Article
How the substitution of K188 of trypsin binding site by aromatic amino acids can influence the processing of beta-casein.
Biochemical and biophysical research communications - 29 May 1998
Chobert J M, Briand L, Tran V, Haertlé T
Abstract excerpt
Aspartyl 189 residue of trypsin is known to be essential for specific lysis of Arg-X and Lys-X bonds. Undertaking to modulate the catalytic properties of this protease, otherwise highly conserved K188 was replaced with aromatic amino acid residues aiming the perturbation of the electrostatics and the amplifying of hydrophobic interactions of the substrate binding site. The catalytic properties of the mutants...
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