The heavy-light chain loop of human cathepsin-L modulates its activity and stability

M. Fairhead, C.F. van der Walle

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)47-53
Number of pages6
JournalProtein and Peptide Letters
Volume15
Issue number1
DOIs
Publication statusPublished - Jan 2008

Keywords

  • cathepsin-L
  • silicatein-alpha
  • cysteine protease
  • protein engineering

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