Information on EC 4.1.3.27 - anthranilate synthase

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

EC NUMBER
COMMENTARY
4.1.3.27
-
RECOMMENDED NAME
GeneOntology No.
anthranilate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
sequential mechanism
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
sequential mechanism
Hansenula henricii
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
trans-6-amino-5-[(2-carboxyethenyl)-oxy]-1,3-cyclohexadiene-1-carboxylic acid is an enzyme-bound inhibitor
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
kinetics
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
thermodynamics
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
mechanism
-
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
mechanism
P00897 and P00500
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
Q9AW95
-
elimination
-, Q7P0J9
-
elimination
-
-
elimination
-, P67001
-
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
2-heptyl-3-hydroxy-4(1H)-quinolone biosynthesis
-
4-hydroxy-2(1H)-quinolone biosynthesis
-
acridone alkaloid biosynthesis
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
tryptophan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
anthranilate synthase
-
-
-
-
anthranilate synthase
-
-
anthranilate synthase
B5AAU2
-
anthranilate synthase
-
-
anthranilate synthase
Q9AW95
-
anthranilate synthase
Q7P0J9
-
anthranilate synthase
-
-
anthranilate synthase
Escherichia coli W3110 trpD9923
-
-
-
anthranilate synthase
-
-
anthranilate synthase
-
-
anthranilate synthase a1
-
-
anthranilate synthase alpha 1
Q5XLF3
-
anthranilate synthase alpha 2
Q5XLF2
-
anthranilate synthase alpha2
-
-
anthranilate synthase component I
P67001
-
anthranilate synthase-phosphoribosyltransferase
-
tryptophan biosynthetic enzyme complex
anthranilate synthetase
-
-
-
-
ASA1
-
major isoform of anthranilate synthase
ASA2
-
anthranilate synthase alpha-subunit
ASA2
-
feedback-insensitive enzyme
ASalpha
-
subunit
ASalpha
-
-
ASalphabeta
-
subunit
ASalphabeta-1
Q9AW95
-
CaASA1
Q5XLF3
anthranilate synthase alpha-subunit
CaASA2
Q5XLF2
anthranilate alpha-subunit
chorismate lyase
-
-
-
-
Glutamine amido-transferase
-
-
-
-
Glutamine amidotransferase
-
-
-
-
OASA1
-
alpha-subunit of anthranilate synthase
OASA1D
-
anthranilate synthase alpha subunit
OASA1D
-
feedback-insensitive alpha-subunit OASA1D (OASA1 with point mutation N323D)
OASA1D
-
gene for anthranilate synthase alpha-subunit
OASA2
-
-
OASA2
-
alpha-subunit of anthranilate synthase
OASA2
-
anthranilate synthase alpha-subunit
PhnAB anthranilate synthase
-
-
synthase, anthranilate
-
-
-
-
synthetase, anthranilate
-
-
-
-
TrpED
Escherichia coli W3110 trpD9923
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9031-59-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
wild-type and 2 classes of mutants: one is defective in the chorismate-binding subunit E and is incapable of catalyzing the anthranilate synthetase reaction. The second class is defective in the G subunit but produces an active E subunit, this mutation results in a requirement for p-aminobenzoate in addition to anthranilate
-
-
Manually annotated by BRENDA team
two isoenzymes: AS-a and AS-b
-
-
Manually annotated by BRENDA team
L. cv. Shokan 1, induction with oligo-N-acetylchitooligosaccharide elicitors
-
-
Manually annotated by BRENDA team
Azospirillum brasilense Yu62
strain Yu62
-
-
Manually annotated by BRENDA team
line ASA-1; line ASAB-1
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
probable anthranilate synthase ORF CV0568
UniProt
Manually annotated by BRENDA team
strain Pepty 695 and strain M5/95F
-
-
Manually annotated by BRENDA team
Claviceps sp.
strain SD58
-
-
Manually annotated by BRENDA team
Claviceps sp.
