[Thermitase--a thermostable serine protease. V. Stereospecificity of the binding of peptide ligands].
The diastereomeric tetrapeptides of the peptide ketone Z-(L-Ala)a-L-PheCH3, a competitively acting inhibitor of thermitase were synthesized with variations of the configuration in all positions. In kinetic experiments the enzyme shows a stereoselectivity for L-configurated amino acid residues in its binding region S1 to S4. The importance of the L-configuration found in the interaction of the enzyme with the inhibitor in S1 diminishes with growing distance from the S1 subsite. The all-L-inhibitor is two hundred times more affine than the LLLD compound. The results are discussed in comparison with the stereospecific behaviour of subtilisin BPN'.
D000192:Actinomycetales / Q000201:enzymology; D001667:Binding, Competitive; D010450:Endopeptidases / Q000378:metabolism*; D007659:Ketones / Q000494:pharmacology; D007700:Kinetics; D008024:Ligands; D010455:Peptides; D011485:Protein Binding; D011487:Protein Conformation; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship
D007659:Ketones; D008024:Ligands; D010455:Peptides; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase
Thermitase--eine thermostabile Serinprotease. V. Zur Stereospezifität der Bindung von Peptidliganden.