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chorismate + ammonia
anthranilate + pyruvate + H2O
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
chorismate + NH3
anthranilate + pyruvate + H2O
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
NH3 + phosphoribosyl diphosphate
phosphoribosyl amine
-
mutant P362L
-
?
additional information
?
-
chorismate + ammonia
anthranilate + pyruvate + H2O
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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-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
-
-
-
?
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
-
-
-
-
?
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+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
10% of the activity with Gln
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
-
-
-
?
chorismate + NH4+
?
-
anthranilate synthase I
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
feedback-insensitive enzyme
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
alpha-subunits (OASA1 or OASA2) alone possess anthranilate synthase activity with NH4+
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
-
-
-
-
?
additional information
?
-
-
Trp biosynthetic enzyme
-
-
?
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of avenanthramides
-
?
additional information
?
-
-
first enzyme in the branch pathway in Trp biosynthesis
-
-
?
additional information
?
-
-
enzyme of the shikimic acid pathway
-
-
?
additional information
?
-
-
active site residue that forms the covalent gamma-glutamyl-AS II intermediate is Cys
-
-
?
additional information
?
-
-
initial steps in glutamine utilization
-
-
?
additional information
?
-
-
subunit ASalpha requires an ASbeta-subunit for Gln-dependent activity
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
-
glutaminase 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
-
?
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(1R,4R,5S,6S)-4-[(1-carboxyethenyl)oxy]-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-ene-2-carboxylic acid
-
-
(3-carbamoylphenoxy)acetic 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)-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylic acid
-
-
(3R,4R)-3-azido-4-hydroxycyclohexa-1,5-diene-1-carboxylic 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
-
-
(3S)-3-[(1-carboxyethenyl)oxy]cyclohepta-1,6-diene-1-carboxylic acid
-
-
(4R,5R)-5-(carboxymethoxy)-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
-
-
(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-(1-carboxyethyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
-
1-(1-carboxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
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-(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
-
-
1-(carboxymethyl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
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-amino-3-(1-carboxyethoxy)benzoic acid
-
-
2-oxoglutarate
-
reaction of component I with NH4+ as substrate
2-[(1-carboxyethyl)amino]pyridine-4-carboxylic acid
-
-
2-[(carboxymethyl)amino]pyridine-4-carboxylic acid
-
-
2-[[(1R,6R)-3-bromo-6-hydroxycyclohexa-2,4-dien-1-yl]oxy]prop-2-enoic acid
-
-
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)-2-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-2-nitrobenzoic acid
-
-
3-(1-carboxyethoxy)-4,5-dihydroxybenzoate
-
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-(hydroxymethyl)benzoic acid
-
-
3-(1-carboxyethoxy)-4-(sulfanylmethyl)benzoic acid
-
-
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methylbenzoic acid
-
-
3-(1-carboxyethoxy)benzoic acid
-
-
3-(carboxymethoxy)benzoic acid
-
-
3-[(1-carboxyethenyl)oxy]-4,5-dihydroxybenzoic acid
-
-
3-[(1-carboxylatoethenyl)oxy]-2-hydroxybenzoate
-
3-[(1-carboxylatoethenyl)oxy]benzoate
-
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoate
-
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic 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
-
4-(azidomethyl)-3-(1-carboxyethoxy)benzoic acid
-
-
4-amino-3-(1-carboxyethoxy)benzoic acid
-
-
4-amino-3-[(1-carboxyethyl)amino]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
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
alpha-Methyltryptophan
-
-
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
DL-4-methyltryptophan
-
-
DL-5-hydroxytryptophan
-
-
DL-6-Fluorotryptophan
-
-
elymoclavine
-
i.e. (6-methyl-8,9-didehydroergolin-8yl)methanol
Gln
-
reaction of component I with NH4+ as substrate
Glu
-
reaction of component I with NH4+ as substrate
L-2-Amino-4-oxo-5-chloropentanoic acid
-
irreversible, Gln protects
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
-
-
[4-carboxy-2-(1-carboxyethoxy)phenyl]methanaminium
-
-
5-Methyltryptophan
-
less effective inhibitor than 4-methylindole or 7-methyl-DL-tryptophan
5-Methyltryptophan
-
79% inhibition at 0.05 mM
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
anthranilate
-
i.e. ortho-aminobenzoate
Ba2+
-
-
Cu2+
-
-
DL-5-fluorotryptophan
-
-
DL-5-fluorotryptophan
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
DL-5-Methyltryptophan
-
0.0054 mM, 50% inhibition
DL-5-Methyltryptophan
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
DL-5-Methyltryptophan
-
no activity in the presence of 0.05 mM
Hg2+
-
0.005 mM HgCl2, complete inhibition
Hg2+
-
1 mM HgCl2, 94.1% inhibition
iodoacetamide
-
-
iodoacetamide
-
irreversible, Gln protects