strain SD58; three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
-
-
Manually annotated by BRENDA team
Claviceps sp. SD58
strain SD58
-
-
Manually annotated by BRENDA team
Cupriavidus necator H 16
H 16
-
-
Manually annotated by BRENDA team
strain with a mutant anthranilate synthase Pro21Gln that is insensitive to feedback inhibition by Trp
-
-
Manually annotated by BRENDA team
W3110 trpD9923
-
-
Manually annotated by BRENDA team
Escherichia coli W3110 trpD9923
W3110 trpD9923
-
-
Manually annotated by BRENDA team
strain Z
-
-
Manually annotated by BRENDA team
Euglena gracilis Z
strain Z
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
Hansenula henricii
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)
-
-
Manually annotated by BRENDA team
multifunctional enzyme complex of anthranilate synthetase with phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase
-
-
Manually annotated by BRENDA team
ASA2 expressed in Astralagus sinicus
-
-
Manually annotated by BRENDA team
cultivar Xanthi
-
-
Manually annotated by BRENDA team
cv. Xanthi
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
cv. Nipponbare
-
-
Manually annotated by BRENDA team
var. Donganbyeo, and mutant lines resistant to growth inhition by 5-methyltryptophan
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
a high rutacridone producing cell line R-20 and low rutacrinone producing cell line R-15
-
-
Manually annotated by BRENDA team
serovar Typhimurium strain LT2
-
-
Manually annotated by BRENDA team
multifunctional anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
-
-
Manually annotated by BRENDA team
multifunctional enzyme anthranilate synthase/N(5'-phosphoribosyl)anthranilate synthase (ec 4.1.3.27/ec 2.4.2.18, or ASI/ASII)
-
-
Manually annotated by BRENDA team
-
P00897 and P00500
SwissProt
Manually annotated by BRENDA team
strain HY150
-
-
Manually annotated by BRENDA team
Serratia marcescens HY150
strain HY150
-
-
Manually annotated by BRENDA team
strain 3022a
-
-
Manually annotated by BRENDA team
Streptomyces sp. 3022a
strain 3022a
-
-
Manually annotated by BRENDA team
Sulfolobus solfataricus MT4
strain MT4
-
-
Manually annotated by BRENDA team
independent expression of subunits in Escherichia coli
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
B5AAU2
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
Escherichia coli W3110 trpD9923
-
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
-
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
B5AAU2
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + ammonia
anthranilate + pyruvate + H2O
show the reaction diagram
-, P67001
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Claviceps purpurea, Claviceps sp.
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Claviceps sp.
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Hansenula henricii
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Hansenula henricii
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
component I is inactive with L-Gln
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
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
show the reaction diagram
-
feedback-insensitive enzyme
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Serratia marcescens HY150
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Claviceps sp. SD58
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Claviceps sp. SD58
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Streptomyces sp. 3022a
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Azospirillum brasilense Yu62
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Euglena gracilis Z
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Sulfolobus solfataricus MT4
-
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Cupriavidus necator H 16
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Q9YGB3, -
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Q9AW95
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-, Q7P0J9
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-, P67001
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Escherichia coli W3110 trpD9923
-
-
-
-
?
chorismate + NH3
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
Claviceps sp.
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
Hansenula henricii
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
10% of the activity with Gln
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
anthranilate synthase I
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
?
show the reaction diagram
-
reaction is catalyzed by component I alone and in combination with component II
-
-
?
chorismate + NH4+
?
show the reaction diagram
Serratia marcescens HY150
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
Claviceps sp. SD58
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
Streptomyces sp. 3022a
-
-
-
-
?
chorismate + NH4+
?
show the reaction diagram
Sulfolobus solfataricus MT4
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
feedback-insensitive enzyme
-
-
?
NH3 + phosphoribosyl diphosphate
phosphoribosyl amine
show the reaction diagram
-
mutant P362L
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
alpha-subunits (OASA1 or OASA2) alone possess anthranilate synthase activity with NH4+
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
glutaminase activity
-
-
-
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
?
-
-
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
?
-
-
active site residue that forms the covalent gamma-glutamyl-AS II intermediate is Cys
-
-
-
additional information
?
-
-
subunit ASalpha requires an ASbeta-subunit for Gln-dependent activity
-
-
-
additional information
?
-
Q9YGB3, -
no substrate: asparagine
-
?
additional information
?
-
-
first enzyme in the branch pathway in Trp biosynthesis
-
-
-
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
-
additional information
?
-
-
Trp biosynthetic enzyme
-
-
-
additional information
?
-
-
initial steps in glutamine utilization
-
-
-
additional information
?
-
-
regulation of the gene by attenuation
-
-
-
additional information
?
-
-
enzyme of the shikimic acid pathway
-
-
-
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of avenanthramides
-
?
additional information
?
-
-
does not possess chorismate mutase promiscuous activity
-
-
-
additional information
?
-
Streptomyces sp. 3022a
-
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, synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chorismate + ammonia
anthranilate + pyruvate + H2O
show the reaction diagram
-, P67001
-
-
-
?
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
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
show the reaction diagram
-
feedback-insensitive enzyme
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
Q9AW95
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-, Q7P0J9
-
-
-
?
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
-, P67001
-
-
-
?
chorismate + NH4+
anthranilate + pyruvate + H2O
show the reaction diagram
-
feedback-insensitive enzyme
-
-
?
additional information
?
-
-
first enzyme in the branch pathway in Trp biosynthesis
-
-
-
additional information
?
-
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
-
additional information
?
-
-
Trp biosynthetic enzyme
-
-
-
additional information
?
-
-
initial steps in glutamine utilization
-
-
-
additional information
?
-
-
regulation of the gene by attenuation
-
-
-
additional information
?
-
-
enzyme of the shikimic acid pathway
-
-
-
additional information
?
-
-
rate-limiting enzyme in the biosynthesis of avenanthramides
-
?
additional information
?
-
Streptomyces sp. 3022a
-
synthesis of the enzyme is repressed by His, anthranilate, Trp and p-aminobenzoate
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
can partially replace Mg2+ in activation
Co2+
Claviceps sp.
-
-
Co2+
-
at 1-5 mM
Fe2+
-
1 mM, can partially replace Mg2+ in activation
K+
Claviceps sp.
