The specificity of the S1' subsite of cysteine proteases

FEBS Letters

Lefebvre, Jean¹  Storer, Andrew C.¹  Brömme, Dieter¹  Carmona, Euridice¹  Plouffe, Céline¹  Ménard, Robert¹  Konishi, Yasuo¹ 

[1] Biotechnology Research Institute, Natlonal Research Council of Canada, 6100 Avenue Royalmount, Montréal, Québec, H4P 2R2 Canada

关键词: Cysteine protease;    Papain;    Cathepsin;    Subsite specificity;   

DOI  :  10.1016/0014-5793(93)80975-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown