Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding

• Published in: Biochimica et biophysica acta Vol. 1800; no. 9; pp. 937 - 945
• Main Authors: Chevigné, Andy, Dumez, Marie-Eve, Dumoulin, Mireille, Matagne, André, Jacquet, Alain, Galleni, Moreno
• Format: Journal Article Web Resource
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2010; Elsevier
• Subjects: Allergen; Animals; Antigens, Dermatophagoides - chemistry; Arthropod Proteins; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; Cysteine Endopeptidases; Cysteine protease; Cysteine Proteases - chemistry; Der p 1; Enzyme Precursors - chemistry; Enzyme Stability; Fluorescence quenching; Hydrogen-Ion Concentration; Life sciences; Mechanism of activation; pH-induced unfolding; Propeptide; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Pyroglyphidae - enzymology; Sciences du vivant; Stability; Thermal denaturation; unfolding; Zymogen; C34A; DTT; Der p 1; ANS; PDC; proDer p 1; AMC; Boc; prop; Mechanism of activation; WT; Fluorescence quenching; PBS; pH-induced unfolding; BMGY; Stability; E-64; Propeptide; Thermal denaturation; EDTA; p; Zymogen; SDS-PAGE; Cysteine protease; Allergen

Papain-like proteases (CA1) are synthesized as inactive precursors carrying an N-terminal propeptide, which is further removed under acidic conditions to generate active enzymes. To have a better insight into the mechanism of activation of this protease family, we compared the pH unfolding of the zy...