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...
Topics
- Amino Acid Sequence
- Amino Acids, Cyclic
- Binding Sites
- Caseins
- Hydrogen-Ion Concentration
- Hydrolysis
- Lysine
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Peptides