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show all sequences of 4.3.1.B2

The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy

Liebold, C.; List, F.; Kalbitzer, H.R.; Sterner, R.; Brunner, E.; Protein Sci. 19, 1774-1782 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermotoga maritima
Engineering
Amino acid exchange
Commentary
Organism
T78M
the mutation does not impair substrate binding to the active site of HisF
Thermotoga maritima
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
Thermotoga maritima
0.0028
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, HisH/HisF holoenzyme with a T78M mutant subunit HisF
Thermotoga maritima
0.0036
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
Thermotoga maritima
0.0059
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, HisH/HisF holoenzyme with a T78M mutant subunit HisF
Thermotoga maritima
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermotoga maritima
-
-
-
Purification (Commentary)
Commentary
Organism
-
Thermotoga maritima
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728756
Thermotoga maritima
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728756
Thermotoga maritima
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermotoga maritima
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
Thermotoga maritima
1.2
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
Thermotoga maritima
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermotoga maritima
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermotoga maritima
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
T78M
the mutation does not impair substrate binding to the active site of HisF
Thermotoga maritima
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.002
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
Thermotoga maritima
0.0028
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, HisH/HisF holoenzyme with a T78M mutant subunit HisF
Thermotoga maritima
0.0036
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
Thermotoga maritima
0.0059
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, HisH/HisF holoenzyme with a T78M mutant subunit HisF
Thermotoga maritima
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermotoga maritima
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-glutamine + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728756
Thermotoga maritima
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
NH4+ + N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
-
728756
Thermotoga maritima
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Thermotoga maritima
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.1
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: L-glutamine, wild-type enzyme
Thermotoga maritima
1.2
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 25°C, cosubstrate: NH4+, wild-type enzyme
Thermotoga maritima
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Thermotoga maritima
Other publictions for EC 4.3.1.B2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728756
Liebold
The interaction of ammonia and ...
Thermotoga maritima
Protein Sci.
19
1774-1782
2010
-
-
1
-
1
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
726941
Myers
Reaction coupling through inte ...
Saccharomyces cerevisiae
Biochemistry
44
11974-11985
2005
-
-
-
-
5
-
-
18
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
18
1
-
-
-
-
-
-
-
18
18
727051
Demin
Kinetic model of imidazologlyc ...
Escherichia coli
Biochemistry
69
1324-1335
2004
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
-
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-
-
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
726938
Chaudhuri
Toward understanding the mecha ...
Saccharomyces cerevisiae
Biochemistry
42
7003-7012
2003
-
-
-
1
-
-
2
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726939
Myers
Substrate-induced changes in t ...
Saccharomyces cerevisiae
Biochemistry
42
7013-7022
2003
-
-
-
-
7
-
3
22
-
-
-
-
-
3
-
-
1
-
-
-
-
-
3
-
1
-
-
22
1
-
-
-
7
-
-
-
-
-
-
-
7
-
-
3
7
22
-
-
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
22
1
-
-
-
-
-
-
-
24
24
727791
Omi
Structure of imidazole glycero ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biochem.
132
759-765
2002
-
-
-
1
-
-
-
-
-
-
-
2
-
93
-
-
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-
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4
-
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1
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2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
728807
Douangamath
Structural evidence for ammoni ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Structure
10
185-193
2002
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
1
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-
-
-
-
-
-
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-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
727736
Klem
-
Subunit interactions and gluta ...
Escherichia coli
J. Bacteriol.
182
989-996
2001
-
-
1
-
4
-
-
10
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
10
-
-
-
1
-
-
-
1
-
-
-
-
2
1
1
-
-
8
1
-
-
-
-
-
-
-
9
9
728818
Chaudhuri
Crystal structure of imidazole ...
Saccharomyces cerevisiae
Structure
9
987-997
2001
-
-
-
1
-
-
1
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
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-
1
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-
-
-
-
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-
1
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-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
748148
Beismann-Driemeyer
Imidazole glycerol phosphate ...
Thermotoga maritima, Thermotoga maritima DSM 3109
J. Biol. Chem.
276
20387-20396
2001
-
-
1
-
9
-
-
2
-
-
-
-
-
6
-
-
1
-
-
-
-
-
6
-
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
9
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
6
-
1
-
-
2
1
-
-
-
-
1
1
-
2
2
728731
Chittur
Expression and purification of ...
Saccharomyces cerevisiae
Protein Expr. Purif.
18
366-377
2000
-
-
1
-
-
-
-
2
-
-
3
1
-
3
-
-
1
-
-
1
-
-
3
1
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
3
1
-
-
-
1
-
1
-
-
3
1
1
-
-
2
1
-
-
-
-
1
1
-
2
2
726928
Klem
Imidazole glycerol phosphate s ...
Escherichia coli
Biochemistry
32
5177-5186
1993
-
-
1
-
-
-
2
7
-
-
5
1
-
2
-
-
1
3
-
-
-
1
4
1
1
-
1
6
3
2
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
7
-
-
5
1
-
-
-
1
-
-
-
1
4
1
1
-
1
6
3
2
-
-
-
-
-
-
7
7