-
stimulates
Mg2+
-
reaction of component I with NH4+ as substrate; required
Mg2+
-
Km for the mutant enzyme: 0.036 mM, Km for the wild-type enzyme: 0.101 mM; required
Mg2+
-
maximal activity at 0.03 mM; required
Mg2+
Claviceps sp.
-
Km: 0.4 mM; required
Mg2+
Hansenula henricii
-
required
Mg2+
-
Km: 0.18 mM; required
Mg2+
-
Km for MgCl2: 0.26 mM
Mg2+
-
maximal activity at 10 mM; required
Mg2+
Q9YGB3, -
required, Km-value: 0.02 mM
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
Claviceps sp.
-
-
Na+
Claviceps sp.
-
stimulates
NH4+
Claviceps sp.
-
stimulates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(3-[[(5S)-6-([2-[6-(3-amino-3-oxopropyl)dibenzo[b,d]furan-4-yl]ethyl]amino)-5-[[2-(4-nitrophenyl)propanoyl]amino]-6-oxohexyl]carbamoyl]phenoxy)acetic acid
-
-
(4R,5S,6S)-4-amino-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohex-1-enecarboxylate
-
-
(4R,5S,6S)-5-[(1-carboxyethenyl)oxy]-4,6-dihydroxycyclohex-1-enecarboxylate
-
-
(4S,5R,6R)-4-hydroxy-5-[(1-carboxyethenyl)oxy]-6-aminocyclohex-1-enecarboxylic acid
-
-
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
-
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
-
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
-
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
-
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
-
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
-
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
-
2-(1-carboxy-ethylamino)-isonicotinate
-
-
-
2-(3-(-(S)-5-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-4-(3-hydroxy-4-methyl-2-nitrobenzamido)-5-oxopentylcarbamoyl)-phenoxy)acetic acid
-
-
-
2-(3-(3-((R)-3-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-2-(3-hydroxy-4-methyl-2-nitrobenzamido)-3-oxopropylthio) propylcarbamoyl)phenoxy)acetic acid
-
-
-
2-(carboxymethyl-amino)-isonicotinate
-
-
-
2-oxoglutarate
-
reaction of component I with NH4+ as substrate
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
-
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
-
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
-
4-amino-3-(1-carboxyethoxy)benzoic acid
-
-
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
-
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
-
4-methylindole
-
inhibits at 0.3 mM
5-fluoro-DL-tryptophan
-
strong, 50% inhibition at 0.005 mM
5-methyl-DL-tryptophan
-
strong, 50% inhibition at 0.004 mM
5-Methyltryptophan
-
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
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
6-diazo-5-oxo-L-norleucine
-
-
6-fluoro-DL-tryptophan
-
strong, 50% inhibition at 0.009 mM
7-methyl-DL-tryptophan
-
inhibits at 0.3 mM
anthranilate
-
-
Ba2+
Claviceps sp.
-
-
Bromopyruvate
-
inactivation prevented by chorismate and Trp
Ca2+
Claviceps sp.
-
-
Co2+
-
10 mM, 67% inhibition of enzyme from cell line R-15, 33% inhibition of enzyme from cell line R-20
Diethylamine
-
reaction of component I with NH4+ as substrate
Dimethylamine
-
reaction of component I with NH4+ as substrate
DL-4-methyltryptophan
-
-
DL-5-fluorotryptophan
-
-
DL-5-fluorotryptophan
Hansenula henricii
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
DL-5-hydroxytryptophan
-
-
DL-5-Methyltryptophan
-
0.0054 mM, 50% inhibition
DL-5-Methyltryptophan
Hansenula henricii
-
competitive with respect to chorismate, noncompetitive with respect to NH4+ and Gln
DL-5-Methyltryptophan
-
no activity in the presence of 0.05 mM
DL-6-Fluorotryptophan
-
-
elymoclavine
Claviceps sp.
-
i.e. (6-methyl-8,9-didehydroergolin-8yl)methanol
Fe2+
Claviceps sp.
-
-
-
Gln
-
reaction of component I with NH4+ as substrate
Glu
-
reaction of component I with NH4+ as substrate
Hg2+
Claviceps sp.
-
0.005 mM HgCl2, complete inhibition
Hg2+
-
1 mM HgCl2, 94.1% inhibition
iodoacetamide
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
iodoacetamide
-
irreversible, Gln protects
iodoacetamide
Claviceps sp.
-
-
L-2-Amino-4-oxo-5-chloropentanoic acid
-
irreversible, Gln protects
L-Trp
-
competitive with chorismate, noncompetitive with NH4+, reaction of component I with NH4+ as substrate
L-Trp
-
feedback inhibition
L-Trp
-
0.0033 mM, 50% inhibition
L-Trp
-
noncompetitive with respect to L-Gln, inhibitory effect increases with rising pH
L-Trp
Claviceps sp.
