Effect of pea and bovine trypsin inhibitors on wild‐type and modified trypsins

FEBS Letters

Haertlé, Thomas²  Pouvreau, Laurice²  Chobert, Jean-Marc²  Quillien, Laurence¹  Guéguen, Jacques¹  Briand, Loı̈c²  Tran, Vinh³ 

[1] Institut National de la Recherche Agronomique, LBTP, P.O. Box 71627, 44026 Nantes Cedex 03, France;Institut National de la Recherche Agronomique, LEIMA, P.O. Box 71627, 44026 Nantes Cedex 03, France;Institut National de la Recherche Agronomique, LPCM, P.O. Box 71627, 44026 Nantes Cedex 03, France

关键词: Trypsin;    Trypsin inhibitor;    Site-directed mutagenesis;   

DOI  :  10.1016/S0014-5793(98)00062-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In order to modify the catalytic properties of trypsin, lysine-188 (S1) of the substrate binding pocket was substituted by an aromatic amino acid residue (Phe, Tyr, Trp) or by a histidyl residue. Two other mutants were obtained by displacement or elimination of the negative charge of aspartic acid-189 (K188D/D189K and G187W/K188F/D189Y, respectively). The high affinity inhibitors, like PSTI II and BPTI, behaved as specific substrates of the trypsin and its mutants. Their inhibiting effect toward modified trypsins was studied. The bovine inhibitor had a higher affinity for all tested enzymes than pea inhibitor. The inhibition constants differed according to the mutations on the protease.

【 授权许可】

Unknown