Any feedback?
Literature summary extracted from
- Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis (1993), Biochemistry, 32, 5177-5186.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.1.B2 | - |
Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.B2 | MgCl2 | 10 mM, activity is reduced by 22% | Escherichia coli |  |
| 4.3.1.B2 | MnCl2 | 10 mM, activity is reduced by 58% | Escherichia coli | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 0.0015 | - |
L-glutamine | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 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 | |
| 4.3.1.B2 | 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 | |
| 4.3.1.B2 | 15 | - |
NH3 | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 16 | - |
NH3 | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 266 | - |
NH4+ | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 291 | - |
NH4+ | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 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 |
| 4.3.1.B2 | 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 |
| 4.3.1.B2 | 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 |
| 4.3.1.B2 | 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 |
| 4.3.1.B2 | 47500 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.B2 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.B2 | Escherichia coli | P60595 and P60664 | P60595: IGP synthase glutamine amidotransferase subunit, P60664: IGP synthase cyclase subunit | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.1.B2 | - |
Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.3.1.B2 | L-glutamine + H2O = L-glutamate + NH3 | (1a) | Escherichia coli | |
| 4.3.1.B2 | 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 | |
| 4.3.1.B2 | 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
| EC Number | Storage Stability | Organism |
|---|---|---|
| 4.3.1.B2 | 27°C, 30 days, imidazole glycerol phosphate synthase holoenzyme, 50% loss of activity | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.B2 | 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 | ? | - |
? | |
| 4.3.1.B2 | 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 | ? | |
| 4.3.1.B2 | 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 | ? | |
| 4.3.1.B2 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.1.B2 | 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 |
| 4.3.1.B2 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.1.B2 | HIS7 | - |
Escherichia coli |
| 4.3.1.B2 | IGP synthase | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 30 | - |
assay at | Escherichia coli |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 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]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 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 | |
| 4.3.1.B2 | 8.5 | - |
L-glutamine | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 8.6 | - |
NH3 | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 8.6 | - |
NH4+ | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 8.8 | - |
NH4+ | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 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
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 6 | 8 | L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme | Escherichia coli |
| 4.3.1.B2 | 8 | - |
assay at | Escherichia coli |
| 4.3.1.B2 | 8 | 9 | ammonia-dependent activity catalyzed by HisF | Escherichia coli |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.B2 | 8.5 | - |
85% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme | Escherichia coli |
| 4.3.1.B2 | 9.5 | - |
22% of maximal activity, L-glutamine-dependent activity catalyzed by IGP synthase holoenzyme | Escherichia coli |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.B2 | 0.03 | - |
NH4+ | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 0.032 | - |
NH4+ | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 0.55 | - |
NH3 | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
| 4.3.1.B2 | 0.57 | - |
NH3 | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 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 | |
| 4.3.1.B2 | 270 | - |
N1-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamido-1-beta-D-ribofuranosyl 5'-phosphate | pH 8.0, 30°C, HisF subunit | Escherichia coli | |
| 4.3.1.B2 | 5700 | - |
L-glutamine | pH 8.0, 30°C, IGP synthase holoenzyme | Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
