EC Number   |
Reference |
|---|
    2.6.1.1 | at 7 M urea and 25°C |
672257 |
| 2.6.1.1 | guanidinium hydrochloride denatured premature form pmAspAT cannot refold at 30°C, but refolds rapidly in presence of the intramitochondrial chaperone homologues GroEL and GroES |
639880 |
| 2.6.1.1 | in the presence of 0.01 mM pyridoxal 5'-phosphate |
672258 |
| 2.6.1.1 | reconstitution of holoenzyme after purification of apoenzyme with pyridoxal 5'-phosphate |
639820 |
| 2.6.1.1 | reconstitution of holoenzyme after purification of apoenzyme with the inhibitor N-5'-phosphopyridoxyl L-aspartate |
639839 |
| 2.6.1.1 | reconstitution of holoenzyme with pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate |
639837 |
| 2.6.1.1 | refolding of SsAspAT can be accelerated by increasing the temperature from 25 to 50°C. Although refolding is faster at 50°C (35% of native enzyme) the highest yield of renaturation is obtained at 37°C (70% reactivation), similar to the yield of 65% of initial activity that is obtained at 25°C |
682626 |
| 2.6.1.1 | reversible dissociation and unfolding of the dimeric enzyme by guanidine hydrochloride |
639842 |
| 2.6.1.1 | thermal denaturation is not reversible |
639820, 639861 |
| 2.6.1.1 | unfolding in 6 M guanidine hydrochloride for different periods of time. Reactivation of equilibrium-unfolded mAAT is sigmoidal, reactivation of the short term unfolded protein displays a double exponential behavior consistent with the presence of fast and slow refolding species. The presence of coenzyme does not perturb the kinetics or pathway of refolding. Covalently attached PLP slows down the interconversion between fast and slow folding populations of unfolded states. Additional structural rearrangements occurring both in the unfolded state and in populations of folding intermediates along the folding pathway |
659290 |
