EC Number |
Activating Compound |
Reference |
---|
4.3.2.10 | 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 |
747052 |
4.3.2.10 | N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide |
binding of the allosteric effector ligand stimulates millisecond timescale motions in the enzyme that enhance its catalytic function. The flexibility of the apo enzyme is nearly identical to that of its N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide activated state at 70°C, whereas conformational motions are considerably different between the two forms of the enzyme at room temperature. Allosteric activation by N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide decreases to 65fold at 70°C, compared to 4200fold at 30°C |
747861 |
4.3.2.10 | 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 |
747052 |