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Delineating functionally important regions and residues in the cathepsin B propeptide for inhibitory activity
Author(s) -
Chen Yanmin,
Plouffe Céline,
Ménard Robert,
Storer Andrew C.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00847-2
Subject(s) - cathepsin b , amino acid , inhibitory postsynaptic potential , biochemistry , alanine , amino acid residue , cathepsin , chemistry , protein precursor , alanine scanning , cathepsin d , cathepsin l , peptide sequence , microbiology and biotechnology , biology , enzyme , gene , mutation , mutagenesis , neuroscience
Synthetic peptides derived from the proregion of rat cathepsin B were used to identify functionally important regions and residues for cathepsin B inhibition. Successive 5 amino acid deletions of a 56 amino acid propeptide from both the N‐ and C‐termini has allowed the identification of two regions important for inhibitory activity: the NTTWQ (residues 21p–25p) and CGTVL (42p–46p) regions. Alanine scanning of residues within these two regions indicates that Trp‐24p and Cys‐42p contribute strongly to inhibition, their replacement by Ala resulting in 160‐ and 140‐fold increases in K i , respectively.