Engineering of papain: selective alteration of substrate specificity by site-directed mutagenesis

The S2 subsite specificity of the plant protease papain has been altered to resemble that of mammalian cathepsin B by site-directed mutagenesis. On the basis of amino acid sequence alignments for papain and cathepsin B, a double mutant (Val133Ala/Ser205Glu) was produced where Val133 and Ser205 are r...

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Veröffentlicht in:	Biochemistry (Easton) 1991-09, Vol.30 (37), p.8929-8936
Hauptverfasser:	Khouri, Henry E, Vernet, Thierry, Menard, Robert, Parlati, Francesco, Laflamme, Pierre, Tessier, Daniel C, Gour-Salin, Barbara, Thomas, David Y, Storer, Andrew C
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Analytical, structural and metabolic biochemistry Animals Base Sequence Biological and medical sciences Cattle Cloning, Molecular Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology GENIE GENETIQUE Humans Hydrogen-Ion Concentration Hydrolases INGENIERIA GENETICA Kinetics Mice Molecular Sequence Data MUTACION Mutagenesis, Site-Directed MUTATION Papain - biosynthesis Papain - genetics PAPAINA PAPAINE Rats Structure-Activity Relationship Substrate Specificity
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