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Information on EC 2.6.1.85 - aminodeoxychorismate synthase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.85 aminodeoxychorismate synthase
IUBMB Comments
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
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Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
aminodeoxychorismate synthase, pabab, 4-amino-4-deoxychorismate synthase, adc synthase, pvadcs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-amino-4-deoxychorismate synthase
-
-
-
-
ADC synthase
-
-
-
-
PabB
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
chorismate:L-glutamine aminotransferase
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
CAS REGISTRY NUMBER
COMMENTARY hide
132264-37-0
-
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
L-glutamate + 4-amino-4-deoxychorismate
show the reaction diagram
-
-
-
?
chorismate + NH3
4-amino-4-deoxychorismate + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, Km value 0.29 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-hydroxyphenazine
inhibitory above 0.200 mM
phosphate
phosphate buffer competitively inhibits PhzE, about 20% inhibition with 100 mM potassium phosphate at pH 7.0
pyocyanin
inhibitory above 0.250 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.216
chorismate
11
L-glutamine
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 2.2
chorismate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
20% of maximum activtiy
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G5ZP80_PSEAI
453
0
49677
TrEMBL
-
A0A8G4A199_PSEAI
453
0
49677
TrEMBL
-
A0A8G4NJ90_PSEAI
453
0
49573
TrEMBL
-
A0A0F6UEY7_PSEAI
453
0
49603
TrEMBL
-
A0A643J2M2_PSEAI
453
0
49630
TrEMBL
-
A0A8G5LFP2_PSEAI
453
0
49634
TrEMBL
-
A0A8G3WEM3_PSEAI
453
0
49661
TrEMBL
-
A0A659BF67_PSEAI
453
0
49604
TrEMBL
-
A0A8G1NIS6_PSEAI
453
0
49590
TrEMBL
-
A0A6A9JZT7_PSEAI
453
0
49661
TrEMBL
-
A0A485IF35_PSEAI
453
0
49671
TrEMBL
-
A0A7M3A0T7_PSEAI
453
0
49573
TrEMBL
-
A0A8B4ZW81_PSEAI
453
0
49621
TrEMBL
-
A0A8G5JYA8_PSEAI
453
0
49593
TrEMBL
-
A0A8G5RB59_PSEAI
453
0
49659
TrEMBL
-
A0A8G7FII7_PSEAI
453
0
49658
TrEMBL
-
A0A8F9P1K7_PSEAI
453
0
49580
TrEMBL
-
A0A8G2VSA8_PSEAI
453
0
49657
TrEMBL
-
A0A8G4IS62_PSEAI
453
0
49664
TrEMBL
-
A0A8G4NY54_PSEAI
453
0
49634
TrEMBL
-
A0A8G7LMH9_PSEAI
453
0
49545
TrEMBL
-
A0A485ETT7_PSEAI
488
0
53932
TrEMBL
-
A0A8G3U7I3_PSEAI
453
0
49664
TrEMBL
-
A0A8G7IIQ1_PSEAI
453
0
49618
TrEMBL
-
A0A8G3YJ50_PSEAI
453
0
49645
TrEMBL
-
A0A8G7AGM0_PSEAI
453
0
49571
TrEMBL
-
A0A8G2JX80_PSEAI
453
0
49635
TrEMBL
-
A0A8G4A986_PSEAI
453
0
49603
TrEMBL
-
A0A8G3BFF4_PSEAI
453
0
49673
TrEMBL
-
A0A080VCT8_PSEAI
453
0
49634
TrEMBL
-
A0A3S0KM22_PSEAI
453
0
49769
TrEMBL
-
A0A241XIG0_PSEAI
453
0
49633
TrEMBL
-
A0A8G4KFN4_PSEAI
453
0
49664
TrEMBL
-
A0A2R3IP88_PSEAI
408
0
44750
TrEMBL
-
A0A444LTV6_PSEAI
453
0
49604
TrEMBL
-
A0A8G3CR46_PSEAI
453
0
49720
TrEMBL
-
A0A5F1BH83_PSEAI
453
0
49623
TrEMBL
-
A0A8G7HS17_PSEAI
453
0
49604
TrEMBL
-
A0A8G3V3P0_PSEAI
453
0
49654
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 71274, calculated, x * 71251, MALDI-TOF, His-tagged recombinant protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Culbertson, J.E.; Toney, M.D.
Expression and characterization of PhzE from P. aeruginosa PAO1: aminodeoxyisochorismate synthase involved in pyocyanin and phenazine-1-carboxylate production
Biochim. Biophys. Acta
1834
240-246
2013
Pseudomonas aeruginosa (Q7DC81), Pseudomonas aeruginosa
Manually annotated by BRENDA team