The specificity of the S1' subsite of cysteine proteases.
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.
Ménard
R
R
Biotechnology Research Institute, National Research Council of Canada, Montréal, Québec.
Carmona
E
E
Plouffe
C
C
Brömme
D
D
Konishi
Y
Y
Lefebvre
J
J
Storer
A C
AC
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
D003619:Dansyl Compounds; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D010206:Papain