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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
chorismate + ammonia
anthranilate + pyruvate + H2O
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
chorismate + NH4+
anthranilate + pyruvate + H2O
-
feedback-insensitive enzyme
-
-
?
additional information
?
-
chorismate + ammonia

anthranilate + pyruvate + H2O
-
-
-
?
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
-
-
-
-
?
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

?
-
-
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
?
-
-
initial steps in glutamine utilization
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00084 - 3.6
L-glutamine
additional information
additional information
-
0.0012
chorismate

-
-
0.003
chorismate
-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60°C
0.0034
chorismate
75°C, glutamine-dependent activity
0.0037
chorismate
-
pH 7.0, 25°C
0.0039
chorismate
-
saturating Mg2+, pH 7.0, 25°C
0.00571
chorismate
-
alpha-subunit OASA1, cosubstrate: NH4+
0.00624
chorismate
-
alpha-subunit OASA1D (N323D), cosubstrate: NH4+
0.007
chorismate
-
enzyme component ASI, with Gln as cosubstrate
0.0082
chorismate
-
at pH 7.5 and 30°C
0.009
chorismate
-
anthranilate formation
0.0123
chorismate
-
pH 8.0, 60°C, without glycerol and KCl
0.0138
chorismate
75°C, ammonia-dependent activity
0.015
chorismate
-
with NH4+ as cosubstrate
0.015
chorismate
at pH 8.0 and 25°C
0.018
chorismate
-
with Gln as cosubstrate
0.023
chorismate
-
Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2)
0.025
chorismate
-
chorismate-dependent glutaminase activity
0.026
chorismate
-
wild-type enzyme
0.038
chorismate
-
at pH 9 and 37°C, wild-type enzyme
0.039
chorismate
-
pH 8.3, 32°C, A369L/L530D mutant anthranilate synthase alpha-subunit OASA2
0.042
chorismate
-
mutant enzyme R429H
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
0.046
chorismate
-
mutant enzyme
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
0.0634
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: NH4+
0.0703
chorismate
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: NH4+
0.073
chorismate
-
isoenzyme As-b
0.076
chorismate
-
pH 8.3, 32°C, Y367A mutant anthranilate synthase alpha-subunit OASA2
0.0828
chorismate
-
alpha-subunit OASA2, cosubstrate: NH4+
0.084
chorismate
-
pH 8.0, 60°C, with 25% glycerol and 2 M KCl
0.09
chorismate
-
two-component enzyme, ASI,ASII, with ammonium as cosubstrate
0.109
chorismate
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: L-Gln
0.11
chorismate
-
reaction of component I, with NH4+ as cosubstrate
0.121
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: L-Gln
0.14
chorismate
-
mutant enzyme R358H and R416H
0.15
chorismate
-
mutant enzyme R321H
0.178
chorismate
-
reconstituted enzyme OASA2-OASB1, cosubstrate: L-Gln
0.22
chorismate
-
cell line R-20
0.239
chorismate
-
reconstituted enzyme OASA2-OASB1, cosubstrate: NH4+
0.28
chorismate
-
cell line R-15
3.1
chorismate
-
NH4+-dependent enzyme, component I
0.05
Gln

-
isoenzyme As-b
0.094
Gln
-
Gln-dependent enzyme that is composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2)
0.18
Gln
-
cell line R-15
0.25
Gln
-
cell line R-20
1.4
Gln
-
anthranilate formation
5.6
Gln
-
chorismate-dependent glutaminase activity
0.0193
L-Gln

-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60°C
0.237
L-Gln
-
mutant enzyme
0.249
L-Gln
-
wild-type enzyme
6.2
L-Gln
-
pH 8.0, 60°C, without glycerol and KCl
7
L-Gln
-
pH 8.0, 60°C, with 25% glycerol and 2 M KCl
0.00084
L-glutamine

