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

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.6.1.86
-
RECOMMENDED NAME
GeneOntology No.
2-amino-4-deoxychorismate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleophilic substitution
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-amino-2-deoxyisochorismate (ADIC) synthase
-
-
2-amino-2-deoxyisochorismate synthase
-
-
2-amino-2desoxyisochorismate synthase
-
-
2-amino-2desoxyisochorismate synthase
Burkholderia lata 383
-
-
-
ADIC synthase
-
-
aminodeoxyisochorismate synthase
-
PhzE
Burkholderia lata 383
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
152060-54-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Burkholderia lata 383
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
-
-
-
?
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
-
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
-
?
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
-
(2S)-2-amino-4-deoxychorismate is formed by a reversible, Mg2+-dependent ADIC synthase activity of anthranilate synthase (EC 4.1.3.27) that can be functionally uncoupled from a Mg2+-dependent ADIC lyase activity of the enzyme by single amino acid substitutions in the TrpE subunit of the anthranilate synthase complex of Salmonella typhimurium
-
?
L-glutamine + chorismate
(S)-2-amino-2-desoxyisochorimate + L-glutamate
show the reaction diagram
Burkholderia lata, Burkholderia lata 383
-
-
-
?
L-glutamine + chorismate
(S)-2-amino-4-deoxychorimate + glutamate
show the reaction diagram
-
-
?
additional information
?
-
-
the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chorismate + L-glutamine
(2S)-2-amino-4-deoxychorismate + L-glutamate
show the reaction diagram
-
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
-
?
additional information
?
-
-
the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
SgcD activity is depended on the inclusion of Mg2+
Mg2+
lower activity with Mn2+, Co2+, no detectable activity with Zn2+, Fe2+, Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
-
reduced activity
Ni2+
-
reduced activity
Zn2+
-
reduced activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0024
chorismate
-
pH 7.0, 25C
0.02
chorismate
L-glutamine as ammonia source, in the presence of Mg2+, pH 7.0, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
chorismate
Burkholderia lata
-
pH 7.0, 25C
0.16
chorismate
Pseudomonas aeruginosa
G3XCK6
ammonium sulfate as ammonia source, pH 7.0, 25C
2.2
chorismate
Pseudomonas aeruginosa
G3XCK6
L-glutamine as ammonia source, pH 7.0, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
optimal activity at low pH values between pH 6.5 and pH 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 58500, SDS-PAGE
?
x * 71251, His-tagged PhzE, MALDI-TOF
homodimer
-
2 * 70000, gel filtration, 140000 Da homodimer found in the asymmetric unit of crystals
homodimer
Burkholderia lata 383
-
2 * 70000, gel filtration, 140000 Da homodimer found in the asymmetric unit of crystals
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, PEG 3350
-
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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