Characterization of the S'-subsite specificity of V8 proteinase via acyl transfer to added nucleophiles.
The S'-subsite specificity of endoproteinase Glu-C (V8 proteinase) was studied by acyl transfer reactions using Z-Glu-OMe as acyl donor and a series of amino acid- and peptide-derived nucleophiles. The partition constant, which characterizes specificity, was determined by a method based on the integrated rate equation. V8 proteinase prefers amino acid residues with hydrophobic side chains in the P'1 position. Di- and tripeptide amides are more efficient nucleophilic amino components than amino acid amides.
Schuster
M
M
Department of Biochemistry, Karl Marx University, Leipzig, F.R.G.
Aaviksaar
A
A
Schellenberger
V
V
Jakubke
H D
HD
D001665:Binding Sites; D007700:Kinetics; D012697:Serine Endopeptidases / Q000737:chemistry*; D012995:Solubility; D013379:Substrate Specificity
D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase