title: The specificity of the S1' subsite of cysteine proteases.
abstract: The specificity of the S1' 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 P1' amino acid (AA) has been varied. Taken individually, each enzyme displays a relatively broad S1' 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 P1' position of a substrate while cathepsin L has an opposite trend, favoring amino acids with small (Ala, Ser) or long but non-branched (Asn, Gln, Lys) side chains. Cathepsin S and papain display a somewhat broader S1' subsite specificity.
authors.affiliation: Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
authors.forename: R
authors.initials: R
authors.lastname: Ménard
authors.forename: E
authors.initials: E
authors.lastname: Carmona
authors.forename: C
authors.initials: C
authors.lastname: Plouffe
authors.forename: D
authors.initials: D
authors.lastname: Brömme
authors.forename: Y
authors.initials: Y
authors.lastname: Konishi
authors.forename: J
authors.initials: J
authors.lastname: Lefebvre
authors.forename: A C
authors.initials: AC
authors.lastname: Storer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000737:chemistry; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D003619:Dansyl Compounds; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry; D051381:Rats; D013379:Substrate Specificity
chemical_list: D003619:Dansyl Compounds; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D010206:Papain