EC Number   |
Activating Compound |
Reference |
|---|
    4.2.1.20 | betaine |
1 M betaine activates the enzyme 1.8fold in the absence of monovalent cations |
729226 |
| 4.2.1.20 | Cs+ |
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site |
650222 |
| 4.2.1.20 | guanidine hydrochloride |
stimulating, dual effector as cation activator and as a modulator of the active site conformation by alteration of the equilibrium distribution of pyridoxal 5'-phosphate intermediates formed in reaction with the beta-subunit, effects on reaction are highly dependent on the substrate, effects are altered by NaCl |
649903 |
| 4.2.1.20 | guanidinium |
i.e. GuH+, involved in the thermal stability and activity equilibrium of the enzyme complex, overview |
649979 |
| 4.2.1.20 | hydroxylamine |
0.4-1.2 M, 7fold stimulation of alpha subunit |
5563 |
| 4.2.1.20 | Indole-3-acetamide |
allosteric effector, binds to the alpha-subunit, slightly activating effect on the enzyme complex, stabilization of the alpha-aminoacrylate Schiff base by perturbing the equilibrium of the catalytic intermediates formed at the beta-active site |
650304 |
| 4.2.1.20 | more |
Trp synthase exhibits low-activity (open) and high-activity (closed conformation). The open conformation is favored by high hydrostatic pressure. It is estimated that there are 35-47 more waters in the solvation shell of the open conformation than in that of the closed conformation |
664115 |
| 4.2.1.20 | Na+ |
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site |
650222 |
| 4.2.1.20 | NH4+ |
wild-type enzyme alpha-site is activated by the formation of the alpha-aminoacrylate Schiff base at the beta-site |
650222 |
| 4.2.1.20 | polyethylene glycol 8000 |
5% (w/v) activates the enzyme 2.1fold in the absence of monovalent cations |
729226 |
