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Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q06121
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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
-
on-pathway
-
glutamine-dependent
-
betaalpha8-barrel
-
betaalpha8
- medicine
- drug development
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
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
-
-
-
-
IGPS
indole-3-glycerol phosphate synthase
Indole-3-glycerol phosphate synthetase
-
-
-
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Indole-3-glycerol-phosphate synthase
-
-
-
-
Indole-3-glycerophosphate synthase
-
-
-
-
Indoleglycerol phosphate synthase
Indoleglycerol phosphate synthetase
-
-
-
-
Indoleglycerolphosphate synthetase
-
-
-
-
InGP synthase
-
-
-
-
InGP synthetase
-
-
-
-
InGPS
-
-
-
-
Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
-
-
-
-
PRAI
-
-
-
-
PRAI-InGPS
-
-
-
-
sIGPS
-
-
-
-
Synthase, indole-3-glycerol phosphate
-
-
-
-
IGPS
-
-
-
-
indole-3-glycerol phosphate synthase
-
-
-
-
Indoleglycerol phosphate synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
mechanism, structures of two putative catalytic intermediates
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
molecular dynamics simulation study of the enzyme-substrate complex at room temperature and at 110°C. Relative specific activity increases 4200fold up to 110°C. Active site residues K53 and K110 control the binding of substrate in the favorable orientation for the general acid-catalyzed intramolecular ring formation reaction
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
molecular dynamics study at different temperatures. K110 is the general acid, E210 the general base. At higher temperature, the enzyme-substrate electrostatic interaction favors the binding of the substrate in near attack conformation, at lower temperature, the substrate is bound in nonreactive conformation
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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
-
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
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
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-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
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
indoleglycerol phosphate + CO2 + H2O
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
the enzyme is involved in tryptophan biosynthesis
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
elucidation of the kinetic reaction mechanism, importance of flexible active loops for substrate binding and catalysis by the enzyme, product release is the rate-limiting step of the overall reaction
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Lys53 acts as the general acid in the dehydration step of the reaction
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
tryptophan biosynthetic enzyme
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
?
-
a different degree of loop mobility correlates with different rate-limiting steps in the catalytic mechanism. Both the application of activating mutations and temperature increase lead to a net increase in the catalytic turnover number due to acceleration of the product release rate relative to the chemical transformation steps
-
-
?
additional information
?
-
-
a different degree of loop mobility correlates with different rate-limiting steps in the catalytic mechanism. Both the application of activating mutations and temperature increase lead to a net increase in the catalytic turnover number due to acceleration of the product release rate relative to the chemical transformation steps
-
-
?
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-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
the enzyme is involved in tryptophan biosynthesis
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
-
tryptophan biosynthetic enzyme
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000013
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E51Q
0.000044
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, wild-type enzyme
0.000045
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555
0.000046
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
0.00005
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
0.000051
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, wild-type enzyme
0.000085
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 25°C
0.000105
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 60°C
0.000109
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
0.000386
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E210Q
0.00106
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme R182A
0.0013
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant F246S, pH 7.5, 25°C
0.00244
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme K53R
0.0029
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant M237T, pH 7.5, 25°C
0.0034
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant L236Q, pH 7.5, 25°C
0.0217
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant G212E, pH 7.5, 25°C
0.045
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C
0.00009
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
wild-type, pH 7.5, 25°C
0.0099
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
N-terminal deletion mutant lacking 26 amino acids, pH 7.5, 25°C
0.000023
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A/N90Q
0.000036
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme N90A
0.000044
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, wild-type enzyme
0.000074
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, wild-type enzyme
0.000074
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90A
0.000074
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A
0.000079
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90A
0.000088
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 27°C, wild-type enzyme
0.000095
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A
0.000107
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A/N90Q
0.000117
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90Q
0.000132
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90Q
0.000145
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme R54A
0.0012
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme F89A
0.00004
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, wild-type enzyme
0.000045
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
0.00005
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, wild-type enzyme
0.00005
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme P2S
0.00005
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60°C, wild-type enzyme
0.0004
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme F246S
0.00042
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/F246S
0.0026
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
at 60°C
0.0056
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme G212E
0.0099
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
truncated mutant
0.0109
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/G212E
