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The specificity of the S 1 ' subsite of cysteine proteases
Author(s) -
Ménard Robert,
Carmona Euridice,
Plouffe Céline,
Brömme Dieter,
Konishi Yasuo,
Lefebvre Jean,
Storer Andrew C.
Publication year - 1993
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(93)80975-z
Subject(s) - proteases , papain , chemistry , cathepsin o , cysteine , cathepsin , cathepsin b , cathepsin c , biochemistry , cathepsin a , cathepsin h , cathepsin l , amino acid , stereochemistry , enzyme , cysteine proteinase inhibitors , substrate specificity , apoptosis , programmed cell death , caspase
The specificity of the S' 1 subsite of the cysteine proteases cathepsin B, L, S and papain has been investigated using a series of intramolecularly quenched fluorogenic substrates (Dansyl‐Phe‐Arg‐AA‐Trp‐Ala) where the P' 1 amino acid (AA) has been varied. Taken individually, each enzyme displays a relatively broad S' 1 subsite specificity and this subsite cannot be considered as a primary site of specificity. Notable differences do exist however between the various proteases. Cathepsin B prefers large hydrophobic residues in the P' 1 position of a substrate while cathepsin L has an opposite trend, favoring amino acids with small (Ala, Ser) or long but non‐branched (Asn, Gin, Lys) side chains. Cathepsin S and papain display a somewhat broader S' 1 subsite specificity.