Information on EC 4.1.1.48 - indole-3-glycerol-phosphate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.1.1.48
-
RECOMMENDED NAME
GeneOntology No.
indole-3-glycerol-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
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 [2.4.2.18 (anthranilate phosphoribosyltransferase), 4.1.3.27 (anthranilate synthase), 4.2.1.20 (tryptophan synthase) and 5.3.1.24 (phosphoribosylanthranilate isomerase)]
-
-
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
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
show the reaction diagram
molecular dynamics simulation study of the enzyme-substrate complex at room temperature and at 110C. Relative specific activity increases 4200fold up to 110C. 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
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
tryptophan biosynthesis
-
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)].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
eIGPS
-
-
-
-
IGP synthase
-
-
IGPS
-
-
-
-
IGPS
Mycobacterium tuberculosis Rv3246c
-
-
-
IGPS
Q06121
-
-
IGPS
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
indole-3-glycerol phosphate synthase
-
-
-
-
indole-3-glycerol phosphate synthase
-
-
indole-3-glycerol phosphate synthase
A1KJ27
-
indole-3-glycerol phosphate synthase
-
-
indole-3-glycerol phosphate synthase
A5U2W7
-
indole-3-glycerol phosphate synthase
P0A632
-
indole-3-glycerol phosphate synthase
Mycobacterium tuberculosis Rv3246c
-
-
-
indole-3-glycerol phosphate synthase
-
-
indole-3-glycerol phosphate synthase
Q06121
-
indole-3-glycerol phosphate synthase
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
-
Indole-3-glycerol phosphate synthetase
-
-
-
-
Indole-3-glycerol-phosphate synthase
-
-
-
-
indole-3-glycerolphosphate synthase
Q9YGB5
-
Indole-3-glycerophosphate synthase
-
-
-
-
Indoleglycerol phosphate synthase
-
-
-
-
Indoleglycerol phosphate synthase
-
-
Indoleglycerol phosphate synthetase
-
-
-
-
Indoleglycerolphosphate synthetase
-
-
-
-
InGP synthase
-
-
-
-
InGP synthetase
-
-
-
-
InGPS
-
-
-
-
Phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
-
-
-
-
Pk-trpC
Q9YGB5
gene name
PRAI
-
-
-
-
PRAI-InGPS
-
-
-
-
sIGPS
-
-
-
-
sIGPS
Q06121
-
-
Synthase, indole-3-glycerol phosphate
-
-
-
-
TrpC
Mycobacterium tuberculosis Rv3246c
-
-
-
TrpC
-
gene name
CAS REGISTRY NUMBER
COMMENTARY
9031-60-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
possibly forms a bifunctional enzyme with phosphoribosylanthranilate isomerase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
Enterobacter liquefaciens
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
strain W3110
-
-
Manually annotated by BRENDA team
Escherichia coli W3110
strain W3110
-
-
Manually annotated by BRENDA team
multifunctional enzyme with the activities of Ec 4.1.4.27, Ec 4.2.2.18, Ec 4.1.1.48 and Ec 4.2.1.20
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
strain H37Rv (ATCC 93009)
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv3246c
-
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
strain X2180-1A wild-type, strain RH 375 (Ndr), RH 558 (Cdr)
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, Ec4.1.1.48/Ec5.3.1.24
-
-
Manually annotated by BRENDA team
wild-type strain 655 and mutant strains
-
-
Manually annotated by BRENDA team
recombinant enzyme, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis riparia
-
-
-
Manually annotated by BRENDA team
Vitis vinifera x Vitis vinifera
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
the enzyme is involved in tryptophan biosynthesis
metabolism
Mycobacterium tuberculosis Rv3246c
-
the enzyme is involved in tryptophan biosynthesis
-
physiological function
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
-
involved in aromatic amino acid metabolism
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-(3-indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
Q06121
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
Q9YGB5, -
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
the enzyme is involved in tryptophan biosynthesis, 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
show the reaction diagram
-
tryptophan biosynthetic enzyme
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
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
show the reaction diagram
Q06121
the enzyme is involved in tryptophan biosynthesis, 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
show the reaction diagram
-
Lys53 acts as the general acid in the dehydration step of the reaction
-
-
?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Q06121
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Q56319
-
-
-
?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
ir
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
ir
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Pectobacterium carotovorum ICPB EC153
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Bacillus subtilis T3
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Serratia marcescens HY
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Escherichia coli W3110
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
Citrobacter freundii NCTC 6021
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
regulation of enzyme activity
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
regulation of enzyme activity
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Pectobacterium carotovorum ICPB EC153
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Bacillus subtilis T3
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Citrobacter freundii NCTC 6021
-
-
-
-
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
indoleglycerol phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate + ?