-
-
L-Trp
Hansenula henricii
-
competitive with respect to chorismate; noncompetitive with respect to NH4+ and Gln
L-Trp
-
isoenzyme AS-b is inhibited 97% by 0.020 mM, isoenzyme AS-a is inhibited 66% by 0.020 mM
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
-
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
L-Trp
-
competitive with respect to chorismate
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-tryptophan
Q9YGB3, -
-
L-tryptophan
-
feedback inhibition, 50% inhibition at 0.004-0.03 mM
L-tryptophan
-
strong, 50% inhibition at 0.005 mM
L-tryptophan
-
slightly inhibited
L-tryptophan
-
no activity in the presence of 0.05 mM
L-tryptophan
-
75.8% inhibition at 0.05 mM
L-tryptophan
-, P67001
-
Methylamine
-
reaction of component I with NH4+ as substrate
N-((S)-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxopropan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
-
-
N-((S)-6-amino-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxohexan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
-
-
N-Methylhydroxylamine
-
reaction of component I with NH4+ as substrate
N6-[3-(carboxymethoxy)benzoyl]-N2-(2,6-dimethoxybenzoyl)-L-lysyl-3-hydroxy-4-nitro-L-phenylalaninamide
-
-
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-3-chloro-L-phenylalaninamide
-
-
N6-[3-(carboxymethoxy)benzoyl]-N2-(3-hydroxy-4-methyl-2-nitrobenzoyl)-L-lysyl-4-cyano-L-phenylalaninamide
-
-
NEM
-
reaction of component I with NH4+ as substrate
p-Hydroxybenzaldehyde
-
-
p-hydroxybenzoate
-
-
Pb2+
Claviceps sp.
-
-
PCMB
-
reaction of component I with NH4+ as substrate
PCMB
Claviceps sp.
-
0.005 mM, complete inhibition
PCMB
-
1 mM, 88.6% inhibition
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
Zn2+
Claviceps sp.
-
1 mM, 75% inhibition
[3-([(5S)-5-[[(3-benzoylpyridin-2-yl)carbonyl]amino]-6-[(1-carbamoylcyclohexyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
-
[3-([(5S)-6-[(1-carbamoylcyclohexyl)amino]-5-[(3,5-dihydroxybenzoyl)amino]-6-oxohexyl]carbamoyl)phenoxy]acetic acid
-
-
[3-([(5S)-6-[(4-carbamoyl-1,1-dioxidotetrahydro-2H-thiopyran-4-yl)amino]-6-oxo-5-[(4-phenoxybenzoyl)amino]hexyl]carbamoyl)phenoxy]acetic acid
-
-
additional information
-
not inhibitory: D-tryptophan
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
chanoclavine
Claviceps sp.
-
slight activation in presence of His
elymoclavine
Claviceps sp.
-
slight activation in presence of His
indoleacrylic acid
Claviceps sp.
-
slight activation in presence of His
prephenic acid
Claviceps sp.
-
slight activation in presence of His
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
-
chorismate
-
-
0.003
-
chorismate
-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60C
0.0031
-
chorismate
-
-
0.0034
-
chorismate
Q9YGB3, -
75C, glutamine-dependent activity
0.0037
-
chorismate
-
pH 7.0, 25C
0.0039
-
chorismate
-
saturating Mg2+, pH 7.0, 25C
0.004
-
chorismate
-
-
0.005
-
chorismate
-
-
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
0.009
-
chorismate
-
anthranilate formation
0.009
-
chorismate
Claviceps sp.
-
-
0.0123
-
chorismate
-
pH 8.0, 60C, without glycerol and KCl
0.0138
-
chorismate
Q9YGB3, -
75C, ammonia-dependent activity
0.015
-
chorismate
-
with NH4+ as cosubstrate
0.018
-
chorismate
-
with Gln as cosubstrate
0.023
-
chorismate
Hansenula henricii
-
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
0.029
-
chorismate
-
pH 7.5
0.038
-
chorismate
-
at pH 9 and 37C, wild-type enzyme
0.039
-
chorismate
-
pH 8.3, 32C, A369L/L530D mutant anthranilate synthase alpha-subunit OASA2
0.04
-
chorismate
Claviceps sp.
-
-
0.042
-
chorismate
-
mutant enzyme R429H
0.043
-
chorismate
-
pH 8.3, 32C, A369L mutant anthranilate synthase alpha-subunit OASA2; pH 8.3, 32C, wild-type enzyme, anthranilate synthase alpha-subunit OASA2
0.046
-
chorismate
-
mutant enzyme
0.049
-
chorismate
-
pH 8.3, 32C, S126F mutant anthranilate synthase alpha-subunit OASA2
0.058
-
chorismate
-
pH 8.3, 32C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2
0.062
-
chorismate
-
pH 8.3, 32C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
0.0634
-
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: NH4+
0.067
-
chorismate
-
-
0.0703
-
chorismate
-
reconstituted enzyme OASA1D(N323D)-OASB1, cosubstrate: NH4+
0.073
-
chorismate
-
isoenzyme As-b
0.076
-
chorismate
-
pH 8.3, 32C, Y367A mutant anthranilate synthase alpha-subunit OASA2
0.0828
-
chorismate
-
alpha-subunit OASA2, cosubstrate: NH4+
0.084
-
chorismate
-
pH 8.0, 60C, 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
Hansenula henricii
-
NH4+-dependent enzyme, component I
0.05
-
Gln
-
isoenzyme As-b
0.094
-
Gln
Hansenula henricii
-
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
4
-
Gln
Claviceps sp.
-
-
5.6
-
Gln
-
chorismate-dependent glutaminase activity
10
-
Gln
Claviceps sp.
