA2
0.049
chorismate
-
pH 8.3, 32°C, S126F mutant anthranilate synthase alpha-subunit OASA2
0.058
chorismate
-
pH 8.3, 32°C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2
0.062
chorismate
-
pH 8.3, 32°C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
0.076
chorismate
-
pH 8.3, 32°C, Y367A mutant anthranilate synthase alpha-subunit OASA2
0.09
chorismate
-
two-component enzyme, ASI,ASII, with ammonium as cosubstrate
0.11
chorismate
-
reaction of component I, with NH4+ as cosubstrate
0.094
Gln
-
Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2)
0.0193
L-Gln
-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60°C
2.5
L-glutamine
-
wild-type, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
3.6
L-glutamine
-
mutant Q147K, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
0.0093
NH4+
-
in 50 mM Tris buffer (pH 8.0), 50 mM NH4Cl, and 10 mM MgCl2, at 60°C
additional information
additional information
-
-
-
additional information
additional information
-
steady-state enzyme kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.092
chorismate
-
pH 8.3, 32°C, Y367A mutant anthranilate synthase alpha-subunit OASA2
0.108
chorismate
-
pH 8.3, 32°C, S126F mutant anthranilate synthase alpha-subunit OASA2
0.22
chorismate
-
pH 8.3, 32°C, A369L mutant anthranilate synthase alpha-subunit OASA2
0.225
chorismate
-
pH 8.3, 32°C, wild-type enzyme, anthranilate synthase alpha-subunit OASA2
0.25
chorismate
-
pH 8.0, 60°C, with or without 2 M KCl and 25% glycerol
0.405
chorismate
-
pH 8.3, 32°C, A369L/L530D mutant anthranilate synthase alpha-subunit OASA2
0.49
chorismate
-
pH 8.3, 32°C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2
0.573
chorismate
-
pH 8.3, 32°C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
6.08
chorismate
-
pH 8.3, 32°C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
138
L-glutamine
-
wild-type, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
152
L-glutamine
-
mutant Q147K, at 25°C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.03
(3S)-3-[(1-carboxyethenyl)oxy]cyclohepta-1,6-diene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.29
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.041
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25°C
0.0053
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
0.059
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25°C
0.12
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
0.1
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
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, 25°C
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, 25°C
0.028
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.23
3-[(1-carboxyethenyl)oxy]-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.09
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
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, 25°C
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, 25°C
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, 25°C
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
0.49 - 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
0.76
(3-carbamoylphenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
2.6
(3-carbamoylphenoxy)acetic acid
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.11
(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
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
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
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
0.03
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
pH and temperature not specified in the publication
0.21
3-(carboxymethoxy)benzoic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
0.55
3-(carboxymethoxy)benzoic acid
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.005
L-tryptophan
75°C, ammonia-dependent activity, competitive to chorismate
0.074
L-tryptophan
75°C, glutamine-dependent activity, competitive to chorismate
0.02
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-3-chloro-L-phenylalaninamide
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
0.054
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-3-chloro-L-phenylalaninamide
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.028
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-4-cyano-L-phenylalaninamide
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
0.081
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-4-cyano-L-phenylalaninamide
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.49
[3-([(5S)-5-[[(3-benzoylpyridin-2-yl)carbonyl]amino]-6-[(1-carbamoylcyclohexyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
1.081
[3-([(5S)-5-[[(3-benzoylpyridin-2-yl)carbonyl]amino]-6-[(1-carbamoylcyclohexyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.16
[3-([(5S)-6-[(1-carbamoylcyclohexyl)amino]-5-[(3,5-dihydroxybenzoyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
0.389
[3-([(5S)-6-[(1-carbamoylcyclohexyl)amino]-5-[(3,5-dihydroxybenzoyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
0.57
[3-([(5S)-6-[(4-carbamoyl-1,1-dioxidotetrahydro-2H-thiopyran-4-yl)amino]-6-oxo-5-[(4-phenoxybenzoyl)amino]hexyl]carbamoyl)phenoxy]acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25°C
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
-
inhibitor binding to the enzyme-chorismate complex, pH 7.8, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.6
8.5
8.7
8.8
additional information
-
NH4+-dependent activity increases linearly through pH 9.0 without reaching a maximum
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
pH 7 20% relative activity, pH 10 60% relative activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
25°C: about 70% of maximal activity, 45°C: about 85% of maximal activity
30 - 37
incubation at temperatures higher than 37°C results in a significant reduction of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
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
-
-
brenda
L. cv. Shokan 1, induction with oligo-N-acetylchitooligosaccharide elicitors
-
-
brenda
Q06128: subunit TrpE, Q06129: subunit TrpG
UniProt
brenda
independent expression of subunits in Escherichia coli
UniProt
brenda
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
-
-
brenda
strain with a mutant anthranilate synthase Pro21Gln that is insensitive to feedback inhibition by Trp
-
-
brenda
multifunctional enzyme complex of anthranilate synthetase with phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
-
-
brenda
two enzyme forms, one form is resistant to feedback inhibition by 0.01 mM Trp, the other form is completely inhibited by Trp at the same concentration
-
-
brenda
CCY 38-10-2, the organism contains an NH4-dependent enzyme (component I) and a Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2)
-
-
brenda
var. Donganbyeo, and mutant lines resistant to growth inhition by 5-methyltryptophan
-
-
brenda
anthranilate synthase phnAB, composed of glutamine amidotransferase component phnB (P09786) and anthranilate synthase component pyocyanine-specific phnA (P09785)
SwissProt
brenda
anthranilate synthase TrpEG, composed of glutamine amidotransferase component trpG (P20576) and anthanilate synthase component trpE (P20580); PA14, genes trpG, trpE
SwissProt
brenda
one anthranilate synthase participates in Trp synthesis and is encoded by the genes trpE and trpG, the other anthranilate synthase is encoded by the genes phnA and phnB and participates in the synthesis of pyocyanin
-
-
brenda