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
P0A632
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate + ?
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
A1KJ27
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate + ?
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
A5U2W7
-
-
-
?
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
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-(3-indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
-
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
show the reaction diagram
-
tryptophan biosynthetic enzyme
-
-
?
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
show the reaction diagram
Q06121
the enzyme is involved in tryptophan biosynthesis
-
-
?
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
1-(3-Indolyl)glycerol-3-phosphate + CO2 + H2O
show the reaction diagram
-
-
-
ir
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
regulation of enzyme activity
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
regulation of enzyme activity
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Pectobacterium carotovorum ICPB EC153
-
-
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Bacillus subtilis T3
-
enzyme is involved in tryptophan biosynthesis
-
-
-
1-(2-Carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
?
show the reaction diagram
Citrobacter freundii NCTC 6021
-
-
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
significantly affects activity, the optimal concentration is about 0.4-2.0 mM
Mg2+
-
significantly affects activity, the optimal concentration is about 0.4-2.0 mM
Mn2+
-
significantly affects activity, the optimal concentration is about 0.4-2.0 mM
Na+
-
significantly affects activity, the optimal concentration is about 0.4-2.0 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATB107
A1KJ27
1-azabicyclo[2.2.2]octan-3-one[4-(phenylamino)-6-(1-piperidinyl)-1,3,5-triazin-2-yl]hydrazone, 0.1 microg/ml minimum inhibitory concentration, potent competitive inhibitor of the substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
ATB107
A5U2W7
1-azabicyclo[2.2.2]octan-3-one[4-(phenylamino)-6-(1-piperidinyl)-1,3,5-triazin-2-yl]hydrazone, 0.1 microg/ml minimum inhibitory concentration, potent competitive inhibitor of the substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
ATB107
P0A632
1-azabicyclo[2.2.2]octan-3-one[4-(phenylamino)-6-(1-piperidinyl)-1,3,5-triazin-2-yl]hydrazone, 0.1 microg/ml minimum inhibitory concentration, potent competitive inhibitor of the substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
ATB107
-
potent inhibitor
H2O2
-
0.001% H2O2 inactivates the enzyme almost completely
L-tryptophan
P0A632
tryptophan at high concentrations has definite inhibitory activity against Mycobacterium tuberculosis but does not antagonize the activity of ATB107
Reduced 1-[2-carboxyphenyl)amino]-1-deoxyribulose 5-phosphate
-
-
-
streptomycin
-
0.5 mg/ml
tryptophan
A5U2W7
tryptophan at high concentrations has definite inhibitory activity against Mycobacterium tuberculosis but does not antagonize the activity of ATB107
methanol
-
enzyme activity is gradually lost in the presence of increasing concentrations of methanol and completely lost at 65%
additional information
A5U2W7
inhibitory effect of ATB107 can not be reversed by the addition of tryptophan
-
additional information
P0A632
inhibitory effect of ATB107 can not be reversed by the addition of tryptophan
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000013
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E51Q
0.000023
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A/N90Q
0.000036
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme N90A
0.000044
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, wild-type enzyme
0.000044
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, wild-type enzyme
0.000045
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, 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, 25C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
0.00005
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
0.000051
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, wild-type enzyme
0.000074
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, wild-type enzyme; pH 7.0, 37C, mutant enzyme N90A; pH 7.0, 75C, mutant enzyme R54A
0.000079
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90A
0.000088
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 27C, wild-type enzyme
0.000095
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A
0.000107
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme R54A/N90Q
0.000109
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
0.000117
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90Q
0.000132
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme N90Q
0.000145
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme R54A
0.000386
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E210Q
0.00106
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme R182A
0.0012
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme F89A
0.00244
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme K53R
0.045
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
0.055