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
-
competitive with respect to chorismate
L-Trp
-
noncompetitive with respect to L-Gln, inhibitory effect increases with rising pH
L-Trp
-
0.0033 mM, 50% inhibition
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
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 respect to chorismate
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
L-Trp
-
feedback inhibition
L-tryptophan
-
strong, 50% inhibition at 0.005 mM
L-tryptophan
-
slightly inhibited
L-tryptophan
-
feedback inhibition, 50% inhibition at 0.004-0.03 mM
L-tryptophan
-
no activity in the presence of 0.05 mM
L-tryptophan
-
75.8% inhibition at 0.05 mM
Pb2+
-
-
PCMB
-
0.005 mM, complete inhibition
PCMB
-
1 mM, 88.6% inhibition
PCMB
-
reaction of component I with NH4+ as substrate
tryptophan
allosteric inhibition
tryptophan
-
complete inhibition at 0.02 mM
tryptophan
-
the enzyme is competitively but non-cooperatively inhibited by tryptophan
Zn2+
-
1 mM, 75% inhibition
additional information
-
not inhibitory: D-tryptophan
-
additional information
-
subunit ASA2 is insensitive to tryptophan feedback inhibition
-
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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
0.03
(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
0.0036
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
0.0019
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
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
0.05
2-(1-carboxy-ethylamino)-isonicotinate
-
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
0.094
2-(carboxymethyl-amino)-isonicotinate
-
pH 7.0, 25°C
0.024
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
pH 7.0, 25°C
0.021
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
pH 7.0, 25°C
0.026
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
pH 7.0, 25°C
0.028
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.0029 - 0.03
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
0.025
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
pH 7.0, 25°C
0.21 - 0.55
3-(carboxymethoxy)benzoic acid
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
0.043
4-amino-3-(1-carboxyethoxy)benzoic acid
-
pH 7.0, 25°C
0.023
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
pH 7.0, 25°C
0.021
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
0.0054
DL-5-Methyltryptophan
-
-
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, 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
0.0111
tryptophan
-
at pH 7.5 and 30°C
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
0.0029
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
pH 7.0, 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
0.00028
L-Trp
-
pH 8.0, 60°C, without glycerol and KCl
0.00031
L-Trp
-
pH 8.0, 60°C, with 25% glycerol and 2 M KCl
0.0053
L-Trp
-
reconstituted enzyme OASA2-OASB1, cosubstrate: L-Gln
0.0397
L-Trp
-
reconstituted enzyme OASA1-OASB1, cosubstrate: L-Gln
0.135
L-Trp
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: L-Gln
0.004
L-tryptophan
-
at 60°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
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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
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
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
-
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
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Mycobacterium tuberculosis (P9WFX2), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (P9WFX2)
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Plach, M.G.; Loeffler, P.; Merkl, R.; Sterner, R.
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Salmonella enterica subsp. enterica serovar Typhimurium
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Arabidopsis thaliana
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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
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Arabidopsis thaliana
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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
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Arabidopsis thaliana
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Svarcova, M.; Kratky, M.; Vinsova, J.
Investigation of potential inhibitors of chorismate-utilizing enzymes
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Serratia marcescens
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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.
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Escherichia coli
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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
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Nicotiana tabacum
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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
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Serratia marcescens
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Ashenafi, M.; Reddy, P.T.; Parsons, J.F.; Byrnes, W.M.
The fused anthranilate synthase from Streptomyces venezuelae functions as a monomer
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Streptomyces venezuelae
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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
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Justicia adhatoda
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