Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Inhibitors | Comment | 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 Maximum [mM] | Substrate | Comment | 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 Maximum [Da] | Comment | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P60595 and P60664 | P60595: IGP synthase glutamine amidotransferase subunit, P60664: IGP synthase cyclase subunit | - |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Organism |
---|---|
27°C, 30 days, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | 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 | 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 | 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 | 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 | Comment | 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 | Escherichia coli |
dimer | 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 |
Synonyms | Comment | Organism |
---|---|---|
HIS7 | - |
Escherichia coli |
IGP synthase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | 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 Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme | Escherichia coli |
8 | - |
assay at | Escherichia coli |
8 | 9 | ammonia-dependent activity catalyzed by HisF | Escherichia coli |
pH Minimum | pH Maximum | Comment | 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 Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | 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 |