a high rutacridone producing cell line R-20 and low rutacrinone producing cell line R-15
-
-
brenda
Q06128: subunit TrpE, Q06129: subunit TrpG
UniProt
brenda
-
-
-
brenda
expression in Escherichia coli
-
-
brenda
multifunctional anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
-
-
brenda
multifunctional enzyme anthranilate synthase/N(5'-phosphoribosyl)anthranilate synthase (ec 4.1.3.27/ec 2.4.2.18, or ASI/ASII)
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
normal cells and cells resistant to growth inhibition by DL-5-methyltryptophan
brenda
high activity in vascular region of yound stem, weak activity in older stem
brenda
additional information
CaASA1 mRNA is first detected at 2 days post imbibition and reaches a maximum at 6 days post imbibition
brenda
additional information
level of CaASA2 is constitutively low in Camptotheca acuminata and is found mainly in the reproductive tissues in transgenic tobacco plants
brenda
additional information
level of CaASA2 is constitutively low in Camptotheca acuminata and is found mainly in the reproductive tissues in transgenic tobacco plants
brenda
additional information
-
level of CaASA2 is constitutively low in Camptotheca acuminata and is found mainly in the reproductive tissues in transgenic tobacco plants
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is synthesized as a higher MW precursor and then imported into chloroplasts and processed into the mature form
brenda
-
subunit Asalpha is synthesized as a cytosolic precursor, the active subunit is localized in the stroma of plastids
brenda
additional information
-
the Trp-sensitive form is localized in particulate fraction
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
malfunction
-
mutation in strain trpD9923 (mutant in the tryptophan operon) results in the synthesis of a truncated anthranilate synthase component II protein, retaining the full glutamine amidotransferase domain and only seven of the 333 amino acid residues of the anthranilate phosphoribosyl transferase domain. Mutation in the trpD gene causes the loss of anthranilate phosphoribosyl transferase activity, but maintains anthranilate synthase activity, thus causing anthranilate accumulation
malfunction
Virus-induced gene silencing of HvCS, HvASa2, and HvCM1 increase formation of Blumeria graminis f. sp. hordei secondary hyphae but not conidiation in Mla6-mediated resistant plants
malfunction
phnAB mutants are tryptophan prototrophs but do not produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone in minimal media
malfunction
trpEG mutants are tryptophan auxotrophs but produce Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone
malfunction
-
mutation in strain trpD9923 (mutant in the tryptophan operon) results in the synthesis of a truncated anthranilate synthase component II protein, retaining the full glutamine amidotransferase domain and only seven of the 333 amino acid residues of the anthranilate phosphoribosyl transferase domain. Mutation in the trpD gene causes the loss of anthranilate phosphoribosyl transferase activity, but maintains anthranilate synthase activity, thus causing anthranilate accumulation
-
metabolism
Pseudomonas aeruginosa possesses two functional anthranilate synthases, TrpEG and PhnAB, and these enzymes are not functionally redundant. They are involved in biosynthesis of Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, which regulates density-dependent production of toxic factors involved in Pseudomonas aeruginosa virulence. TrpED catalyzes the first step in tryptophan biosynthesis
metabolism
Pseudomonas aeruginosa possesses two functional anthranilate synthases, TrpEG and PhnAB, and these enzymes are not functionally redundant. They are involved in biosynthesis of Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, which regulates density-dependent production of toxic factors involved Pseudomonas aeruginosa virulence. TrpED catalyzes the first step in tryptophan biosynthesis
metabolism
-
the enzyme catalyzes the initial step in the pathway for both tryptophan-dependent and tryptophan-independent pathways in the biosynthesis of indole-3-acetic acid, the transfer of the alpha-amino group of glutamine to chorismate producing anthranilate
metabolism
-
the enzyme catalyzes the initial step in the pathway for both tryptophan-dependent and tryptophan-independent pathways in the biosynthesis of indole-3-acetic acid, the transfer of the alpha-amino group of glutamine to chorismate producing anthranilate
metabolism
-
anthranilate synthase functions as rate-limiting factor for the biosynthesis of pyrroloquinazoline alkaloids
physiological function
-
plastid transformed lines exhibit a higher level of anthranilate synthase activity that is less sensitive to tryptophan-feedback inhibition and, consequently, increases free tryptophan levels in leaves about 7fold. Overexpression of ASA2 gene does not result in any negative effects for the plants
physiological function
role of HvCS, HvASa2, and HvCM1 in penetration resistance to Blumeria graminis f. sp.hordei. HvCS, HvCM1, and HvASa2 contribute to mlo-mediated broad-spectrum resistance
physiological function
conversion of the central metabolite chorismate to anthranilate by anthranilate synthase is required for Pseudomonas quinolone signal 2-heptyl-3-hydroxy-4-quinolone, PQS, biosynthesis. The reaction is also the first step in tryptophan biosynthesis
physiological function
-
enhanced cellular glutamine may account for the enhanced growth in glutamine synthase-expressing transgenic poplar plants through the regulation of auxin biosynthesis
physiological function
-
enzyme activity is required for indole-3-butyric acid-induced adventitious root formation
Show AA Sequence and Transmembrane Helices (42078 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
150000
160000
18000
20000
-
2 * 20000 + 2 * 50000, Gln-dependent enzyme, composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, I2II2, gel filtration
200000
21100
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
23000
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
400000
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, gel filtration
48500
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
50000
57000
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
60000
70000
71000
80000
86000
-
gel filtration or sucrose density gradient centrifugation in presence of 30% glycerol
additional information
160000
-
Gln-dependent enzyme composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2), gel filtration
200000
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, sucrose density gradient centrifugation
70000
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
additional information
-
anthranilate synthetase component II has a MW of 21684 Da, determined by amino acid sequence analysis after separation of the two protein components
additional information
-
anthranilate synthetase component II has a MW of 21684 Da, determined by amino acid sequence analysis after separation of the two protein components
additional information
-
anthranilate synthetase component II has a MW of 21684 Da, determined by amino acid sequence analysis after separation of the two protein components
additional information
-
the beta-subunit has a MW of 84000 Da determined by SDS-PAGE
additional information
experimental value between 84 and 95 kDa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
heterotetramer
monomer
tetramer
additional information
?
