Fairhead, M. and van der Walle, C.F. (2008) The heavy-light chain loop of human cathepsin-L modulates its activity and stability. Protein and Peptide Letters, 15 (1). pp. 47-53.Full text not available in this repository. (Request a copy from the Strathclyde author)
Differences evident in the sequence alignment of human cathepsin-L with shrimp cathepsin-L and silicatein-alpha suggest the indirect involvement of the heavy to light chain loop (E 286 to E 289) in the function of these enzymes. Deletion of the loop and adjacent residues S 290 to N 293, decreased specific protease activity by 81% and 63%, respectively; complete substitution for the corresponding silicatein-alpha 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 E 286 to E 289 but increased on deletion of S 290 to N 293. Therefore, shortening the loop does not change substrate affinity but does influence activity, in part via conformational change.
|Keywords:||cathepsin-L, silicatein-alpha, cysteine protease, protein engineering, Pharmacy and materia medica, Biochemistry, Structural Biology|
|Subjects:||Medicine > Pharmacy and materia medica|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Strathprints Administrator|
|Date Deposited:||02 Jun 2010 16:39|
|Last modified:||05 May 2016 00:04|