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 ACCESSION NO.
LITERATURE
(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-glutamine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleophilic substitution
G3XCK6, -
-
PATHWAY
KEGG Link
MetaCyc Link
phenazine-1-carboxylate biosynthesis
-
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 ACCESSION NO.
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
G3XCK6
-
PhzE
Burkholderia lata 383
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
152060-54-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Burkholderia lata 383
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
G3XCK6, -
-
-
-
?
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
SgcD activity is depended on the inclusion of Mg2+
Mg2+
G3XCK6, -
lower activity with Mn2+, Co2+, no detectable activity with Zn2+, Fe2+, Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Mn2+
-
reduced activity
Ni2+
-
reduced activity
Zn2+
-
reduced activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0024
-
chorismate
-
pH 7.0, 25C
0.02
-
chorismate
G3XCK6, -
L-glutamine as ammonia source, in the presence of Mg2+, pH 7.0, 25C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
chorismate
-
pH 7.0, 25C
0.16
-
chorismate
G3XCK6, -
ammonium sulfate as ammonia source, pH 7.0, 25C
2.2
-
chorismate
G3XCK6, -
L-glutamine as ammonia source, pH 7.0, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
G3XCK6, -
optimal activity at low pH values between pH 6.5 and pH 8.5
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.5
G3XCK6, -
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
30
G3XCK6, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
45
G3XCK6, -
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 58500, SDS-PAGE
?
G3XCK6, -
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 ACCESSION NO.
LITERATURE
hanging-drop vapor diffusion method, PEG 3350
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), cleavage of the tag, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-tagged protein expressed in Escherichia coli BL21(DE3)
-
the gene for SgcD is cloned into pET-30 Xa/LIC and expressed in Escherichia coli
-