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Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.48 indole-3-glycerol-phosphate synthase
IUBMB Comments
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 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
indole-3-glycerol phosphate synthase, sigps, igp synthase, indoleglycerol phosphate synthase, indole-3-glycerol-phosphate synthase, indoleglycerol phosphate synthetase, prai-ingps, eigps, indole-3-glycerolphosphate synthase, indole-3-glycerol phosphate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
eIGPS
-
-
-
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indole-3-glycerol phosphate synthase
Indole-3-glycerol phosphate synthetase
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-
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Indole-3-glycerol-phosphate synthase
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-
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Indole-3-glycerophosphate synthase
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-
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Indoleglycerol phosphate synthase
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-
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Indoleglycerol phosphate synthetase
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-
-
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Indoleglycerolphosphate synthetase
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-
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InGP synthase
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-
-
-
InGP synthetase
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-
-
-
InGPS
-
-
-
-
Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
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-
-
-
PRAI
-
-
-
-
PRAI-InGPS
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-
-
-
sIGPS
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-
-
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Synthase, indole-3-glycerol phosphate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate carboxy-lyase [cyclizing; 1-C-(indol-3-yl)glycerol-3-phosphate-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 4.1.3.27 (anthranilate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)].
CAS REGISTRY NUMBER
COMMENTARY hide
9031-60-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0113
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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at 37°C and pH 8.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.1
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
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at 37°C and pH 8.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
980
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
at 37°C and pH 8.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.2
-
activity begins to decrease above pH 8.2 and is 70% of maximum at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
the enzyme is about 2fold more active at 37°C than it is at 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme catalyzes the fifth reaction in the synthesis of tryptophan from chorismate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A367MAM9_PSEAI
278
0
30347
TrEMBL
-
A0A8G4E3U4_PSEAI
278
0
30333
TrEMBL
-
A0A8B5BLD2_PSEAI
278
0
30365
TrEMBL
-
A0A8F8R293_PSEAI
278
0
30363
TrEMBL
-
A0A8G3PQE5_PSEAI
278
0
30416
TrEMBL
-
A0A8G2RED3_PSEAI
278
0
30306
TrEMBL
-
A0A077JL91_PSEAI
278
0
30333
TrEMBL
-
A0A8G5CNR5_PSEAI
278
0
30332
TrEMBL
-
A0A8G4D0Q0_PSEAI
278
0
30347
TrEMBL
-
A0A7M3ANA6_PSEAI
278
0
30416
TrEMBL
-
A0A8G7KVH0_PSEAI
278
0
30344
TrEMBL
-
A0A8G5ZJE8_PSEAI
278
0
30379
TrEMBL
-
A0A6A9JZD5_PSEAI
278
0
30257
TrEMBL
-
A0A3M5DNR6_PSEAI
278
0
30314
TrEMBL
-
A0A509JFM6_PSEAI
278
0
30376
TrEMBL
-
A0A8G4TB93_PSEAI
278
0
30314
TrEMBL
-
A0A8G6LNI6_PSEAI
278
0
30361
TrEMBL
-
A0A8G1Q8X6_PSEAI
278
0
30319
TrEMBL
-
A0A7M2ZXV5_PSEAI
278
0
30344
TrEMBL
-
A0A8G2VAH5_PSEAI
278
0
30372
TrEMBL
-
A0A0A8RCA1_PSEAI
278
0
30299
TrEMBL
-
A0A8B4ZVN5_PSEAI
278
0
30280
TrEMBL
-
A0A8G7H5L2_PSEAI
278
0
30320
TrEMBL
-
A0A2R3J352_PSEAI
278
0
30317
TrEMBL
-
A0A8G5RQP3_PSEAI
278
0
30402
TrEMBL
-
A0A8G2VUE7_PSEAI
278
0
30377
TrEMBL
-
A0A8G4NQY4_PSEAI
278
0
30349
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
x * 31000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 31000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TALON metal affinity resin column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain KK-8(pDM)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gerth, M.L.; Nigon, L.V.; Patrick, W.M.
Characterization of the indole-3-glycerol phosphate synthase from Pseudomonas aeruginosa PAO1
Protein J.
31
359-365
2012
Pseudomonas aeruginosa
Manually annotated by BRENDA team