-
-
0.36
-
glutamine
-
-
0.0193
-
L-Gln
-
in 50 mM potassium phosphate buffer (pH 7.5), 20 mM L-glutamine, and 10 mM MgCl2, at 60C
0.237
-
L-Gln
-
mutant enzyme
0.249
-
L-Gln
-
wild-type enzyme
6.2
-
L-Gln
-
pH 8.0, 60C, without glycerol and KCl
7
-
L-Gln
-
pH 8.0, 60C, with 25% glycerol and 2 M KCl
0.088
-
L-glutamine
Q9YGB3, -
75C
2.5
-
L-glutamine
-
wild-type, at 25C, 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 60C
1.2
-
NH4+
Hansenula henricii
-
NH4+-dependent enzyme, component I
5.7
-
NH4+
-
pH 8.0, 60C, without glycerol and KCl
7.3
-
NH4+
-
pH 8.0, 60C, with 25% glycerol and 2 M KCl
8
9
NH4+
Claviceps sp.
-
-
26
-
NH4+
-
two-component enzyme, ASI,ASII
46
-
NH4+
-
at pH 9 and 37C
3.6
-
L-glutamine
-
mutant Q147K, at 25C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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, 32C, Y367A mutant anthranilate synthase alpha-subunit OASA2
0.108
-
chorismate
-
pH 8.3, 32C, S126F mutant anthranilate synthase alpha-subunit OASA2
0.22
-
chorismate
-
pH 8.3, 32C, A369L mutant anthranilate synthase alpha-subunit OASA2
0.225
-
chorismate
-
pH 8.3, 32C, 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, 60C, with or without 2 M KCl and 25% glycerol
0.27
-
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: NH4+
0.405
-
chorismate
-
pH 8.3, 32C, 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, 32C, Y367A/L530D mutant anthranilate synthase alpha-subunit OASA2
0.573
-
chorismate
-
pH 8.3, 32C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
0.58
-
chorismate
-
reconstituted enzyme OASA1-OASB1, cosubstrate: L-Gln
5.6
-
chorismate
-
pH 7.0, 25C
6.08
-
chorismate
-
pH 8.3, 32C, S126F/L530D mutant anthranilate synthase alpha-subunit OASA2
383
-
chorismate
-
at pH 9 and 37C, with NH4+ as cosubstrate
0.25
-
L-Gln
-
pH 8.0, 60C, with or without 2 M KCl and 25% glycerol
138
-
L-glutamine
-
wild-type, at 25C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
152
-
L-glutamine
-
mutant Q147K, at 25C, in 100 mM phosphate buffer, pH 7.0, with 20 mM L-glutamine and 5 mM MgCl2
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.76
-
(3-carbamoylphenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
2.6
-
(3-carbamoylphenoxy)acetic acid
-
inhibitior binding to the enzyme-chorismate complex, pH 7.8, 25C
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, 25C
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, 25C
0.0036
-
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.0019
-
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.041
-
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25C
-
0.0053
-
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
-
0.059
-
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25C
-
0.12
-
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
-
0.1
-
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25C
-
0.05
-
2-(1-carboxy-ethylamino)-isonicotinate
-
pH 7.0, 25C
-
0.041
-
2-(3-(-(S)-5-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-4-(3-hydroxy-4-methyl-2-nitrobenzamido)-5-oxopentylcarbamoyl)-phenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
-
0.096
-
2-(3-(3-((R)-3-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-2-(3-hydroxy-4-methyl-2-nitrobenzamido)-3-oxopropylthio) propylcarbamoyl)phenoxy)acetic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
-
0.094
-
2-(carboxymethyl-amino)-isonicotinate
-
pH 7.0, 25C
-
0.024
-
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
pH 7.0, 25C
0.021
-
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
pH 7.0, 25C
0.026
-
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
pH 7.0, 25C
0.0029
-
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
pH 7.0, 25C
0.025
-
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
pH 7.0, 25C
0.21
-
3-(carboxymethoxy)benzoic acid
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.55
-
3-(carboxymethoxy)benzoic acid
-
inhibitior binding to the enzyme-chorismate complex, pH 7.8, 25C
0.4
-
3-carboxymethylaminomethyl-4-hydroxybenzoate
-
pH 7.5
0.043
-
4-amino-3-(1-carboxyethoxy)benzoic acid
-
pH 7.0, 25C
0.023
-
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
pH 7.0, 25C
0.021
-
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25C
0.0054
-
DL-5-Methyltryptophan
-
-
0.00028
-
L-Trp
-
pH 8.0, 60C, without glycerol and KCl
0.00031
-
L-Trp
-
pH 8.0, 60C, with 25% glycerol and 2 M KCl
0.0033
-
L-Trp
-
-
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 60C
0.005
-
L-tryptophan
Q9YGB3, -
75C, ammonia-dependent activity, competitive to chorismate
0.074
-
L-tryptophan
Q9YGB3, -
75C, glutamine-dependent activity, competitive to chorismate
0.2
-
N-((S)-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxopropan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
-
0.11
-
N-((S)-6-amino-1-((S)-1-amino-3-(3-chlorophenyl)-1-oxopropan-2-ylamino)-1-oxohexan-2-yl)-3-hydroxy-4-methyl-2-nitrobenzamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
-
0.08
-
N6-[3-(carboxymethoxy)benzoyl]-N2-(2,6-dimethoxybenzoyl)-L-lysyl-3-hydroxy-4-nitro-L-phenylalaninamide
-
inhibition with respect to chorismate binding, pH 7.8, 25C
0.02
-
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, 25C
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, 25C
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, 25C
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, 25C
0.33
-
p-Hydroxybenzaldehyde
-
pH 7.5
0.002
-
p-hydroxybenzoate
-
pH 7.5
0.26
-
vanillate
-
pH 7.5
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, 25C
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, 25C
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, 25C
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, 25C
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, 25C
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, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0063
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00077
-
Q9AW95
original activity, un-induced state
0.0017
-
Q9AW95
original activity, induced state
0.0022
-
Q9AW95
activity after 5 years, un-induced state
0.0262
-
Q9AW95
activity after 5 years, induced state
0.585
-
Claviceps sp.
