Literature summary for 1.18.1.2 extracted from

Bhatt, A.N.; Shukla, N.; Aliverti, A.; Zanetti, G.; Bhakuni, V.
Modulation of cooperativity in Mycobacterium tuberculosis NADPH-ferredoxin reductase: cation-and pH-induced alterations in native conformation and destabilization of the NADP+-binding domain (2005), Protein Sci., 14, 980-992.

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
on thermal treatment, native enzyme undergoes partial denaturation with unfolding of only the FAD-binding domain and release of the protein-bound flavin. Thermal treatment in presence of either 150 mM NaCl or KCl or 0.01 mM MgCl2 or CaCl2 or pH of 6.0, results in a highly cooperative and complete thermal unfolding of the protein. Cations and pH 6.0 destabilize only the heat-stable NADP-binding domain	Mycobacterium tuberculosis

Renatured (Comment)

Organism

on thermal treatment, native enzyme undergoes partial denaturation with unfolding of only the FAD-binding domain and release of the protein-bound flavin. Thermal treatment in presence of either 150 mM NaCl or KCl or 0.01 mM MgCl2 or CaCl2 or pH of 6.0, results in a highly cooperative and complete thermal unfolding of the protein. Cations and pH 6.0 destabilize only the heat-stable NADP-binding domain

Mycobacterium tuberculosis

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Release 2023.1 (January 2023)