-
at pH 7.5 and 30°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
1.2
NH4+
-
NH4+-dependent enzyme, component I
5.7
NH4+
-
pH 8.0, 60°C, without glycerol and KCl
7.3
NH4+
-
pH 8.0, 60°C, with 25% glycerol and 2 M KCl
24
NH4+
-
reaction of component I
26
NH4+
-
two-component enzyme, ASI,ASII
46
NH4+
-
at pH 9 and 37°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.
0.25
L-Gln
-
pH 8.0, 60°C, with or without 2 M KCl and 25% glycerol
0.0061
chorismate

-
alpha-subunit OASA2, cosubstrate: NH4+
0.0124
chorismate
-
alpha-subunit OASA1D (N323D, cosubstrate: NH4+)
0.0185
chorismate
-
alpha-subunit OASA1, cosubstrate: NH4+
0.079
chorismate
-
reconstituted enzyme OASA2-OASB1, cosubstrate: NH4+
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
0.228
chorismate
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: NH4+
0.24
chorismate
-
reconstituted enzyme OASA2-OASB1, cosubstrate: L-Gln
0.25
chorismate
-
pH 8.0, 60°C, with or without 2 M KCl and 25% glycerol
0.26
chorismate
at pH 8.0 and 25°C
0.27
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: NH4+
0.405
chorismate
-
pH 8.3, 32°C, A369L/L530D mutant anthranilate synthase alpha-subunit OASA2
0.48
chorismate
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: L-Gln
0.49
chorismate
-
pH 8.3, 32°C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2
0.57
chorismate
-
at pH 7.5 and 30°C
0.573
chorismate
-
pH 8.3, 32°C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
0.58
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: L-Gln
5.6
chorismate
-
pH 7.0, 25°C
6.08
chorismate
-
pH 8.3, 32°C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
383
chorismate
-
at pH 9 and 37°C, with NH4+ as cosubstrate
0.57
L-glutamine

-
at pH 7.5 and 30°C
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.
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
-
inhibitior 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