-
x * 60000-65000 + x + 60000-65000, Asalpha-subunit and Asbeta-subunit are of a similar MW
dimer
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
heterodimer
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
heterotetramer
association of 2 * enzyme + 2 * glutamine amidotransferase, crystallographic data
heterotetramer
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
heterotetramer
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
-
heterotetramer
-
association of 2 * enzyme + 2 * glutamine amidotransferase, crystallographic data
-
heterotetramer
-
crystallographic data
tetramer
-
2 * 20000 + 2 * 50000, Gln-dependent enzyme, composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, I2II2, gel filtration
additional information
-
the large component from Bacillus subtilis (IB) complements well with the small component from Pseudomonas aeruginosa (IIP) to reconstitute a glutamine-reactive anthranilate synthase. Complementation was also observed with the large component from Pseudomonas aeruginosa (Iv) and the small subunit from Bacillus subtilis (IIB)
additional information
-
one subunit is a trifunctional peptide which contains the catalytic sites for phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase reactions, and associates with the second subunit to form Gln-dependent anthranilate synthetase
additional information
-
recombinant alpha-subunit interacts with native beta-subunit to form an active enzyme
additional information
-
the organism contains an NH4-dependent enzyme, i.e. component I, and a Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, i.e. I2II2
additional information
-
the large component from Bacillus subtilis (IB) complements well with the small component from Pseudomonas aeruginosa (IIP) to reconstitute a glutamine-reactive anthranilate synthase. Complementation was also observed with the large component from Pseudomonas aeruginosa (Iv) and the small subunit from Bacillus subtilis (IIB)
additional information
-
glutamine, 10 mM, enhances binding of AS I and II, as does Mg2+. ASI and ASII play a joint role in the binding of L-Gln, negligible binding to either component alone
additional information
-
component I has a MW of 63000 Da, gel filtration
additional information
-
multifunctional anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
additional information
-
multifunctional enzyme anthranilate synthase/N(5'-phosphoribosyl)anthranilate synthase, EC 4.1.3.27/EC 2.4.2.18, or ASI/ASII. ASI, is encoded by the gene TrpE and catalyzes the formation of anthranilate from chorismate and NH4+ as an independent subunit and from chorismate and Gln, when complexed with ASII. ASII consists of a glutamine amidotransferase domain, TrpG, which enables the complex to utilize Gln as an NH4+ source and an N-(5'-phosphoribosyl)anthranilate synthase domain, which catalyzes the production of N-(5'-phosphoribosyl)anthranilate from anthranilate and (5-phosphoribosyl)anthranilate
additional information
-
partial complex anthranilate synthase consists of two TrpE:TrpG heterodimers
additional information
-
subunit ASI catalyzes NH4+-dependent synthesis of anthranilate. Gln is not a substrate for ASI. ASII provides Gln-amide transfer function
additional information
-
subunit ASI catalyzes NH4+-dependent synthesis of anthranilate. Gln is not a substrate for ASI. ASII provides Gln-amide transfer function
-
additional information
-
the 72000 Da subunit converts chorismate to anthranilate using NH4+. The 28000 Da subunit confers the enzyme the ability to use Gln instead of NH4+ as substrate
additional information
-
the 72000 Da subunit converts chorismate to anthranilate using NH4+. The 28000 Da subunit confers the enzyme the ability to use Gln instead of NH4+ as substrate
-
additional information
-
synthase subunit TrpE and glutaminase subunit TrpG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 150 mM trisodium citrate pH 5.5, 0.75-1.5 M ammonium sulfate, 0.25-0.5 M lithium sulfate
in complex with allosteric inhibitor L-tryptophan
-
in complex with chorismate, glutamine and glutamate and in complex with L-tryptophan
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
Y349A
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y349F
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y367A/L530D
-
accumulation of free Trp in cells expressing the mutant OASA2 is 2.3fold of that of cells expressing wild-type D126F /L530D
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
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
additional information
additional information
-
the trpE-mutant is created by deletion of the fragment between positions +64 and +926 in the trpE coding region and replacement with the 1.2 kb Km resistance fragment from plasmid pUC4K, the mutant shows a marked inhibition by L-tryptophan compared to the wild type strain
additional information
-
the trpE1(G)-mutant is created by deleting a DNA segment containing the N-terminal portion (from the 2nd codon to 374th codon) of the trpE1(G) gene by PCR amplification of chromosomal sequences flanking the trpE1(G) locus in wild type strain Yu62, the mutant shows no inhibition by L-tryptophan compared to the wild type strain
additional information
-
the trpE-mutant is created by deletion of the fragment between positions +64 and +926 in the trpE coding region and replacement with the 1.2 kb Km resistance fragment from plasmid pUC4K, the mutant shows a marked inhibition by L-tryptophan compared to the wild type strain
-
additional information
-
the trpE1(G)-mutant is created by deleting a DNA segment containing the N-terminal portion (from the 2nd codon to 374th codon) of the trpE1(G) gene by PCR amplification of chromosomal sequences flanking the trpE1(G) locus in wild type strain Yu62, the mutant shows no inhibition by L-tryptophan compared to the wild type strain
-
additional information
-
construction of an L-tryptophan overproducing Escherichia coli strain from strain JM109 by defined genetic modification methodology via elimination of feedback inhibitions of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase (AroF) and anthranilate synthase by site-directed mutagenesis. Expression of deregulated AroF and TrpED is achieved by using a temperature-inducible expression plasmid pSV. Transcriptional regulation of trp repressor is removed by deleting trpR. The pathway for L-Trp degradation is removed by deleting tnaA. L-Phenylalanine and L-tyrosine biosynthesis pathways that compete with L-tryptophan biosynthesis are blocked by deleting their critical genes, pheA and tyrA. L-Phe, L-Tyr, and L-Trp accumulate in the culture medium, phenotype, overview
additional information
Escherichia coli W3110 / ATCC 27325
-
construction of an L-tryptophan overproducing Escherichia coli strain from strain JM109 by defined genetic modification methodology via elimination of feedback inhibitions of 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase (AroF) and anthranilate synthase by site-directed mutagenesis. Expression of deregulated AroF and TrpED is achieved by using a temperature-inducible expression plasmid pSV. Transcriptional regulation of trp repressor is removed by deleting trpR. The pathway for L-Trp degradation is removed by deleting tnaA. L-Phenylalanine and L-tyrosine biosynthesis pathways that compete with L-tryptophan biosynthesis are blocked by deleting their critical genes, pheA and tyrA. L-Phe, L-Tyr, and L-Trp accumulate in the culture medium, phenotype, overview
-
additional information
-
