Literature summary for 2.6.1.1 extracted from

Oses-Prieto, J.A.; Bengoechea-Alonso, M.T.; Artigues, A.; Iriarte, A.; Martinez-Carrion, M.
The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase (2003), J. Biol. Chem., 278, 49988-49999.

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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	Rattus norvegicus

Renatured (Comment)

Organism

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

Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Rattus norvegicus

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Release 2023.1 (January 2023)