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, pH 7.5
0.09
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
0.000006
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C
0.000014
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 45C
0.000025
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
Q56319
wild-type, pH 7.5, 25C
0.00004
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, wild-type enzyme
0.000045
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
0.000047
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
genetically engineered monofunctional enzyme form IGPS[1-259]
0.00005
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme P2S; pH 7.5, 37C, wild-type enzyme; pH 7.5, 60C, wild-type enzyme
0.000053
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60C
0.00009
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type, pH 7.5, 25C
0.000123
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 80C
0.00021
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
mutant Leu5Val
0.00034
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
0.0004
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme F246S
0.00042
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
bifunctional enzyme
0.00042
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/F246S
0.00069
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
Q56319
N-terminal deletion mutant lacking 25 amino acids, pH 7.5, 25C
0.0012
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
0.0026
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
at 60C
0.005
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
-
0.0056
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme G212E
0.0058
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
-
0.0099
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
truncated mutant
0.0099
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
N-terminal deletion mutant lacking 26 amino acids, pH 7.5, 25C
0.0109
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/G212E
0.013
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
genetically engineered monofunctional enzyme form IGPS[1-252FAG]
0.54
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
mutant Lys55Ser
1.13
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
increased Km value in the presence of ATB107
1.13
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
increased Km value in the presence of ATB107
1.19
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
H170A site directed mutagenesis
1.19
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
H170A site directed mutagenesis
1.42
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
L193A site directed mutagenesis
1.42
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
L193A site directed mutagenesis
1.53
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
S64A site directed mutagenesis; V169A site directed mutagenesis
1.53
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
S64A site directed mutagenesis; V169A site directed mutagenesis
1.81
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
L196A site directed mutagenesis
1.81
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
L196A site directed mutagenesis
2.49
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
P63A site directed mutagenesis
2.49
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
P63A site directed mutagenesis
2.57
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
N192A site directed mutagenesis
2.57
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
N192A site directed mutagenesis
6.63
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
R191A site directed mutagenesis
6.63
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
R191A site directed mutagenesis
20.34
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
N189A site directed mutagenesis
20.34
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
N189A site directed mutagenesis
21.67
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
A5U2W7
E168A site directed mutagenesis
21.67
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
P0A632
E168A site directed mutagenesis
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme K53Q
0.007
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E51Q
0.033
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
0.038
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
0.04
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555
0.04
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme N90A
0.042
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
0.06
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme K53R
0.06
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme F89A
0.062
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, wild-type enzyme
0.065
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
0.16
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, pH 7.5
0.16
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme R54A; pH 7.0, 25C, wild-type enzyme
0.17
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme N90A
0.19
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A/N90Q
0.3
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme N90Q
0.35