tobacco leaves fed with 30 mM glutamine and 2 mM chorismate produce significantly enhanced ASA alpha-subunit (ASA1) transcript and protein, approximately 175% and 90% higher than in the untransformed controls, respectively
additional information
-
tryptophan decarboxylase inactivity is a contributory factor for the accumulation of Trp in rice transgenics overexpressing the feedback-resistant anthranilate synthase alpha-subunit mutant OASA1D, high-Trp transgenic line overexpressing OASA1D line HW5 phenotype, overview. The calli expressing OsTDC and OASA1D reveal the accumulation of serotonin and serotonin-derived indole compounds (potentially pharmacoactive beta-carbolines), and of two epimers of 2-hydroxy-3-(3'-aminoethyl-5'-hydroxyindol-2'-yl)-3-indol-3'-yl-propyl beta-D-glucopyranoside not described previously. Metabolic profiles, overview
additional information
-
tryptophan decarboxylase inactivity is a contributory factor for the accumulation of Trp in rice transgenics overexpressing the feedback-resistant anthranilate synthase alpha-subunit mutant OASA1D, high-Trp transgenic line overexpressing OASA1D line HW5 phenotype, overview. The calli expressing OsTDC and OASA1D reveal the accumulation of serotonin and serotonin-derived indole compounds (potentially pharmacoactive beta-carbolines), and of two epimers of 2-hydroxy-3-(3'-aminoethyl-5'-hydroxyindol-2'-yl)-3-indol-3'-yl-propyl beta-D-glucopyranoside not described previously. Metabolic profiles, overview
-
additional information
-
leaves of transgenic poplar with ectopic expression of the pine cytosolic glutamine synthetase, GS1a, EC 6.3.1.2, produce significantly more glutamine and significantly enhanced ASA alpha-subunit (ASA1) transcript and protein, approximately 130% and 120% higher than in the untransformed controls, respectively. L-Glutamate, tryptophan, and 4-aminobutanoate are also significantly enhanced in the GS1a transgenic poplars
additional information
-
a mutant enzyme that has a considerable portion of its coding sequence deleted and replaced by a tetracycline resistance gene is not feedback inhibited by Trp
additional information
construction of several different trpE and phnAB knockout mutants. DELTAtrpE tryptophan auxotrophy is dependent upon phnAB expression. Overexpression of either anthranilate synthase complements the loss of the other
additional information
construction of several different trpE and phnAB knockout mutants. DELTAtrpE tryptophan auxotrophy is dependent upon phnAB expression. Overexpression of either anthranilate synthase complements the loss of the other
additional information
-
construction of several different trpE and phnAB knockout mutants. DELTAtrpE tryptophan auxotrophy is dependent upon phnAB expression. Overexpression of either anthranilate synthase complements the loss of the other
additional information
-
in contrast to wild-type TrpG, two TrpG variants with single exchanges constitutively hydrolyze glutamine in the absence of TrpE. The introduced amino acid exchanges result in a distance reduction between the active site Cys-His pair, which facilitates the deprotonation of the sulfhydryl group of the catalytic cysteine and thus enables its nucleophilic attack onto the carboxamide group of the glutamine side chain, molecular dynamics simulations, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 85
-
activity steadily increases with the rising of temperature in the range 25°C to 85°C, the enzyme is fully active above 85°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 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
-
-80°C, 20 mM KH2PO4 buffer, 50 mM KCl, 1 mM DTT, pH 7.5
-
2°C or -10°C, activity declines to 3400 or 4000 units per mg and remains constant for several months
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange chromatography
-
L-Trp-agarose in the purification of the anthranilate synthetase complex
-
Ni-NTA column chromatography and Superdex 200 gel filtration
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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
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 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
-
wild-type and mutant overexpressed in Escherichia coli cells (strain CB694) harboring the pSTC25 plasmid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both exogenous indole-3-acetic acid and exogenous indole-3-butyric acid induce the expression of the enzyme's alpha subunit
-
L-glutamine induces the enzyme transcription and translation through the regulation of auxin biosynthesis
L-glutamine induces the enzyme transcription and translation through the regulation of auxin biosynthesis
-
L-glutamine induces the enzyme transcription and translation through the regulation of auxin biosynthesis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
biotechnology
-
development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923
biotechnology
-
development of ASA2 as a chloroplast selective marker, which is important not only for biosafety reasons, but also for practical reason due to the scarcity of primary selective markers available
biotechnology
-
Oryza sativacalli overexpressing OASA1D:OASA1D is a system for the production of significant amounts of pharmacologically useful indole alkaloids in rice
biotechnology
-
Oryza sativacalli overexpressing OASA1D:OASA1D is a system for the production of significant amounts of pharmacologically useful indole alkaloids in rice
-
biotechnology
-
development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923
-
medicine
TrpE is a promising target for the design of novel anti-tuberculosis drugs
medicine
-
TrpE is a promising target for the design of novel anti-tuberculosis drugs
-
synthesis
-
Oryza sativacalli overexpressing OASA1D:OASA1D is a system for the production of significant amounts of pharmacologically useful indole alkaloids in rice
synthesis
-
Oryza sativacalli overexpressing OASA1D:OASA1D is a system for the production of significant amounts of pharmacologically useful indole alkaloids in rice
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hulett, F.M.; DeMoss, J.A.
Subunit structure of anthranilate synthetase from Neurospora crassa
J. Biol. Chem.
250
6648-6652
1975
Neurospora crassa
brenda
Baker, T.I.; Crawford, I.P.
Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli
J. Biol. Chem.
241
5577-5584
1966
Escherichia coli
brenda
Zalkin, H.; Kling, D.
Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium
Biochemistry
7
3566-3573
1968
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Robb, F.; Hutchinson, M.A.; Belser, W.L.
Anthranilate synthetase. Some physical and kinetic properties of the enzyme from Serratia marcescens
J. Biol. Chem.
246
6908-6912
1971
Serratia marcescens
brenda
Zalkin, H.; Hwang, L.H.
Anthranilate synthetase from Serratia marcescens
J. Biol. Chem.
246
6899-6907
1971
Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
-
brenda
Widholm, J.M.
Anthranilate synthetase from 5-methyltryptophan-susceptible and -resistant cultured Daucus carota cells
Biochim. Biophys. Acta
279
48-57
1972
Daucus carota
brenda
Queener, S.W.; Queener, S.F.; Meeks, J.R.; Gunsalus, I.C.
Anthranilate synthase from Pseudomonas putida. Purification and properties of a two-component enzyme
J. Biol. Chem.
248
151-161
1973
Pseudomonas putida
brenda
Sawula, R.V.; Crawford, I.P.
Anthranilate synthetase of Acinetobacter calcoaceticus. Separation and partial characterization of subunits
J. Biol. Chem.
248
3573-3581
1973
Acinetobacter calcoaceticus
brenda
Zalkin, H.
Anthranilate synthetase
Adv. Enzymol. Relat. Areas Mol. Biol.
