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-CHN2, in which Phe promotes binding at S2 (terminology of [(1968) Biochem. Biophys. Res. Commun. 32, 898-902]) while the amino acid X probes S1, 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)CHN2 inactivates cathepsin L with a rate 2.5 x 10(4) greater than that for cathepsin B.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kirschke H,Wikstrom P,Shaw Edoi
10.1016/0014-5793(88)80600-8subject
Has Abstractpub_date
1988-02-08 00:00:00pages
128-30issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(88)80600-8journal_volume
228pub_type
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