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme K53Q
0.007
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E51Q
0.033
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C
0.038
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
0.04
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555
0.042
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
0.06
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme K53R
0.062
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, wild-type enzyme
0.065
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
0.11
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 25°C
0.16
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant G212E, pH 7.5, 25°C
0.2
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant L236Q, pH 7.5, 25°C
0.23
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant M237T, pH 7.5, 25°C
0.32
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant F246S, pH 7.5, 25°C
0.41
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme R182A
0.67
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, wild-type enzyme
0.97
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E210Q
2.1
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 60°C
0.025
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
wild-type, pH 7.5, 25°C
0.028
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
N-terminal deletion mutant lacking 26 amino acids, pH 7.5, 25°C
0.04
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme N90A
0.06
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme F89A
0.16
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, wild-type enzyme
0.16
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme R54A
0.17
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90A
0.19
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A/N90Q
0.3
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90Q
0.35
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A
0.42
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, wild-type enzyme
0.51
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A/N90Q
0.55
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90A
0.67
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, wild-type enzyme
0.89
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90Q
1.2
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A
0.03
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, wild-type enzyme
0.033
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
0.041
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
truncated mutant
0.15
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, wild-type enzyme
0.16
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme P2S
0.27
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/F246S
0.35
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme F246S
0.36
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme G212E
0.57
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/G212E
0.98
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60°C, wild-type enzyme
3.15
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
at 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.36
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C
10
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant G212E, pH 7.5, 25°C
30
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme K53R
60
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant L236Q, pH 7.5, 25°C
80
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant M237T, pH 7.5, 25°C
240
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
mutant F246S, pH 7.5, 25°C
380
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme R182A
540
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E51Q
596
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
826
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
840
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
888
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555
1180
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 25°C
1215
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 25°C, wild-type enzyme
2500
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, mutant enzyme E210Q
15230
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
pH 7.5, 75°C, wild-type enzyme
20000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
wild-type, pH 7.5, 60°C
50
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme F89A
1000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme N90A
2200
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, mutant enzyme R54A
2200
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25°C, wild-type enzyme
2300
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90A
2300
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme N90Q
3700
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A
4800
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, wild-type enzyme
4800
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A/N90Q
7000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90A
7600
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme N90Q
8200
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37°C, mutant enzyme R54A/N90Q
15000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, wild-type enzyme
16000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75°C, mutant enzyme R54A
100
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/G212E
100
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme G212E
600
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, mutant enzyme P2S/F246S
750
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25°C, wild-type enzyme
900
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme F246S
3000
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, wild-type enzyme
3200
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37°C, mutant enzyme P2S
14200
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23500
gel filtration, N-terminal deletion mutant lacking 26 amino acids
26400
1 * 26400, N-terminal deletion mutant lacking 26 amino acids, 1 * 28600, wild-type, calculated
28600
28600
1 * 26400, N-terminal deletion mutant lacking 26 amino acids, 1 * 28600, wild-type, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 26400, N-terminal deletion mutant lacking 26 amino acids, 1 * 28600, wild-type, calculated
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, with a substrate analogue, and with product indole-3-glycerol phosphate
molecular dynamics simulations of wild-type at 25°C in the apo form and in the presence of the substrate
mutagenesis data and crystal structure analysis of IGPS from Sulfolobus solfataricus allows for the formulation of a plausible chemical mechanism of the reaction
N-terminal deletion mutant lacking 26 amino acids, structure of core is unchanged compared to wild-type
vapour diffusion method in hanging drops, the 2.0 A crystal structure is determined and compared with the known 2.0 A structure of the IGPS domain of the bifunctional enzyme from Escherichia coli. Both enzymes have only 30% sequence identity, but share high structural similarity
crystal packing seems to be influenced by ionic strength of the solvent