-
-
2.16
-
-, P67001
crude supernatant
4.44
-
-, P67001
purification step Ni-NTA column
5.2
-
-, P67001
after concentration step
43
-
Hansenula henricii
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
-
Hansenula henricii
-
Gln-dependent reaction
7.2
7.6
-
Gln-dependent activity
7.3
8
-
isoenzyme AS-b
7.3
-
Hansenula henricii
-
NH4+-dependent enzyme
7.5
8.3
-
Gln-dependent activity
7.6
-
-
Gln-dependent activity
7.8
-
Claviceps sp.
-
Gln-dependent activity
8
-
-
NH4+-dependent reaction, with 25% glycerol and 2 M KCl
8
-
Q9AW95
anthranilate synthase enzyme assay
8.1
-
-
L-Gln-dependent reaction, with 25% glycerol and 2 M KCl
8.5
-
-
above pH 8.5
8.6
-
Claviceps sp.
-
NH4+-dependent activity
8.7
-
-
Gln-dependent activity
8.7
-
-
NH4+-dependent reaction, without glycerol and KCl
8.8
-
-
reaction of ASI with chorismate and NH4+
8.8
-
-
L-Gln+-dependent reaction, without glycerol and KCl
9
-
-, P67001
activity assay
additional information
-
-
NH4+-dependent activity increases linearly through pH 9.0 without reaching a maximum
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
about 75% of maximal activity, Gln-dependent activity
6.5
9
-
pH 6.5: about 20% of maximal activity, pH 9.0: optimum
7
10
-, P67001
pH 7 20% relative activity, pH 10 60% relative activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
Q9AW95
anthranilate synthase enzyme assay
30
-
-, P67001
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
45
-
25C: about 70% of maximal activity, 45C: about 85% of maximal activity
30
37
-, P67001
incubation at temperatures higher than 37C results in a significant reduction of activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.72
-
-, Q5XLF2, Q5XLF3
calculation from nucleotide sequence
8.38
-
-, Q5XLF2, Q5XLF3
calculation from nucleotide sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
normal cells and cells resistant to growth inhibition by DL-5-methyltryptophan
Manually annotated by BRENDA team
Claviceps sp.
-
-
Manually annotated by BRENDA team
Claviceps sp. SD58
-
-
-
Manually annotated by BRENDA team
-, Q5XLF2, Q5XLF3
CaASA1 mRNA is first detected at 2 days post imbibition and reaches a maximum at 6 days post imbibition
Manually annotated by BRENDA team
-, Q5XLF2, Q5XLF3
high activity in vascular region of yound stem, weak activity in older stem
Manually annotated by BRENDA team
additional information
-, Q5XLF2, Q5XLF3
level of CaASA2 is constitutively low in Camptotheca acuminata and is found mainly in the reproductive tissues in transgenic tobacco plants
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is synthesized as a higher MW precursor and then imported into chloroplasts and processed into the mature form
Manually annotated by BRENDA team
-
,subunit Asalpha is synthesized as a cytosolic precursor, the active subunit is localized in the stroma of plastids
Manually annotated by BRENDA team
-
cultured cell protoplasts
-
Manually annotated by BRENDA team
-
Trp-resistant form
Manually annotated by BRENDA team
additional information
-
the Trp-sensitive form is localized in particulate fraction
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia sp. (strain 383)
Burkholderia sp. (strain 383)
Burkholderia sp. (strain 383)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
21050
-
-, Q7P0J9
calculated, beta, PabA subunit
47930
-
-, Q7P0J9
calculated, probable anthranilate synthase ORF CV0568
50000
-
Hansenula henricii
-
NH4-dependent enzyme, i.e. component I, gel filtration
54020
-
-, Q7P0J9
calculated, alpha, TrpE subunit
60000
-
Q9YGB3, -
gel filtration
62300
-
-, P67001
recombinant fusion protein, determined by SDS-PAGE
62350
-
-, P67001
determined by mass spectrometry
62370
-
-, P67001
calculated
80000
-
-
gel filtration
86000
-
-
gel filtration or sucrose density gradient centrifugation in presence of 30% glycerol
94000
117000
-
gel filtration
122000
-
-
gel filtration
126000
-
-
sucrose density gradient centrifugation
139300
-
-
deduced from amino acid sequence
140000
-
-
sucrose density gradient centrifugation
141000
-
-
sucrose density gradient centrifugation
143000
-
-
gel filtration
150000
-
-
gel filtration
150000
-
-
Trp-sensitive form, gel filtration
150000
-
-
-
150000
-
-
gel filtration
158000
-
-
gel filtration
160000
-
Hansenula henricii
-
Gln-dependent enzyme composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits (I2II2), gel filtration
160000
-
-
-
200000
-
Claviceps sp.