38
1-39
1973
Klebsiella aerogenes, Aspergillus nidulans, Bacillus subtilis, Saccharomyces cerevisiae, Chromobacterium violaceum, Delftia acidovorans, Comamonas testosteroni, Escherichia coli, Neurospora crassa, Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
brenda
Marcus, S.L.
L-Tryptophan-agarose in the purification of an anthranilate synthetase complex
Methods Enzymol.
34B
389-394
1974
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Goto, Y.; Zalkin, H.; Keim, P.S.; Heinrikson, R.L.
Properties of anthranilate synthetase component II from Pseudomonas putida
J. Biol. Chem.
251
941-949
1976
Pseudomonas putida
brenda
Friedrich, C.G.; Friedrich, B.; Schlegel, H.G.
Aromatic amino acid biosynthesis in Alcaligenes eutrophus H 16 III. Properites and regulation of anthranilate synthase
Arch. Microbiol.
107
125-131
1976
Cupriavidus necator, Cupriavidus necator H 16
brenda
Schmauder, H.P.; Grger, D.
Zur Charakterisierung der Anthranilat-Synthetase bei Claviceps
Biochem. Physiol. Pflanz.
169
471-486
1976
Claviceps purpurea, Claviceps sp., Claviceps sp. SD58
-
brenda
Hankins, C.N.; Mills, S.E.
Anthranilate synthase-amidotransferase (combined). A novel from of antrhanilate synthase from Euglena gracilis
J. Biol. Chem.
251
7774-7778
1976
Euglena gracilis, Euglena gracilis Z
brenda
Mann, D.F.; Floss, H.G.
Purification and properties of anthranilate synthetase from the ergot fungus, Claviceps spec., strain SD 58
Lloydia
40
136-145
1977
Claviceps sp., Claviceps sp. SD58
brenda
Bode, R.; Birnbaum, D.
Die Enzyme der Biosynthese aromatischer Aminosuren bei Hansenula henricii: Charakterisierung der Anthranilat-synthase
Biochem. Physiol. Pflanz.
172
245-253
1978
Ogataea henricii
-
brenda
Bode, R.; Birnbaum, D.
Die Enzyme der Biosynthese aromatischer Aminosuren bei Hansenula henricii: Hemmung der Anthranilat-Synthase durch Tryptophan und Tryptophanderivate
Biochem. Physiol. Pflanz.
172
255-261
1978
Ogataea henricii
-
brenda
Francis, M.M.; Vining, L.C.; Westlake, D.W.S.
Characterization and regulation of anthranilate synthetase from a chloramphenicol-producing streptomycete
J. Bacteriol.
134
10-16
1978
Streptomyces sp., Streptomyces sp. 3022a
brenda
Kawamura, M.; Keim, P.S.; Goto, Y.; Zalkin, H.; Heinrikson, R.L.
Anthranilate synthetase component II from Pseudomonas putida. Covalent structure and identification of the cysteine residue involved in catalysis
J. Biol. Chem.
253
4659-4668
1978
Pseudomonas putida
brenda
Tso, J.Y.; Hermodson, M.A.; Zalkin, H.
Primary structure of Serratia marcescens anthranilate synthase component II
J. Biol. Chem.
255
1451-1457
1980
Serratia marcescens
brenda
Keesey, J.; Paukert, J.; Demoss, J.A.
Subunit structure of anthranilate synthase from Neurospora crassa: preparation and characterization of a protease-free form
Arch. Biochem. Biophys.
207
103-109
1981
Neurospora crassa
brenda
Walker, M.S.; DeMoss, J.A.
Purification and characterization of the trifunctional beta-subunit of anthranilate synthase from Neurospora crassa
J. Biol. Chem.
258
3571-3575
1983
Neurospora crassa
brenda
Zalkin, H.
Anthranilate synthase
Methods Enzymol.
113
287-292
1985
Serratia marcescens, Serratia marcescens HY150
brenda
Brotherton, J.E.; Hauptmann, R.M.; Widholm, J.M.
Anthranilate synthase forms in plants and cultured cells of Nicotiana tabacum L.
Planta
168
214-221
1986
Daucus carota, Nicotiana tabacum, Zea mays
brenda
Crawford, I.P.
Anthranilate synthase from fluorescent Pseudomonads
Methods Enzymol.
142
300-306
1987
Pseudomonas putida
brenda
Romero, R.M.; Roberts, M.F.
Anthranilate synthase from Ailanthus altissima cells suspension cultures
Phytochemistry
41
395-402
1996
Ailanthus altissimus, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Zhao, J.; Last, R.L.
Immunological characterization and chloroplast localization of the tryptophan biosynthetic enzymes of the flowering plant Arabidopsis thaliana
J. Biol. Chem.
270
6081-6087
1995
Arabidopsis thaliana
brenda
Morollo, A.A.; Bauerle, R.
Characterization of composite aminodeoxyisochorismate synthase and aminodeoxyisochorismate lyase activities of anthranilate synthase
Proc. Natl. Acad. Sci. USA
90
9983-9987
1993
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Tolbert, W.D.; Chatterji, S.; Bauerle, R.; Kretsinger, R.
Crystallization and preliminary crystallographic studies of the anthranilate synthase partial complex from Salmonella typhimurium
Acta Crystallogr. Sect. D
55
305-306
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Poulsen, C.; Bongaerts, R.J.M.; Verpoorte, R.
Purification and characterization of anthranilate synthase from Catharanthus roseus
Eur. J. Biochem.
212
431-440
1993
Catharanthus roseus
brenda
Kozlowski, M.C.; Tom, N.J.; Seto, C.T.; Sefler, A.M.; Bartlett, P.A.
Chorismate-utilizing enzymes isochorismate synthase, anthranilate synthase, and p-aminobenzoate synthase: mechanistic insight through inhibitor design
J. Am. Chem. Soc.
117
2128-2140
1995
Escherichia coli
-
brenda
Bohlmann, J.; DeLuca, V.; Eilert, U.; Martin, W.
Purification and cDNA cloning of anthranilate synthase from Ruta graveolens: modes of expression and properties of native and recombinant enzymes
Plant J.
7
491-501
1995
Ruta graveolens
brenda
Caligiuri, M.G.; Bauerle, R.
Subunit communication in the anthranilate synthase complex from Salmonella typhimurium
Science
252
1845-1848
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Shiratsuchi, A.; Sato, S.