-
inhibitior 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
-
inhibitior 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
-
inhibitior 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
-
inhibitior 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
-
inhibitior 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
-
inhibitior 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
-
inhibitior binding to the enzyme-chorismate complex, pH 7.8, 25°C
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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
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brenda
two isoenzymes: AS-a and AS-b
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brenda
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brenda
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brenda
L. cv. Shokan 1, induction with oligo-N-acetylchitooligosaccharide elicitors
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brenda
-
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brenda
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-
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brenda
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-
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brenda
-
-
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brenda
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SwissProt
brenda
strain Pepty 695 and strain M5/95F
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brenda
-
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brenda
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-
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brenda
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-
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brenda
H 16
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brenda
H 16
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brenda
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-
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brenda
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brenda
gene trpED
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brenda
W3110 trpD9923
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brenda
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-
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brenda
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-
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brenda
-
UniProt
brenda
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brenda
-
-
-
brenda
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UniProt
brenda
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UniProt
brenda
ASA2 expressed in Astralagus sinicus
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brenda
-
-
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brenda
hybrid, clone INRA 7171-B4
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brenda
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-
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brenda
-
-
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brenda
Q06128: subunit TrpE, Q06129: subunit TrpG
UniProt
brenda
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-
brenda
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-
brenda
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-
brenda
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-
-
brenda
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brenda
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brenda
independent expression of subunits in Escherichia coli
UniProt
brenda
genes trpE, trpGD, and trpG
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brenda
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brenda
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brenda
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brenda
ecotype Col-0
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brenda
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UniProt
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line ASA-1
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brenda
line ASAB-1
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brenda
monofunctional enzyme
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brenda
-
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brenda
probable anthranilate synthase ORF CV0568
UniProt
brenda
-
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-
brenda
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
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brenda
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brenda
gene trpED
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brenda
strain with a mutant anthranilate synthase Pro21Gln that is insensitive to feedback inhibition by Trp
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brenda
W3110 trpD9923
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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
multifunctional enzyme complex of anthranilate synthetase with phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
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brenda
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brenda
cultivar Xanthi
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brenda
cv. Xanthi
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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
-
-
-
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)
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brenda
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brenda
cv. Nipponbare
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brenda
var. Donganbyeo, and mutant lines resistant to growth inhition by 5-methyltryptophan
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brenda
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-
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
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brenda
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a high rutacridone producing cell line R-20 and low rutacrinone producing cell line R-15
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brenda
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brenda
Q06128: subunit TrpE, Q06129: subunit TrpG
UniProt
brenda
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brenda
serovar Typhimurium strain LT2
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brenda
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brenda
expression in Escherichia coli
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brenda
multifunctional anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
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-
brenda
multifunctional enzyme anthranilate synthase/N(5'-phosphoribosyl)anthranilate synthase (ec 4.1.3.27/ec 2.4.2.18, or ASI/ASII)
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
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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
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
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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
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126000
-
sucrose density gradient centrifugation
139300
-
deduced from amino acid sequence
14000
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
140000
-
sucrose density gradient centrifugation
141000
-
sucrose density gradient centrifugation
16000
-
1 * 16000 + 1 * 80000
20000
-
2 * 20000 + 2 * 50000, Gln-dependent enzyme, composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, I2II2, gel filtration
20956
-
2 * 20956 + 2 * 60000
21000
-
ASI, ASII, 2 * 21000 + 2 * 60000, SDS-PAGE
21050
calculated, beta, PabA subunit
21100
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
21913
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
23000
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
25500
-
2 * 25500 + 2 * 67000, SDS-PAGE
28000
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
37000
-
1 * 37000 + 1 * 60000, isoenzyme AS-b, SDS-PAGE
400000
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, gel filtration
47743
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
47930
calculated, probable anthranilate synthase ORF CV0568
48500
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
54020
calculated, alpha, TrpE subunit
57000
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
62300
recombinant fusion protein, determined by SDS-PAGE
62350
determined by mass spectrometry
63400
-
1 * 18000 + 1 * 63400, sucrose density gradient centrifugation
64000
-
1 * 18000 + 1 * 64000
64512
x * 64512, calculation from nucleotide sequence
65013
x * 65013, calculation from nucleotide sequence
67000
-
2 * 25500 + 2 * 67000, SDS-PAGE
72000
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
76000
-
2 * 76000 + 2 * 84000, alpha2,beta2, SDS-PAGE
79000
-
1 * 79000, SDS-PAGE
84000
-
2 * 76000 + 2 * 84000, alpha2,beta2, SDS-PAGE
86000
-
gel filtration or sucrose density gradient centrifugation in presence of 30% glycerol
94000
-
alpha2,beta2, 2 * 70000 + 2 * 94000, SDS-PAGE
94000 - 117000
-
gel filtration
150000

-
-
150000
-
Trp-sensitive form, gel filtration
160000

-
-
160000
-
Gln-dependent enzyme composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2), gel filtration
18000

-
1 * 18000 + 1 * 64000
18000
-
1 * 18000 + 1 * 63400, sucrose density gradient centrifugation
18000
-
2 * 18000 + 2 * 71000
18000
-
2 * 18000 + 2 * 71000
18000
-
alpha2beta2, 2 * 18000 + 2 * 50000, SDS-PAGE
200000

-
Trp-resistant enzyme form, gel filtration
200000
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, sucrose density gradient centrifugation
50000

-
NH4-dependent enzyme, i.e. component I, gel filtration
50000
-
alpha2beta2, 2 * 18000 + 2 * 50000, SDS-PAGE
60000

gel filtration
60000
-
1 * 37000 + 1 * 60000, isoenzyme AS-b, SDS-PAGE
60000
-
ASI, ASII, 2 * 21000 + 2 * 60000, SDS-PAGE
60000
-
2 * 20956 + 2 * 60000
70000