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, sucrose density gradient centrifugation
200000
-
-
Trp-resistant enzyme form, gel filtration
220000
-
-
gel filtration
400000
-
Claviceps sp.
-
three-enzyme complex containing anthranilate synthetase, phosphoribosyl anthranilate isomerase and indole-3-glycerol phosphate synthetase, gel filtration
additional information
-
-
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
-
-
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
-
-, Q7P0J9
experimental value between 84 and 95 kDa
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60000-65000 + x + 60000-65000, Asalpha-subunit and Asbeta-subunit are of a similar MW
?
-, Q5XLF2, Q5XLF3
x * 64512, calculation from nucleotide sequence; x * 65013, calculation from nucleotide sequence
dimer
-
1 * 18000 + 1 * 63400, sucrose density gradient centrifugation
dimer
-
1 * 14000 + 1 * 70000, gel filtration or sucrose density gradient centrifugation after separation of subunits
dimer
-
1 * 16000 + 1 * 80000
dimer
-
1 * 18000 + 1 * 64000
dimer
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
dimer
-
1 * 37000 + 1 * 60000, isoenzyme AS-b, SDS-PAGE
dimer
Streptomyces sp. 3022a
-
1 * 28000 + 1 * 72000, gel filtration after separation of subunits
-
heterodimer
Q9YGB3, -
1 * 57000 + 1 * 23000, SDS-PAGE, 1 * 48500 + 1 * 21100, deduced from gene sequence
heterodimer
-, Q7P0J9
alpha, TrpE, and beta, PabA, subunit
heterotetramer
-
crystallographic data
heterotetramer
-
association of 2 * enzyme + 2 * glutamine amidotransferase, crystallographic data
heterotetramer
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
heterotetramer
Sulfolobus solfataricus MT4
-
2 * 47743 + 2 * 21913, deduced from amino acid sequence
-
monomer
-
1 * 79000, SDS-PAGE
monomer
-
crystallographic data
tetramer
-
2 * 18000 + 2 * 71000
tetramer
-
-
tetramer
-
ASI, ASII, 2 * 21000 + 2 * 60000, SDS-PAGE
tetramer
Hansenula henricii
-
2 * 20000 + 2 * 50000, Gln-dependent enzyme, composed of 2 NH4+-dependent subunits and of 2 amidotransferase subunits, I2II2, gel filtration
tetramer
-
2 * 76000 + 2 * 84000, alpha2,beta2, SDS-PAGE
tetramer
-
2 * 20956 + 2 * 60000
tetramer
-
2 * 25500 + 2 * 67000, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 70000 + 2 * 94000, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 18000 + 2 * 50000, SDS-PAGE
tetramer
Serratia marcescens HY150
-
2 * 20956 + 2 * 60000
-
monomer
Euglena gracilis Z
-
1 * 79000, SDS-PAGE
-
additional information
-
component I has a MW of 63000 Da, gel filtration
additional information
-
multifunctional anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase
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
Hansenula henricii
-
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 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
-
subunit ASI catalyzes NH4+-dependent synthesis of anthranilate. Gln is not a substrate for ASI. ASII provides Gln-amide transfer function
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
-
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 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
-
partial complex anthranilate synthase consists of two TrpE:TrpG heterodimers
additional information
Serratia marcescens HY150
-
subunit ASI catalyzes NH4+-dependent synthesis of anthranilate. Gln is not a substrate for ASI. ASII provides Gln-amide transfer function
-
additional information
Streptomyces sp. 3022a
-
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
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with its product 4-hydroxybenzoate
-
in complex with allosteric inhibitor L-tryptophan
-
in complex with chorismate, glutamine and glutamate and in complex with L-tryptophan
P00897 and P00500
in the absence of physiological ligands
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
85
-
activity steadily increases with the rising of temperature in the range 25C to 85C, the enzyme is fully active above 85C
35
-
-
5 min, about 25% loss of activity
40
-
-
5 min, about 50% loss of activity
45
-
-
5 min, about 80% loss of activity
50
-
-
5 min, about 90% loss of activity
75
-
-
half-life in presence of 25% glycerol without KCl: 4.6 min, in 25% glycerol with 2 M KCl activity is constant for over 4 h after initial drop in activity to 83%
80
-
-
half-life in presence of 25% glycerol without KCl: 1.2 min, half-life in presence of 25% glycerol and 2 M KCl: 200 min
85
-
-
half-life in presence of 25% glycerol without KCl: 0.9 min, half-life in presence of 25% glycerol and 2 M KCl: 50 min
90
-
-
half-life in presence of 25% glycerol and 2 M KCl: 12 min
95
-
-
half-life in presence of 25% glycerol and 2 M KCl: 4.1 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
anthranilate synthetase activity of the enzyme complex is quite unstable unless Gln, MgCl2, Tris and glycerol are included in the extraction buffer
Claviceps sp.