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A
0.41
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme R182A
0.42
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, wild-type enzyme
0.51
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme R54A/N90Q
0.55
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90A
0.67
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, wild-type enzyme
0.67
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, wild-type enzyme
0.89
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90Q
0.97
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E210Q
1.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
1.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme R54A
0.025
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type, pH 7.5, 25C
0.028
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
N-terminal deletion mutant lacking 26 amino acids, pH 7.5, 25C
0.03
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, 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
0.06
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
Q56319
N-terminal deletion mutant lacking 25 amino acids, pH 7.5, 25C
0.095
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
Q56319
wild-type, pH 7.5, 25C
0.12
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
mutant enzyme Lys55Ser
0.15
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, wild-type enzyme
0.16
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme P2S
0.27
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/F246S
0.35
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme F246S
0.36
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme G212E
0.57
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/G212E
0.98
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60C, wild-type enzyme
2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
mutant Leu5Val
2.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
3.15
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
at 60C
3.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
genetically engineered monofunctional enzyme form IGPS[1-259]
3.6
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
bifunctional enzyme
4.3
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
genetically engineered monofunctional enzyme form IGPS[1-252FAG]
7.2
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.36
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
825
2.9
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
25C, pH 7.5
825
13.3
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C
825
30
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme K53R
825
50
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme F89A
825
380
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme R182A
825
540
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E51Q
825
596
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme D61C labeled with the fluorescent dye Alexa Fluor 555
825
826
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme D61C labeled with the fluorescent dye PyMPO
825
840
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme R18C labeled with the fluorescent dye PyMPO
825
888
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, mutant enzyme R18C labeled with the fluorescent dye Alexa Fluor 555
825
1000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme N90A
825
1215
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 25C, wild-type enzyme
825
2200
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 25C, mutant enzyme R54A; pH 7.0, 25C, wild-type enzyme
825
2300
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme N90A; pH 7.0, 37C, mutant enzyme N90Q
825
2500
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, mutant enzyme E210Q
825
3700
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A
825
4800
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, wild-type enzyme; pH 7.0, 75C, mutant enzyme R54A/N90Q
825
7000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90A
825
7600
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme N90Q
825
8200
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 37C, mutant enzyme R54A/N90Q
825
15000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, wild-type enzyme
825
15230
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.5, 75C, wild-type enzyme
825
16000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
-
pH 7.0, 75C, mutant enzyme R54A
825
100
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/G212E; pH 7.5, 37C, mutant enzyme G212E
826
600
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, mutant enzyme P2S/F246S
826
750
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 25C, wild-type enzyme
826
900
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme F246S
826
3000
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, wild-type enzyme
826
3200
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 37C, mutant enzyme P2S
826
14200
-
1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate
-
pH 7.5, 60C, wild-type enzyme
826
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.27
-
phosphate
-
60C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.004
-
-
recombinant enzyme, at 37C, pH 7.0