Characterization of Bacillus caldotenax anthranilate synthase I produced in Escherichia coli and identification of its essential arginine residue by site-directed mutagenesis
J. Biochem.
112
714-718
1992
[Bacillus] caldotenax
brenda
Kwak, J.H.; Hong, K.W.; Lee, S.H.; Hong, J.H.; Lee, S.Y.
Identification of amino acid residues involved in feedback inhibition of the anthranilate synthase in Escherichia coli
J. Biochem. Mol. Biol.
32
20-24
1999
Corynebacterium glutamicum, Escherichia coli
-
brenda
Bae, Y.M.; Crawford, I.P.
The Rhizobium meliloti trpE(G) gene is regulated by attenuation, and its product, anthranilate synthase, is regulated by feedback inhibition
J. Bacteriol.
172
3318-3327
1990
Sinorhizobium meliloti
brenda
Essar, D.W.; Eberly, L.; Hadero, A.; Crawford, I.P.
Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications
J. Bacteriol.
172
884-900
1990
Pseudomonas aeruginosa
brenda
Hertel, S.C.; Hieke, M.; Grger, D.
Anthranilate synthase from Ruta graveolens: partial purification and properties
Biochem. Physiol. Pflanz.
187
121-129
1991
Ruta graveolens
-
brenda
Tang, X.F.; Ezaki, S.; Atomi, H.; Imanaka, T.
Anthranilate synthase without an LLES motif from a hyperthermophilic archaeon is inhibited by tryptophan
Biochem. Biophys. Res. Commun.
281
858-865
2001
Thermococcus kodakarensis (Q9YGB3)
brenda
Byrnes, W.M.; Goldberg, R.N.; Holden, M.J.; Mayhew, M.P.; Tewari, Y.B.
Thermodynamics of reactions catalyzed by anthranilate synthase
Biophys. Chem.
84
45-64
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ramos, I.; Downs, D.M.
Anthranilate synthase can generate sufficient phosphoribosyl amine for thiamine synthesis in Salmonella enterica
J. Bacteriol.
185
5125-5132
2003
Salmonella enterica
brenda
Morollo, A.A.; Eck, M.J.
Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium
Nat. Struct. Biol.
8
243-247
2001
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cho, H.J.; Brotherton, J.E.; Song, H.S.; Widholm, J.M.
Increasing tryptophan synthesis in a forage legume Astragalus sinicus by expressing the tobacco feedback-insensitive anthranilate synthase (ASA2) gene
Plant Physiol.
123
1069-1076
2000
Nicotiana sylvestris
brenda
Knochel, T.; Ivens, A.; Hester, G.; Gonzalez, A.; Bauerle, R.; Wilmanns, M.; Kirschner, K.; Jansonius, J.N.
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications
Proc. Natl. Acad. Sci. USA
96
9479-9484
1999
Saccharolobus solfataricus (Q06128 and Q06129), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q06128 and Q06129)
brenda
Spraggon, G.; Kim, C.; Nguyen-Huu, X.; Yee, M.C.; Yanofsky, C.; Mills, S.E.
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan
Proc. Natl. Acad. Sci. USA
98
6021-6026
2001
Serratia marcescens (P00897 and P00500), Serratia marcescens
brenda
Gallagher, D.T.; Mayhew, M.; Holden, M.J.; Howard, A.; Kim, K.J.; Vilker, V.L.
The crystal structure of chorismate lyase shows a new fold and a tightly retained product
Proteins
44
304-311
2001
Escherichia coli
brenda
Matsukawa, T.; Ishihara, A.; Iwamura, H.
Induction of anthranilate synthase activity by elicitors in oats
Z. Naturforsch. C
57
121-128
2002
Avena sativa
brenda
Byrnes, W.M.; Vilker, V.L.
Extrinsic factors potassium chloride and glycerol induce thermostability in recombinant anthranilate synthase from Archaeoglobus fulgidus
Extremophiles
8
455-462
2004
Archaeoglobus fulgidus
brenda
Patel, N.; Holmes, W.M.; Kane, J.F.
Intergeneric complementation of anthranilate synthase subunits
J. Bacteriol.
114
600-602
1973
Bacillus subtilis, Pseudomonas aeruginosa
brenda
Yamada, T.; Tozawa, Y.; Hasegawa, H.; Terakawa, T.; Ohkawa, Y.; Wakasa, K.
Use of a feedback-insensitive ? subunit of anthranilate synthase as a selectable marker for transformation of rice and potato.
Mol. Breed.
14
363-373
2004
Oryza sativa
brenda
Payne, R.J.; Bulloch, E.M.; Abell, A.D.; Abell, C.
Design and synthesis of aromatic inhibitors of anthranilate synthase
Org. Biomol. Chem.
3
3629-3635
2005
Serratia marcescens
brenda
Tsai, F.Y.; Brotherton, J.E.; Widholm, J.M.
Overexpression of the feedback-insensitive anthranilate synthase gene in tobacco causes tryptophan accumulation
Plant Cell Rep.
23
548-556
2005
Nicotiana tabacum
brenda
Kim, D.S.; Lee, I.S.; Jang, C.S.; Kang, S.Y.; Seo, Y.W.
Characterization of the altered anthranilate synthase in 5-methyltryptophan-resistant rice mutants
Plant Cell Rep.
24
357-365
2005
Oryza sativa
brenda
Kanno, T.; Kasai, K.; Ikejiri-Kanno, Y.; Wakasa, K.; Tozawa, Y.
In vitro reconstitution of rice anthranilate synthase: distinct functional properties of the alpha subunits OASA1 and OASA2
Plant Mol. Biol.
54
11-23
2004
Oryza sativa
brenda
Kanno, T.; Komatsu, A.; Kasai, K.; Dubouzet, J.G.; Sakurai, M.; Ikejiri-Kanno, Y.; Wakasa, K.; Tozawa, Y.
Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway
Plant Physiol.
138
2260-2268
2005
Oryza sativa
brenda
Lu, H.; Gorman, E.; McKnight, T.D.
Molecular characterization of two anthranilate synthase alpha subunit genes in Camptotheca acuminata
Planta
221
352-360
2005
Camptotheca acuminata (Q5XLF2), Camptotheca acuminata (Q5XLF3), Camptotheca acuminata
brenda
Matsuda, F.; Yamada, T.; Miyazawa, H.; Miyagawa, H.; Wakasa, K.