-
1 mM dithiothreitol and 50 mM L-glutamine have a stabilizing effect each
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, in a 1:1 mixture of glycerol, 50 mM tricine, pH 7.5,1 mM DTT, 0.1 mM EDTA, additional protein bands appear upon storage, after an initial 10 15% drop in activity, little or no loss of enzyme activity is observed over a period of several weeks
-
4C, TEA-sulfuric acid buffer, PH 7.2, stable for at least 2 days
-
-80C, indefinitely stable
-
-20C, unstable
-
-80C, 20 mM KH2PO4 buffer, 50 mM KCl, 1 mM DTT, pH 7.5
-
2C or -10C, activity declines to 3400 or 4000 units per mg and remains constant for several months
-
-20C, activity of partially purified enzyme declines during storage
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isoenzyme As-b
-
anthranilate synthase I, from a plasmid bearing Escherichia coli
-
recombinant CaASA1
-, Q5XLF2, Q5XLF3
partial
Claviceps sp.
-
-
Hansenula henricii
-
using Ni-NTA His-binding resin, the 6xHis-tag is removed by digestion with enterokinase
-, P67001
partial, from a high rutacridone producing cell line R-20 and from a low rutacrinone producing cell line R-15
-
ammonium sulfate precipitation, ion exchange chromatography
-
L-Trp-agarose in the purification of the anthranilate synthetase complex
-
wild-type and mutant purified by hydroxyapatite chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha subunit (with a point mutation to confer feedback resistance to tryptophan) expressed in hairy root of Catharanthus roseus
-
expression in Escherichia coli
-
expressed in Escherichia coli strain JM109
-
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
B5AAU2
into the pGEM-T Easy vector for expression in Escherichia coli cells
-
expression in Nicotiana tabacum; expression in Nicotiana tabacum
-, Q5XLF2, Q5XLF3
mutant anthanilate synthase Pro21Ser that is insensitive to feedback inhibition by Trp
-
into the vector pET30a for expression in Escherichia coli BL21DE3 cells
-, P67001
expressed in Glycine max
-
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
-
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
-
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
-
expressed in Arabidopsis thaliana
-
expressed in Vigna angularis
-
expression in Saccharomyces cerevisiae
-
expression of OASA1D/N323 in Solanum tuberosum induces a 2fold to 20fold increase in the amount of Trp
-
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
-
cloning of the genes phnA and phnB of the anthranilate synthase that participates in the synthesis of pyocyanin
-
expression in Escherichia coli
-
partial complex anthranilate synthase expressed in Escherichia coli CB694
-
wild-type and mutant overexpressed in Escherichia coli cells (strain CB694) harboring the pSTC25 plasmid
-
His-tagged veresion expressed in Escherichia coli C41(DE3)
-
TrpE subunit
P00897 and P00500
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R321H
-
Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R358H
-
Km-value is increased 3fold to 4fold compared to the value for the wild-type enzyme, little effect on turnover number
R429H
-
similar Km value to the wild-type enzyme and a slightly larger turnover number
R452H
-
less than 0.05% of the activity of the wild-type enzyme
C14S
-
increase of Km value by 50%, improved behaviour in solution and crystallization
C81S
-
increase of Km value by 50%, improved behaviour in solution and crystallization
P21S
-
insensitive to feedback inhibition by Trp
A369L
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
A380S
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
A532Y
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
G518A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
G521A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
G522A
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
G522Y
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
L520F
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
L530D
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
N351A
-
increased sensitivity to Trp feedback inhibition of anthranilate synthase alpha-subunit OASA2 mutant
N351D
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
N363A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
N363D
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P364A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P364L
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
P366A
-
mutation of anthranilate synthase alpha-subunit OASA2 abolishes activity
S126A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
S356A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
Y349A
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y349F
-
mutation of anthranilate synthase alpha-subunit OASA2 enhances catalytic activity
Y367A
-
Trp-insensitive mutant of anthranilate synthase alpha-subunit OASA2
Y367A/L530D
-
accumulation of free Trp in cells expressing the mutant OASA2 is 2.3fold of that of cells expressing wild-type D126F /L530D
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
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; 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
Azospirillum brasilense Yu62
-
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; 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
-
Y516A
-
nonfunctional protein, anthranilate synthase alpha-subunit OASA2
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923
biotechnology
Escherichia coli W3110 trpD9923
-
development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923
-
medicine
-, P67001
TrpE is a promising target for the design of novel anti-tuberculosis drugs
biotechnology
-
development of ASA2 as a chloroplast selective marker, which is important not only for biosafety reasons, but also for practical reason due to the scarcity of primary selective markers available
molecular biology
-
use of the feedback-insensitive alpha-subunit OASA1D (N323D) of anthranilate synthase as a selectable marker for transformation of rice and potato, the selection system will prove applicable to a wide range of plant species and culture procedures