additional information
-
-
rapid and sensitive continous spectrophotofluorometric assay that can be used in presence of glycerol
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
in 5 mM Tris-HCl buffer
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8
-
in 5 mM Tris-HCl buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
in 5 mM Tris-HCl buffer
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
35
-
activation energy value of 8.4 kcal/mol, the linearity of the Arrhenius plot demonstrates that there is no change in the rate-limiting step in the temperature range employed
60
95
Q9YGB5, -
60C: about 50% of maximal activity, 95C: about 45% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
10% (v/v) oleate-albumin-dextrose complex
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella abortus (strain 2308)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
21000
-
-
gel filtration
22000
-
-
gel filtration
23500
-
-
gel filtration, N-terminal deletion mutant lacking 26 amino acids
23600
-
-
gel filtration
24200
-
Q56319
gel filtration, N-terminal deletion mutant lacking 25 amino acids
26300
-
-
gel filtration, wild-type
28000
-
-
SDS-PAGE, recombinant enzyme
28200
-
Q56319
gel filtration, wild-type
30000
-
-
gel-filtration chromatography
31000
-
-
gel filtration
31000
-
-
equilibrium sedimentation analysis
32000
-
-
gel filtration
39300
-
Q56319
gel filtration, N-terminal deletion mutant lacking 25 amino acids
44000
-
-
equilibrium sedimentation
45000
-
-
gel filtration
47100
-
Q56319
gel filtration, wild-type
48000
-
-
gel filtration
53000
-
-
gel filtration
320000
340000
-
anthranilate synthetase complex, gel filtration
325000
-
-
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 28600, SDS-PAGE
dimer
-
2 * 155000, SDS-PAGE
dimer
Q56319
and dimer, 2 * 26600, N-terminal deletion mutant lacking 25 amino acids, 2 * 28700, wild-type, calculated
monomer
-
1 * 23500, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
monomer
-
-
monomer
-
1 * 27000, SDS-PAGE; 1 * 28566, calculation from nucleotide sequence
monomer
-
1 * 28700, deduced from gene sequence
monomer
-
1 * 26400, N-terminal deletion mutant lacking 26 amino acids, 1 * 28600, wild-type, calculated
monomer
Q56319
and dimer, 1 * 26600, N-terminal deletion mutant lacking 25 amino acids, 1 * 28700, wild-type, calculated
monomer
-
1 * 30000
monomer
Bacillus subtilis T3
-
1 * 23500, SDS-PAGE
-
tetramer
-
2 * 94000 + 2 * 70000, anthranilate synthetase complex, one subunit is a trifunctional peptide which contains the catalytic sites for the phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase reactions, and associates with the second subunit to form glutamine-dependent anthranilate synthetase, SDS-PAGE
monomer
Serratia marcescens HY
-
1 * 48000, SDS-PAGE
-
additional information
A5U2W7
one typical (beta /alpha)8-barrel structure
additional information
P0A632
one typical (beta /alpha)8-barrel structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
kinetic studies of folding mechanism
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2.0 A structure; 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
-
in complex with substrate 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate, with a substrate analogue, and with product indole-3-glycerol phosphate
-
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
-
contains 17 strong salt bridges
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
slight activity at pH 5.0
8
-
-
almost no activity at pH 8.0
additional information
-
-
melting temperature is higher at alkaline that at neutral pH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
50
-
little loss of activity after a 10 min heating in a water bath at temperatures from 40 to 50C
44
-
-
half-life: 1.8 min
73
-
-
335 min, half-life for irreversible thermal inactivation
75
-
-
90 min, 50% loss of activity
75
-
-
half-life of wild-type, 123 min, half-life of N-terminal deletion mutant lacking 26 amino acids, 2.9 min
75
-
Q56319
half-life of wild-type, 258 min, half-life of N-terminal deletion mutant lacking 25 amino acids, 6.3 min
80
-
-
first-order kinetic constant at pH 6.5, pH 8.0 and pH 9.5: 0.020 per min
80
-
-
20 min, 50% loss of activity
83.5
-
-
110 min, half-life for irreversible thermal inactivation
84
-
-
110 min, half-life for irreversible thermal denaturation
85.5
-
-
14.4 min, half-life for irreversible thermal inactivation, mutant R241A; 36.1 min, half-life for irreversible thermal inactivation, mutant D184A; 42.3 min, half-life for irreversible thermal inactivation
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
89
-
-
half-life: 4.4 min
90
-
-
11 min, half-life for irreversible thermal inactivation
90
-
-
mutant enzyme N90A shows 2fold decrease in the rate of thermal inactivation at 90C as compared to wild-type enzyme. Thermal inactivation constant of muta t enzymes N90A or N90Q at 90C is similar to wild-type enzyme
additional information
-
-
melting temperature is higher at alkaline that at neutral pH
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
optimal stabilization by 0.8 M sucrose
-
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
-
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 87C) in comparison to HEPPS buffer (t1/2: 4.4 min at 89C)
