Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate | the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide | Escherichia coli | |
N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide | the catalytic turnover of glutamine can be increased up to 37fold by the addition of either the product D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate or the biosynthetic precursor N1-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli FB1 | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: L-glutamine | Escherichia coli | |
0.023 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: NH4+ | Escherichia coli | |
0.24 | - |
L-glutamine | pH 8.0, 30°C | Escherichia coli | |
291 | - |
NH4+ | pH 8.0, 30°C | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
47500 | - |
1:1 dimeric complex of HisH and HisF proteins, gel filtration | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | Escherichia coli | the enzyme is involved in histidine biosynthesis | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | Escherichia coli K12 | the enzyme is involved in histidine biosynthesis | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli K12 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | the enzyme is involved in histidine biosynthesis | Escherichia coli | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000 | Escherichia coli | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | the enzyme is involved in histidine biosynthesis | Escherichia coli K12 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine | glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000 | Escherichia coli K12 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+ | glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000 | Escherichia coli | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O | - |
? | |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + NH4+ | glutamine is a more efficient substrate relative to ammonium ion by a factor of 1000 | Escherichia coli K12 | 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 21653 (subunit HisH) + 1 * 28454 (subunit HisF), calculated from sequence, HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the IGP synthase holoenzyme | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
hisFH | - |
Escherichia coli |
IGP synthase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
6.1 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: NH4+ | Escherichia coli | |
8.5 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: L-glutamine | Escherichia coli | |
8.8 | - |
NH4+ | pH 8.0, 30°C | Escherichia coli | |
9.1 | - |
L-glutamine | pH 8.0, 30°C | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 8 | activity with glutamine | Escherichia coli |
8 | 9 | activity with NH4+ | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9.5 | the pH optimum with glutamine is broad over the range of values from 6.0 to 8.0 but diminishes to 85% at pH 8.5 and 22% at pH 9.5 | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in histidine biosynthesis | 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 | Escherichia coli | |
37.9 | - |
L-glutamine | pH 8.0, 30°C | Escherichia coli | |
265.2 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: NH4+ | Escherichia coli | |
5667 | - |
5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide | pH 8.0, 30°C, cosubstrate: L-glutamine | Escherichia coli |