EC Number   |
General Stability |
Reference |
|---|
    6.3.4.3 | addition of monovalent cations to the dissociated enzyme causes the inactive monomers to reassociate to the active tetramer. The order of cation effectiveness is NH4+ > Tl+ > Rb+ ~ K+ > Cs+ > Na+ ~ Li+. The rate and extent of reactivation is influenced by the counter ion: sulfate and phosphate stimulate reassociation, thiocyanate, trichloroacetate, and perchlorate completly inhibit reassociation. The extent of reactivation is dependent upon protein concentration. The optimum protein concentration depends on the pH at which reactivation is performed |
1514 |
| 6.3.4.3 | enzyme is unstable in phosphate buffers in the absence of high concentrations of salt |
1519 |
| 6.3.4.3 | K+ or NH4+ increase stability of the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase |
1532 |
| 6.3.4.3 | photooxidation in presence of methylene blue results in a pseudo-first order loss of enzymatic activity and destruction of histidine residues |
1517 |
| 6.3.4.3 | purified enzyme as crystalline suspension, 15% loss of activity after 1 month |
1506 |
| 6.3.4.3 | tetramer is stabilized by 0.1 M sulfate in absence of an active monovalent cation |
1506 |
| 6.3.4.3 | the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ alters the susceptibility to digestion by chymotrypsin |
1503 |
| 6.3.4.3 | unstable in absence of monovalent cations |
1506 |
| 6.3.4.3 | unstable in presence of urea and guanidinium chloride |
1506 |