Characterization of tryptophan-overproducing potato transgenic for a mutant rice anthranilate synthase alpha-subunit gene (OASA1D)
Planta
222
535-545
2005
Oryza sativa
brenda
Tutino, M.L.; Tosco, A.; Marino, G.; Sannia, G.
Expression of Sulfolobus solfataricus trpE and trpG genes in E. coli
Biochem. Biophys. Res. Commun.
230
306-310
1997
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
brenda
Ge, S.M.; Xie, B.E.; Chen, S.F.
Characterization of two trpE genes encoding anthranilate synthase alpha-subunit in Azospirillum brasilense
Biochem. Biophys. Res. Commun.
341
494-499
2006
Azospirillum brasilense, Azospirillum brasilense Yu62
brenda
Peebles, C.A.; Hong, S.; Gibson, S.I.; Shanks, J.V.; San, K.
Effects of terpenoid precursor feeding on Catharanthus roseus hairy roots over-expressing the alpha or the alpha and beta subunits of anthranilate synthase
Biotechnol. Bioeng.
93
534-540
2006
Catharanthus roseus
brenda
Browne, B.A.; Ramos, A.I.; Downs, D.M.
PurF-independent phosphoribosyl amine formation in yjgF mutants of Salmonella enterica utilizes the tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase
J. Bacteriol.
188
6786-6792
2006
Salmonella enterica
brenda
Farrow, J.M.; Pesci, E.C.
Two distinct pathways supply anthranilate as a precursor of the Pseudomonas quinolone signal
J. Bacteriol.
189
3425-3433
2007
Pseudomonas aeruginosa
brenda
Dubouzet, J.G.; Ishihara, A.; Matsuda, F.; Miyagawa, H.; Iwata, H.; Wakasa, K.
Integrated metabolomic and transcriptomic analyses of high-tryptophan rice expressing a mutant anthranilate synthase alpha subunit
J. Exp. Bot.
58
3309-3321
2007
Oryza sativa
brenda
Schuhegger, R.; Rauhut, T.; Glawischnig, E.
Regulatory variability of camalexin biosynthesis
J. Plant Physiol.
164
636-644
2007
Arabidopsis thaliana
brenda
Ishihara, A.; Asada, Y.; Takahashi, Y.; Yabe, N.; Komeda, Y.; Nishioka, T.; Miyagawa, H.; Wakasa, K.
Metabolic changes in Arabidopsis thaliana expressing the feedback-resistant anthranilate synthase alpha subunit gene OASA1D
Phytochemistry
67
2349-2362
2006
Oryza sativa
brenda
Inaba, Y.; Brotherton, J.E.; Ulanov, A.; Widholm, J.M.
Expression of a feedback insensitive anthranilate synthase gene from tobacco increases free tryptophan in soybean plants
Plant Cell Rep.
26
1763-1771
2007
Nicotiana tabacum
brenda
Barone, P.; Widholm, J.M.
Use of 4-methylindole or 7-methyl-DL-tryptophan in a transformant selection system based on the feedback-insensitive anthranilate synthase alpha-subunit of tobacco (ASA2)
Plant Cell Rep.
27
509-517
2008
Nicotiana tabacum
brenda
Hanafy, M.S.; Rahman, S.M.; Khalafalla, M.M.; El-Shemy, H.A.; Nakamoto, Y.; Ishimoto, M.; Wakasa, K.
Accumulation of free tryptophan in azuki bean (Vigna angularis) induced by expression of a gene (OASA1D) for a modified ?-subunit of rice anthranilate synthase
Plant Sci.
171
670-676
2006
Oryza sativa
brenda
Peebles, C.A.; Sander, G.W.; Li, M.; Shanks, J.V.; San, K.Y.
Five year maintenance of the inducible expression of anthranilate synthase in Catharanthus roseus hairy roots
Biotechnol. Bioeng.
102
1521-1525
2008
Catharanthus roseus (Q9AW95), Catharanthus roseus
brenda
Carminatti, C.A.; Oliveira, I.L.; Recouvreux, D.O.; Antonio, R.V.; Porto, L.M.
Anthranilate synthase subunit organization in Chromobacterium violaceum
Genet. Mol. Res.
7
830-838
2008
Chromobacterium violaceum (Q7P0J9), Chromobacterium violaceum
brenda
Huang, C.Y.; Lee, C.Y.; Wu, H.C.; Kuo, M.H.; Lai, C.Y.
Interactions of chaperonin with a weakly active anthranilate synthase from the aphid endosymbiont Buchnera aphidicola
Microb. Ecol.
56
696-703
2008
Buchnera aphidicola
brenda
Lin, X.; Xu, S.; Yang, Y.; Wu, J.; Wang, H.; Shen, H.; Wang, H.
Purification and characterization of anthranilate synthase component I (TrpE) from Mycobacterium tuberculosis H37Rv
Protein Expr. Purif.
64
8-15
2009
Mycobacterium tuberculosis (P9WFX3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WFX3), Mycobacterium tuberculosis H37Rv
brenda
Ziebart, K.T.; Toney, M.D.
Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase
Biochemistry
49
2851-2859
2010
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Barone, P.; Zhang, X.H.; Widholm, J.M.
Tobacco plastid transformation using the feedback-insensitive anthranilate synthase [alpha]-subunit of tobacco (ASA2) as a new selectable marker
J. Exp. Bot.
60
3195-3202
2009
Nicotiana tabacum
brenda
Balderas-Hernandez, V.E.; Sabido-Ramos, A.; Silva, P.; Cabrera-Valladares, N.; Hernandez-Chavez, G.; Baez-Viveros, J.L.; Martinez, A.; Bolivar, F.; Gosset, G.
Metabolic engineering for improving anthranilate synthesis from glucose in Escherichia coli
Microb. Cell Fact.
8
19
2009
Escherichia coli, Escherichia coli W3110 trpD9923
brenda
Hu, P.; Meng, Y.; Wise, R.P.
Functional contribution of chorismate synthase, anthranilate synthase, and chorismate mutase to penetration resistance in barley-powdery mildew interactions
Mol. Plant Microbe Interact.
22
311-320
2009
Hordeum vulgare subsp. vulgare (B5AAU2)
brenda
Ziebart, K.T.; Dixon, S.M.; Avila, B.; El-Badri, M.H.; Guggenheim, K.G.; Kurth, M.J.; Toney, M.D.