-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
70000
-
alpha2,beta2, 2 * 70000 + 2 * 94000, SDS-PAGE
71000

-
2 * 18000 + 2 * 71000
71000
-
2 * 18000 + 2 * 71000
80000

-
gel filtration
80000
-
1 * 16000 + 1 * 80000
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
additional information
-
experimental value between 84 and 95 kDa
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?

x * 64512, calculation from nucleotide sequence
?
x * 65013, calculation from nucleotide sequence
?
-
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
dimer
-
1 * 37000 + 1 * 60000, isoenzyme AS-b, SDS-PAGE
dimer
-
1 * 16000 + 1 * 80000
dimer
-
1 * 18000 + 1 * 64000
dimer
-
1 * 18000 + 1 * 63400, sucrose density gradient centrifugation
dimer
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
dimer
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
heterodimer

alpha, TrpE, and beta, PabA, subunit
heterodimer
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
heterotetramer

-
2 * ? + 2 * 32000, SDS-PAGE
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
monomer

-
crystallographic data
monomer
-
1 * 79000, SDS-PAGE
monomer
-
1 * 79000, SDS-PAGE
monomer
-
1 * 67000, SDS-PAGE
monomer
-
1 * 66600, laser light scattering
tetramer

-
alpha2beta2, 2 * 18000 + 2 * 50000, SDS-PAGE
tetramer
-
2 * 25500 + 2 * 67000, SDS-PAGE
tetramer
-
2 * 18000 + 2 * 71000
tetramer
-
2 * 18000 + 2 * 71000
tetramer
-
alpha2,beta2, 2 * 70000 + 2 * 94000, SDS-PAGE
tetramer
-
2 * 76000 + 2 * 84000, alpha2,beta2, SDS-PAGE
tetramer
-
2 * 20000 + 2 * 50000, Gln-dependent enzyme, composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, I2II2, gel filtration
tetramer
-
ASI, ASII, 2 * 21000 + 2 * 60000, SDS-PAGE
tetramer
-
2 * 20956 + 2 * 60000
tetramer
-
2 * 20956 + 2 * 60000
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
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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
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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
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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
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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
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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
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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
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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
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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
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Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R358H
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Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R429H
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similar Km value to the wild-type enzyme and a slightly larger turnover number
R452H
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less than 0.05% of the activity of the wild-type enzyme
additional information

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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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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alpha subunit (with a point mutation to confer feedback resistance to tryptophan) expressed in hairy root of Catharanthus roseus
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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
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cloning of the genes phnA and phnB of the anthranilate synthase that participates in the synthesis of pyocyanin
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expressed in a Catharanthus roseus hairy root line
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expressed in Arabidopsis thaliana
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expressed in Catharanthus roseus hairy roots
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain JM109
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expressed in Glycine max
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expressed in Pseudomonas putida strain KT2440
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expressed in Vigna angularis
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expression in Escherichia coli
expression in Nicotiana tabacum
expression in Saccharomyces cerevisiae
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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
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expression of OASA1D/N323 in Solanum tuberosum induces a 2fold to 20fold increase in the amount of Trp
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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
His-tagged veresion expressed in Escherichia coli C41(DE3)
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into the BSMVm:gamma vector, the UbiNos_2-3 vector is used to express HvASa2. Into the hairpin vector pIPKTA30, hairpin construct co-bombarded with a Ubi:GUS expression vector into barley epidermal cells
into the pGEM-T Easy vector for expression in Escherichia coli cells
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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
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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
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mutant anthanilate synthase Pro21Ser that is insensitive to feedback inhibition by Trp
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partial complex anthranilate synthase expressed in Escherichia coli CB694
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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
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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
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wild-type and mutant overexpressed in Escherichia coli cells (strain CB694) harboring the pSTC25 plasmid
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expressed in Escherichia coli BL21(DE3) cells

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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
