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Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase and Organism(s) Thermotoga maritima and UniProt Accession Q56319
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4.1.1.48 indole-3-glycerol-phosphate synthaseIUBMB 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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Word Map
- 4.1.1.48
- sulfolobus
- solfataricus
-
amidotransferase
- chorismate
-
prfar
-
n-5'-phosphoribosylanthranilate
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on-pathway
-
glutamine-dependent
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betaalpha8-barrel
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betaalpha8
- medicine
- drug development
The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
eIGPS
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IGPS
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indole-3-glycerol phosphate synthase
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Indole-3-glycerol phosphate synthetase
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Indole-3-glycerol-phosphate synthase
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Indole-3-glycerophosphate synthase
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Indoleglycerol phosphate synthase
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Indoleglycerol phosphate synthetase
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Indoleglycerolphosphate synthetase
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InGP synthase
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InGP synthetase
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InGPS
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Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
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PRAI
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PRAI-InGPS
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sIGPS
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Synthase, indole-3-glycerol phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
9031-60-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
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-
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?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
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ir
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
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ir
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
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-
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ir
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000025
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
wild-type, pH 7.5, 25°C
0.00069
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
N-terminal deletion mutant lacking 25 amino acids, pH 7.5, 25°C
0.000006
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
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pH 7.5, 25°C
0.000014
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
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pH 7.5, 45°C
0.000053
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
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pH 7.5, 60°C
0.000123
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
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pH 7.5, 80°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
N-terminal deletion mutant lacking 25 amino acids, pH 7.5, 25°C
0.095
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
wild-type, pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24200
gel filtration, N-terminal deletion mutant lacking 25 amino acids
26600
28700
39300
gel filtration, N-terminal deletion mutant lacking 25 amino acids
26600
and dimer, 1 * 26600, N-terminal deletion mutant lacking 25 amino acids, 1 * 28700, wild-type, calculated
26600
and dimer, 2 * 26600, N-terminal deletion mutant lacking 25 amino acids, 2 * 28700, wild-type, calculated
28700
and dimer, 1 * 26600, N-terminal deletion mutant lacking 25 amino acids, 1 * 28700, wild-type, calculated
28700
and dimer, 2 * 26600, N-terminal deletion mutant lacking 25 amino acids, 2 * 28700, wild-type, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
and dimer, 2 * 26600, N-terminal deletion mutant lacking 25 amino acids, 2 * 28700, wild-type, calculated
monomer
and dimer, 1 * 26600, N-terminal deletion mutant lacking 25 amino acids, 1 * 28700, wild-type, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D184A
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no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability
R241A
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no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability
additional information
additional information
deletion of N-terminal 25 amino acids, unchanged oligomerzation states and turnover numbers, increase in Km-value for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, decrease in resistance towards unfolding induced by heat and guanidinium chloride
additional information
-
deletion of N-terminal 25 amino acids, unchanged oligomerzation states and turnover numbers, increase in Km-value for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, decrease in resistance towards unfolding induced by heat and guanidinium chloride
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
half-life of wild-type, 258 min, half-life of N-terminal deletion mutant lacking 25 amino acids, 6.3 min
85.5
85.5
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14.4 min, half-life for irreversible thermal inactivation, mutant R241A
85.5
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36.1 min, half-life for irreversible thermal inactivation, mutant D184A
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 mM potassium phosphate buffer pH 7.5, 1 mM dithiothreitol, stable for hours
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sterner, R.; Merz, A.; Thoma, R.; Kirschner, K.
Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima
Methods Enzymol.
331
270-280
2001
Thermotoga maritima
Knochel, T.; Pappenberger, A.; Jansonius, J.N.; Kirschner, K.
The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges
J. Biol. Chem.
277
8626-8634
2002
Thermotoga maritima
Merz, A.; Knochel, T.; Jansonius, J.N.; Kirschner, K.
The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges
J. Mol. Biol.
288
753-763
1999
Thermotoga maritima
Schneider, B.; Knochel, T.; Darimont, B.; Hennig, M.; Dietrich, S.; Babinger, K.; Kirschner, K.; Sterner, R.
Role of the N-terminal extension of the (betaalpha)(8)-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity
Biochemistry
44
16405-16412
2005
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus, Thermotoga maritima (Q56319), Thermotoga maritima
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