Information on EC 2.6.1.86 - 2-amino-4-deoxychorismate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.86
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RECOMMENDED NAME
GeneOntology No.
2-amino-4-deoxychorismate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleophilic substitution
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of enediyne antibiotics
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Phenazine biosynthesis
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phenazine-1-carboxylate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-amino-4-deoxychorismate:2-oxoglutarate aminotransferase
Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 [1,2]. In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity [3,4].
CAS REGISTRY NUMBER
COMMENTARY hide
152060-54-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
L-glutamine + chorismate
(S)-2-amino-2-deoxyisochorismate + glutamate
show the reaction diagram
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?
L-glutamine + chorismate
(S)-2-amino-2-deoxyisochorismate + L-glutamate
show the reaction diagram
additional information
?
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the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
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the net conversion of chorismate to 3-enolpyruvoylanthranilate by the tandem action of SgcD and SgcG establishes a new branching point in chorismate metabolism leading to synthesis of C-1027, an enediyne antitumor antibiotic
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?
additional information
?
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the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mn2+
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reduced activity
Ni2+
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reduced activity
Zn2+
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reduced activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.02
chorismate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 2.2
chorismate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
optimal activity at low pH values between pH 6.5 and pH 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58500
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x * 58500, SDS-PAGE
70000
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2 * 70000, gel filtration, 140000 Da homodimer found in the asymmetric unit of crystals
71251
x * 71251, His-tagged PhzE, MALDI-TOF
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, PEG 3350
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), cleavage of the tag, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged protein expressed in Escherichia coli BL21(DE3)
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the gene for SgcD is cloned into pET-30 Xa/LIC and expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K274A/L277R/D299E/N303H/I306L/F334Y/C391G
mutant displaying anthranilate synthase activity, the kcat/Kchoris value for anthranilate formation is 25% of the wild-type aminodeoxychorismate synthase value for 4-amino-4-deoxychorismate production
N213V/L214P/K274A/L277R/D299E/N303H/F334Y/P363N/I367L/C391G/G425A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
N213V/L214P/R259S/K274A/L277R/N303H/F334Y/S366T/C391G/G254A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate