Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Regular paperDelineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content
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Cited by (21)
Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme
2008, Journal of Biological ChemistryCitation Excerpt :Although the binding site of GAGs and the prosegment on the TPP I molecule appear to partially overlap, the binding of GAGs was not saturable, and the interaction of the prosegment with its cognate enzyme was tight and saturable. It was documented that alkaline pH-induced inactivation of chicken cathepsin L was accompanied by the loss of α-helical content (35). Thus, it is reasonable to propose that the TPP I prosegment, by tightly binding its parent protease, might stabilize the activity of TPP I at alkaline pH by preventing pH-induced unfolding of the protein.
Identification, characterization and deduced amino acid sequence of the dominant protease from Kudoa paniformis and K. thyrsites: A unique cytoplasmic cysteine protease
2008, Comparative Biochemistry and Physiology - B Biochemistry and Molecular BiologyNon-binding property of cathepsin L to myosin
2008, Food ChemistryCathepsin X binds to cell surface heparan sulfate proteoglycans
2005, Archives of Biochemistry and BiophysicsCitation Excerpt :The deprotonation of His199 in cathepsin B, catalyzed by OH− ions, is considered a crucial event for alkaline pH-induced inactivation of this cysteine proteinase [38]. The break of the thiolate–imidazolium ion pair Cys29-His199 influences ionization and solvent exposure of some charged residues located at the interdomain interface, such as Asp40-Arg202 and Arg41-Glu163, resulting in conformational changes that promote destabilization of the central α-helix [38–40]. Fig. 4 shows that the secondary structure of cathepsin X is changed at pH 7.4, with loss of α-helix and concomitant gain of β structures.