Targeting multiple chorismate-utilizing enzymes with a single inhibitor: validation of a three-stage design
J. Med. Chem.
53
3718-3729
2010
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Peebles, C.A.; Sander, G.W.; Hughes, E.H.; Peacock, R.; Shanks, J.V.; San, K.Y.
The expression of 1-deoxy-d-xylulose synthase and geraniol-10-hydroxylase or anthranilate synthase increases terpenoid indole alkaloid accumulation in Catharanthus roseus hairy roots
Metab. Eng.
13
234-240
2010
Arabidopsis thaliana
brenda
Sun, J.; Chen, Q.; Qi, L.; Jiang, H.; Li, S.; Xu, Y.; Liu, F.; Zhou, W.; Pan, J.; Li, X.; Palme, K.; Li, C.
Jasmonate modulates endocytosis and plasma membrane accumulation of the Arabidopsis PIN2 protein
New Phytol.
191
360-375
2011
Arabidopsis thaliana
brenda
Payne, R.J.; Bulloch, E.M.; Kerbarh, O.; Abell, C.
Inhibition of chorismate-utilising enzymes by 2-amino-4-carboxypyridine and 4-carboxypyridone and 5-carboxypyridone analogues
Org. Biomol. Chem.
8
3534-3542
2010
Serratia marcescens
brenda
List, F.; Bocola, M.; Haeger, M.C.; Sterner, R.
Constitutively active glutaminase variants provide insights into the activation mechanism of anthranilate synthase
Biochemistry
51
2812-2818
2012
Thermotoga maritima
brenda
Man, H.; Pollmann, S.; Weiler, E.W.; Kirby, E.G.
Increased glutamine in leaves of poplar transgenic with pine GS1a caused greater anthranilate synthetase alpha-subunit (ASA1) transcript and protein abundances: an auxin-related mechanism for enhanced growth in GS transgenics?
J. Exp. Bot.
62
4423-4431
2011
Nicotiana tabacum, Populus tremula x Populus alba
brenda
Zhao, Z.J.; Zou, C.; Zhu, Y.X.; Dai, J.; Chen, S.; Wu, D.; Wu, J.; Chen, J.
Development of L-tryptophan production strains by defined genetic modification in Escherichia coli
J. Ind. Microbiol. Biotechnol.
38
1921-1929
2011
Escherichia coli, Escherichia coli W3110 / ATCC 27325
brenda
Palmer, G.C.; Jorth, P.A.; Whiteley, M.
The role of two Pseudomonas aeruginosa anthranilate synthases in tryptophan and quorum signal production
Microbiology
159
959-969
2013
Pseudomonas aeruginosa (P09785 and P09786), Pseudomonas aeruginosa (P20576 and P20580), Pseudomonas aeruginosa
brenda
Dubouzet, J.G.; Matsuda, F.; Ishihara, A.; Miyagawa, H.; Wakasa, K.
Production of indole alkaloids by metabolic engineering of the tryptophan pathway in rice
Plant Biotechnol. J.
11
1103-1111
2013
Oryza sativa, Oryza sativa Nipponbare
brenda
Bashiri, G.; Johnston, J.M.; Evans, G.L.; Bulloch, E.M.; Goldstone, D.C.; Jirgis, E.N.; Kleinboelting, S.; Castell, A.; Ramsay, R.J.; Manos-Turvey, A.; Payne, R.J.; Lott, J.S.; Baker, E.N.
Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex
Acta Crystallogr. Sect. D
71
2297-2308
2015
Mycobacterium tuberculosis (P9WFX2), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (P9WFX2)
brenda
Plach, M.G.; Loeffler, P.; Merkl, R.; Sterner, R.
Conversion of anthranilate synthase into isochorismate synthase implications for the evolution of chorismate-utilizing enzymes
Angew. Chem. Int. Ed. Engl.
54
11270-11274
2015
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Sun, J.; Ma, L.; San, K.Y.; Peebles, C.A.
Still stable after 11 years A Catharanthus roseus hairy root line maintains inducible expression of anthranilate synthase
Biotechnol. Prog.
33
66-69
2017
Arabidopsis thaliana
brenda
Sun, J.; Manmathan, H.; Sun, C.; Peebles, C.A.
Examining the transcriptional response of overexpressing anthranilate synthase in the hairy roots of an important medicinal plant Catharanthus roseus by RNA-seq
BMC Plant Biol.
16
108
2016
Arabidopsis thaliana
brenda
Fattorini, L.; Veloccia, A.; Della Rovere, F.; DAngeli, S.; Falasca, G.; Altamura, M.M.
Indole-3-butyric acid promotes adventitious rooting in Arabidopsis thaliana thin cell layers by conversion into indole-3-acetic acid and stimulation of anthranilate synthase activity
BMC Plant Biol.
17
121
2017
Arabidopsis thaliana
brenda
Svarcova, M.; Kratky, M.; Vinsova, J.
Investigation of potential inhibitors of chorismate-utilizing enzymes
Curr. Med. Chem.
22
1383-1399
2015
Serratia marcescens
brenda
Kuepper, J.; Dickler, J.; Biggel, M.; Behnken, S.; Jaeger, G.; Wierckx, N.; Blank, L.M.
Metabolic engineering of Pseudomonas putida KT2440 to produce anthranilate from glucose
Front. Microbiol.
6
1310
2015
Escherichia coli
brenda
Zhang, X.; Brotherton, J.; Widholm, J.
Co-expression of the tobacco anthranilate synthase beta subunit with its feedback-insensitive alpha subunit as a selectable marker that also markedly increases the free tryptophan content
In Vitro Cell. Dev. Biol. Plant
51
564-570
2015
Nicotiana tabacum
-
brenda
Srivastava, A.; Sinha, S.
Uncoupling of an ammonia channel as a mechanism of allosteric inhibition in anthranilate synthase of Serratia marcescens dynamic and graph theoretical analysis
Mol. Biosyst.
13
142-155
2017
Serratia marcescens
brenda
Ashenafi, M.; Reddy, P.T.; Parsons, J.F.; Byrnes, W.M.
The fused anthranilate synthase from Streptomyces venezuelae functions as a monomer
Mol. Cell. Biochem.
400
9-15
2015
Streptomyces venezuelae
brenda
Singh, B.; Sahu, P.M.; Sharma, R.A.
Effect of elicitors on the production of pyrroloquinazoline alkaloids by stimulating anthranilate synthase activity in Adhatoda vasica Nees cell cultures
Planta
246
1125-1137
2017
Justicia adhatoda
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.1.3.27)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