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D61C
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value
E210Q
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 6fold lower than wild-type value
E51Q
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 28fold lower than wild-type value
K53Q
low activity, kcat is 570fold lower than wild-type value
K53R
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 500fold lower than wild-type value
R182A
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 39fold lower than wild-type value
R18C
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value
R64A/D65A
mutation disrupts interactions on the C-terminal side of the beta1alpha1 loop and decreases catalytic efficiency, slows down the dehydration step and quenches loop dynamics
R64A/D65A/N90A
mutation leads to new micros-ms timescale loop dynamics and makes the ring-closure step rate-determining once again
F246S
-
about 2fold increase in turnover-number, 8fold increase in KM-value, decrease in kcat/Km
F89A
-
approximately 24fold increase in the KM-value, eleven-fold decrease in the maximum turnover rate
G212E
-
about 2fold increase in turnover-number, 100fold increase Km-value, decrease in kcat/Km. Mutant enzyme is about as thermostable as wild-type enzyme
M237T
-
kcat/Km of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate is fold than wild-type value
N90A
-
loss of the descending limb in the pH rate profile, 5-fold decrease in kcat at 25°C, but at higher temperatures (i.e. 75°C), the kinetic parameters for the N90A mutant enzyme closer to wild-type enzyme. Mutant enzyme has substantially reduced solvent deuterium kinetic isotope effects compared to wild-type enzyme at 75°C. 2fold decrease in the rate of thermal inactivation at 90°C as compared to wild-type enzyme
N90Q
-
the steady-state kinetics for the mutant enzyme are substantially decreased compared to wild-type enzyme at lower temperatures, but kcat of the N90Q variant approaches that of wild-type enzyme at higher temperatures. The solvent deuterium kinetic isotope effects on kcat is also substantially reduced compared to wild-type enzyme. 2fold decrease in the rate of thermal inactivation at 90°C
P2S
-
slight increase in kcat/Km (substrate: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate). Mutant enzyme is about as thermostable as wild-type enzyme
P2S/F246S
-
about 2fold increase in turnover-number, 8fold increase in KM-value, decrease in kcat/Km
P2S/G212E
-
about 4fold increase in turnover-number,200fold increase in Km-valuer, decrease in kcat/Km
R54A
-
mutation does not result in any substantial change to the steady-state kinetic parameters at any of the temperatures assayed (25°C, 37°C, 75°C). At 75°C, the mutant enzyme shows a small increase to kcat (about 1.8 fold) compared to wild-type enzyme. Mutant enzyme has substantially reduced solvent deuterium kinetic isotope effects compared to wild-type enzyme at 75°C. Thermal inactivation constant at 90°C is similar to wild-typ enzyme
R54A/N90A
-
the R54A/N90A double substitution are not additive with the effects of the R54A and N90A single substitutions suggesting some type of thermodynamic coupling between these residues
additional information
additional information
deletion of N-terminal 26 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 26 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
-
mutant enzyme with deletion of 8 terminal residues is soluble and has the same turnover number as the wild-type protein but a 220-fold greater Km-value
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
melting temperature is higher at alkaline that at neutral pH
4610
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
half-life of wild-type, 123 min, half-life of N-terminal deletion mutant lacking 26 amino acids, 2.9 min
80
86.5
-
in 0.05 M potassium phosphate at pH 7.5. Half-life of wild-type enzyme: 46 min, half-life of mutant enzyme P2S: 18 min, hal-life of mutant enzyme F246S 1 min, half-life of mutant enzyme G212E: 38 min, half-life of mutant enzyme P2S/F246S: less than 0.1 min, half-life of mutant enzyme P2S/G212E: 19 min
90
-
mutant enzyme N90A shows 2fold decrease in the rate of thermal inactivation at 90°C as compared to wild-type enzyme. Thermal inactivation constant of muta t enzymes N90A or N90Q at 90°C is similar to wild-type enzyme
additional information
80
-
first-order kinetic constant at pH 6.5, pH 8.0 and pH 9.5: 0.020 per min
additional information
-
the higher stability of the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus compared to indole-3-glycerol phosphate synthase from Escherichia coli seems to be the result of several improved interactions. These include a larger number of salt bridges, stabilization of alpha helices and strengthening of both polypeptide chain termini and solvent-exposed loops
additional information
the higher stability of the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus compared to indole-3-glycerol phosphate synthase from Escherichia coli seems to be the result of several improved interactions. These include a larger number of salt bridges, stabilization of alpha helices and strengthening of both polypeptide chain termini and solvent-exposed loops
additional information
-
melting temperature is higher at alkaline that at neutral pH
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
guanidinium-induced denaturation. Unfolding mechanism closely approaches a two-state model at pH 7.0 and a more complex mechanism at pH 9.0
-
half-life after trypsinolysis in 0.1 M Tris acetate at pH 7.8 and 25°C: wild-type enzyme (120 min), mutant enzyme P2S (60 min), mutant enzyme F246S (40 min), mutant enzyme G212E (40 min), mutant enzyme P2S/F246S (8 min), mutant enzyme P2S/G212E (15 min)
-
the enzyme is strongly stabilized in phosphate buffer (t1/2: 46 min at 87°C) in comparison to HEPPS buffer (t1/2: 4.4 min at 89°C)
-
the higher stability of the enzyme from Sulfolobus solfataricus compared with the enzyme from E. coli seems to be the result of several improved interactions. Including a large number of salt bridges, stabilization of alpha-helices and strengthening of both polypeptide chain termini and solvent-exposed loops
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
the structure of partially folded states of the enzyme is assessed by hydrogen exchange mass spectrometry and Gö model simulations. HX-MS analysis of the peptic peptides derived from the pulse-labeled product of the submillisecond folding reaction from the urea-denatured state reveal strong protection in the (betaalpha)4 region, modest protection in the neighboring (betaalpha)13 and (betaalpha)5beta6 segments and no significant protection in the remaining N and C-terminal segments. The results demonstrate that this species is not a collapsed form of the unfolded state under native-favoring conditions nor is it the native state formed via fast-track folding
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
initiated by rapid 11fold dilution in refolding buffer (10 mM phosphate pH 7.8 and 25°C)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stehlin, C.; Dahm, A.; Kirschner, K.
Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes
FEBS Lett.
403
268-272
1997
Escherichia coli, Saccharolobus solfataricus
Andreotti, G.; Cubellis, M.V.; di Palo, M.; Fessas, D.; Sannia, G.; Marino, G.
Stability of a thermophilic TIM-barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus
Biochem. J.
323
259-264
1997
Saccharolobus solfataricus
Andreotti, G.; Tutino, M.L.; Sannia, G.; Marino, G.; Cubellis, M.V.
Indole-3-glycerol-phosphate synthase from Sulfolobus solfataricus as a model for studying thermostable TIM-barrel enzymes
Biochim. Biophys. Acta
1208
310-315
1994
Escherichia coli, Saccharolobus solfataricus
Knchel, T.R.; Hennig, M.; Merz, A.; Darimont, B.; Kirschner, K.; Jansonius, J.N.
The crystal structure of indole-3-glycerol phosphate synthase from hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength
J. Mol. Biol.
262
502-515
1996
Saccharolobus solfataricus
Hennig, M.; Darimont, B.; Sterner, R.; Kirschner, K.; Jansonius, J.N.
2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability
Structure
3
1295-1306
1995
Escherichia coli, Saccharolobus solfataricus, Saccharolobus solfataricus (Q06121)
Hennig, M.; Darimont, B.D.; Jansonius, J.N.; Kirschner, K.
The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product
J. Mol. Biol.
319
757-766
2002
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus
Forsyth, W.R.; Matthews, C.R.
Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels
J. Mol. Biol.
320
1119-1133
2002
Saccharolobus solfataricus
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
Mazumder-Shivakumar, D.; Kahn, K.; Bruice, T.C.
Computational study of the ground state of thermophilic indole glycerol phosphate synthase: structural alterations at the active site with temperature
J. Am. Chem. Soc.
126
5936-5937
2004
Saccharolobus solfataricus (Q06121)
Mazumder-Shivakumar, D.; Bruice, T.C.
Molecular dynamics studies of ground state and intermediate of the hyperthermophilic indole-3-glycerol phosphate synthase
Proc. Natl. Acad. Sci. USA
101
14379-14384
2004
Saccharolobus solfataricus (Q06121)
Gu, Z.; Zitzewitz, J.A.; Matthews, C.R.
Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus
J. Mol. Biol.
368
582-594
2007
Saccharolobus solfataricus
Gu, Z.; Rao, M.K.; Forsyth, W.R.; Finke, J.M.; Matthews, C.R.
Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Go model simulation
J. Mol. Biol.
374
528-546
2007
Saccharolobus solfataricus, Saccharolobus solfataricus (Q06121)
Schlee, S.; Dietrich, S.; Kurcon, T.; Delaney, P.; Goodey, N.M.; Sterner, R.
Kinetic mechanism of indole-3-glycerol phosphate synthase
Biochemistry
52
132-142
2012
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q06121)
Merz, A.; Yee, M.C.; Szadkowski, H.; Pappenberger, G.; Crameri, A.; Stemmer, W.P.; Yanofsky, C.; Kirschner, K.
Improving the catalytic activity of a thermophilic enzyme at low temperatures
Biochemistry
39
880-889
2000
Saccharolobus solfataricus
Zaccardi, M.J.; Yezdimer, E.M.; Boehr, D.D.
Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis
J. Biol. Chem.
288
26350-26356
2013
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q06121)
Zaccardi, M.J., O'Rourke, K.F.; Yezdimer, E.M.; Loggia, L.J.; Woldt, S.; Boehr, D.D.
Loop-loop interactions govern multiple steps in indole-3-glycerol phosphate synthase catalysis
Protein Sci.
23
302-311
2014
Saccharolobus solfataricus
Schlee, S.; Klein, T.; Schumacher, M.; Nazet, J.; Merkl, R.; Steinhoff, H.J.; Sterner, R.
Relationship of Catalysis and Active Site Loop Dynamics in the (betaalpha)8 barrel enzyme indole-3-glycerol phosphate synthase
Biochemistry
57
3265-3277
2018
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus
O'Rourke, K.; Jelowicki, A.; Boehr, D.
Controlling active site loop dynamics in the (beta/alpha)8 barrel enzyme indole-3-glycerol phosphate synthase
Catalysts
6
129
2016
Saccharolobus solfataricus (Q06121), Saccharolobus solfataricus DSM 1617 (Q06121)
-
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