BRENDA - Enzyme Database
show all sequences of 4.3.1.B2

Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis

Klem, T.J.; Davisson, V.J.; Biochemistry 32, 5177-5186 (1993)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
MgCl2
10 mM, activity is reduced by 22%
Escherichia coli
MnCl2
10 mM, activity is reduced by 58%
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.021
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit, saturating concentrations of ammonium chloride can not be achieved due to inhibition of the enzyme activity at chloride ion concentrations
Escherichia coli
0.24
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
15
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
16
-
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
266
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
291
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
21655
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
28457
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
31600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
47500
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine
Escherichia coli
for the IGP synthase holoenzyme L-glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000. The HisF subunit alone does not ulilize L-glutamine. It supports an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P60595 and P60664
P60595: IGP synthase glutamine amidotransferase subunit, P60664: IGP synthase cyclase subunit
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Reaction
Reaction
Commentary
Organism
L-glutamine + H2O = L-glutamate + NH3
(1a)
Escherichia coli
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine = L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
overall reaction
Escherichia coli
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3 = D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
(1b)
Escherichia coli
Storage Stability
Storage Stability
Organism
27°C, 30 days, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the glutaminase activity for the holoenzyme is 0.8% of that in the presence of the nucleotide substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
726928
Escherichia coli
?
-
-
-
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine
for the IGP synthase holoenzyme L-glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000. The HisF subunit alone does not ulilize L-glutamine. It supports an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine
726928
Escherichia coli
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
726928
Escherichia coli
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH4+
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
726928
Escherichia coli
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme; 1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
27
-
30 d, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity. The HisF and HisH proteins exhibit half-lives of less than 48 h under similar conditions
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.5
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
8.6
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.6
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.8
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
9.1
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
8
9
ammonia-dependent activity catalyzed by HisF
Escherichia coli
8
-
assay at
Escherichia coli
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8.5
-
85% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
9.5
-
22% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
MgCl2
10 mM, activity is reduced by 22%
Escherichia coli
MnCl2
10 mM, activity is reduced by 58%
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0015
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.021
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit, saturating concentrations of ammonium chloride can not be achieved due to inhibition of the enzyme activity at chloride ion concentrations
Escherichia coli
0.24
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
15
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
16
-
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
266
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
291
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
11600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
21655
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
28457
-
1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
31600
-
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
47500
-
gel filtration
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine
Escherichia coli
for the IGP synthase holoenzyme L-glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000. The HisF subunit alone does not ulilize L-glutamine. It supports an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Storage Stability (protein specific)
Storage Stability
Organism
27°C, 30 days, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the glutaminase activity for the holoenzyme is 0.8% of that in the presence of the nucleotide substrate N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
726928
Escherichia coli
?
-
-
-
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + L-glutamine
for the IGP synthase holoenzyme L-glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000. The HisF subunit alone does not ulilize L-glutamine. It supports an ammonia-dependent reaction with a turnover number similar to that of the holoenzyme with glutamine
726928
Escherichia coli
L-glutamate + D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH3
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
726928
Escherichia coli
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate + NH4+
the protein encoded by the hisF gene has an ammonia-dependent activity, it does not utilize L-glutamine as substrate. The ammonia-dependent reaction is completely independent of the HisH protein
726928
Escherichia coli
D-erythro-1-(imidazol-4-yl)glycerol phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
D-erythro-1-(imidazol-4-yl)glycerol phosphate i.e. (2R,3S)-2,3-dihydroxy-3-(1H-imidazol-4-yl)propyl phosphate. 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide i.e. [(2R,3S,4R,5R)-5-(4-carbamoyl-5-aminoimidazol-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate i.e. AICAR
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
1 * 11600 (HisH) + 1 * 31600 (HisF), gel filtration (Sephacryl S-100), the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme; 1 * 21655 (HisH) + 1 * 28457 (HisF), calculated from sequence, the HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the imidazole glycerol phosphate synthase holoenzyme
Escherichia coli
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Escherichia coli
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
27
-
30 d, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity. The HisF and HisH proteins exhibit half-lives of less than 48 h under similar conditions
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.5
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
8.6
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.6
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
8.8
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
9.1
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
8
L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
8
9
ammonia-dependent activity catalyzed by HisF
Escherichia coli
8
-
assay at
Escherichia coli
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8.5
-
85% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
9.5
-
22% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.03
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.032
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
0.55
-
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.57
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
38
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
270
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
Escherichia coli
5700
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.03
-
NH4+
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.032
-
NH4+
pH 8.0, 30°C, HisF subunit
Escherichia coli
0.55
-
NH3
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
0.57
-
NH3
pH 8.0, 30°C, HisF subunit
Escherichia coli
38
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
270
-
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate
pH 8.0, 30°C, HisF subunit
Escherichia coli
5700
-
L-glutamine
pH 8.0, 30°C, IGP synthase holoenzyme
Escherichia coli
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
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726941
Myers
Reaction coupling through inte ...
Saccharomyces cerevisiae
Biochemistry
44
11974-11985
2005
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5
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18
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1
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3
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1
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18
1
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5
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18
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3
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1
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18
1
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18
18
727051
Demin
Kinetic model of imidazologlyc ...
Escherichia coli
Biochemistry
69
1324-1335
2004
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1
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1
1
726938
Chaudhuri
Toward understanding the mecha ...
Saccharomyces cerevisiae
Biochemistry
42
7003-7012
2003
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1
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2
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1
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1
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3
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726939
Myers
Substrate-induced changes in t ...
Saccharomyces cerevisiae
Biochemistry
42
7013-7022
2003
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7
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3
22
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3
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1
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3
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1
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22
1
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7
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7
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3
7
22
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1
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3
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1
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22
1
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24
24
727791
Omi
Structure of imidazole glycero ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
J. Biochem.
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759-765
2002
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4
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1
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4
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1
1
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728807
Douangamath
Structural evidence for ammoni ...
Thermotoga maritima, Thermotoga maritima DSM 3109
Structure
10
185-193
2002
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1
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4
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2
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727736
Klem
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Subunit interactions and gluta ...
Escherichia coli
J. Bacteriol.
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989-996
2001
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1
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4
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1
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2
1
1
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8
1
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1
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4
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10
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1
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2
1
1
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8
1
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9
9
728818
Chaudhuri
Crystal structure of imidazole ...
Saccharomyces cerevisiae
Structure
9
987-997
2001
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1
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2
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748148
Beismann-Driemeyer
Imidazole glycerol phosphate ...
Thermotoga maritima, Thermotoga maritima DSM 3109
J. Biol. Chem.
276
20387-20396
2001
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9
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1
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6
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1
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2
1
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1
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9
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2
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1
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6
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1
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2
1
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1
1
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2
2
728731
Chittur
Expression and purification of ...
Saccharomyces cerevisiae
Protein Expr. Purif.
18
366-377
2000
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1
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2
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3
1
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3
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1
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1
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3
1
1
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2
1
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1
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1
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1
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1
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3
1
1
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2
1
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1
1
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2
2
726928
Klem
Imidazole glycerol phosphate s ...
Escherichia coli
Biochemistry
32
5177-5186
1993
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1
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2
7
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5
1
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2
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1
3
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1
4
1
1
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1
6
3
2
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1
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2
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7
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5
1
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1
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1
4
1
1
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1
6
3
2
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7
7