The Heavy-Light Chain Loop of Human Cathepsin-L Modulates Its Activity and Stability
Differences evident in the sequence alignment of human cathepsin-L with shrimp cathepsin-L and silicatein-α suggest the indirect involvement of the heavy to light chain loop (E286 to E289) in the function of these enzymes. Deletion of the loop and adjacent residues S290 to N293, decreased specific protease activity by 81% and 63%, respectively; complete substitution for the corresponding silicatein-α loop decreased activity by 35%. In all cases the Km was largely unchanged. The conformational stability of human procathepsin-L was not altered by deletion of E286 to E289 but increased on deletion of S290 to N293. Therefore, shortening the loop does not change substrate affinity but does influence activity, in part via conformational change.
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Document Type: Research Article
Publication date: January 1, 2008
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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