Active center differences between cathepsins L and B: The S 1 binding region
Abstract
The substrate peptide bond cleaved by cathepsins B and L is determined not by the amino acid contributing the carboxyl group to this bond as in the case of serine proteases but rather by the presence of a neighboring amino acid with a large hydrophobic side chain. From a study of the inhibitory potency in a series, Cbz-Phe-X-CHN 2, in which Phe promotes binding at S 2 (terminology of [(1968) Biochem. Biophys. Res. Commun. 32, 898–902]) while the amino acid X probes S 1, it is shown that this region of cathepsin L also has the ability to accommodate large hydrophobic side chains. In this respect cathepsin L differs from cathepsin B. Thus Cbz-Phe-Tyr( O- t-Bu)CHN 2 inactivates cathepsin L with a rate 2.5 × 10 4 greater than that for cathepsin B.
- Publication:
-
FEBS Letters
- Pub Date:
- January 1988
- DOI:
- 10.1016/0014-5793(88)80600-8
- Bibcode:
- 1988FEBSL.228..128K
- Keywords:
-
- Cathepsin L;
- Cathepsin B;
- Selective inhibitor;
- Peptidyl diazomethyl ketone