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
urea
-
the structure of partially folded states of the enzyme is assessed by hydrogen exchange mass spectrometry and G 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
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, in presence of 0.8 M sucrose, 20% loss of activity
-
-70C, 5 mM Tris-HCl (pH 7.0), at least 2 months, remains stable
-
4C, 1 mM potassium phosphate buffer pH 7.5, 1 mM dithiothreitol, stable for hours
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
-
monofunctional enzyme
-
multifunctional enzyme with the activities of Ec 4.1.4.27, Ec 4.2.2.18, Ec 4.1.1.48 and Ec 4.2.1.20
-
chromatographic purification, Phenyl Sepharose High Sub FF column, ultrafiltration membrane (molecular weight cutoff) of 10,000 Da, Sephacryl S-100 column
-
Ni-NTA His-binding resin affinity chromatography
-
bifunctional enzyme phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase
-
final step with Superdex-75 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain BL21 (DE3)
-
expression in Escherichia coli BL21(DE3) STAR
-
expressed in Escherichia coli strain BL21
A5U2W7
expressed in Escherichia coli strain BL21
P0A632
expression in Escherichia coli
-
expression in Escherichia coli
Q9YGB5, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATB107 does not affect the expression of IGPS
-
ATB107 does not affect the expression of IGPS
Mycobacterium tuberculosis Rv3246c
-
-
a significant increase in trp mRNA level is observed in cells grown in medium depleted of L-tryptophan, compared to cells grown in medium supplemented with L-tryptophan, indicating that expression of the gene cluster is regulated at the transcriptional level
Q9YGB5, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L55S
-
Lys55Ser with 60fold decrease in turnover-number and 450fold increase in Km-value
E168A
A5U2W7
site directed mutagenesis
H170A
A5U2W7
site directed mutagenesis
L193A
A5U2W7
site directed mutagenesis
N189A
A5U2W7
site directed mutagenesis
N192A
A5U2W7
site directed mutagenesis
P63A
A5U2W7
site directed mutagenesis
R191A
A5U2W7
site directed mutagenesis
S64A
A5U2W7
site directed mutagenesis
V169A
A5U2W7
site directed mutagenesis
E168A
P0A632
site directed mutagenesis
H170A
P0A632
site directed mutagenesis
L193A
P0A632
site directed mutagenesis
N189A
P0A632
site directed mutagenesis
N192A
P0A632
site directed mutagenesis
P63A
P0A632
site directed mutagenesis
R191A
P0A632
site directed mutagenesis
S64A
P0A632
site directed mutagenesis
V169A
P0A632
site directed mutagenesis
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
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
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
N90A
-
loss of the descending limb in the pH rate profile, 5-fold decrease in kcat at 25C, but at higher temperatures (i.e. 75C), 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 75C. 2fold decrease in the rate of thermal inactivation at 90C 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 90C
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
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
R54A
-
mutation does not result in any substantial change to the steady-state kinetic parameters at any of the temperatures assayed (25C, 37C, 75C). At 75C, 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 75C. Thermal inactivation constant at 90C 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
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
-
R241A
-
no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability
L5V
-
Leu5Val without effect on turnover-number and Km
additional information
-
-
additional information
-
engineering of a monofunctional enzyme by separating the domains on the gene level and expression as monofunctional enzymes
L196A
A5U2W7
site directed mutagenesis
additional information
A5U2W7
site directed mutagenesis studies indicate that ATB107 may inhibit IGPS activity by reducing the binding affinity for substrate of residues Glu168 and Asn189
L196A
P0A632
site directed mutagenesis
additional information
P0A632
site directed mutagenesis studies indicate that ATB107 may inhibit IGPS activity by reducing the binding affinity for substrate of residues Glu168 and Asn189
M237T
-
kcat/Km of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose-5-phosphate is fold than wild-type value
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
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
D184A
-
no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability
additional information
Q56319
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
initiated by rapid 11fold dilution in refolding buffer (10 mM phosphate pH 7.8 and 25C)
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
A1KJ27
IGPS may be a potential target for the development of anti-tuberculosis drugs
drug development
-
indole-3-glycerol phosphate synthase of Mycobacterium tuberculosis is an attractive target for new anti-Tuberculosis drug development
medicine
A5U2W7
IGPS may be a potential target for the development of anti-tuberculosis drugs
medicine
P0A632
IGPS may be a potential target for the development of anti-tuberculosis drugs