Influence of synthetic peptide inhibitors on the thermal stability of thermitase, a serine proteinase from Thermoactinomyces vulgaris.
The influence of chloromethyl ketones and methyl ketones of N-acylated peptides on the thermal denaturation of thermitase was investigated in the presence and the absence of calcium ions. The chloromethyl ketone derivatives are known to react irreversibly with the enzyme, whereas the corresponding methyl ketones are reversible inhibitors. Both groups of inhibitors offer a broad variety of affinity constants. The irreversible inhibition of thermitase causes a marked stabilization against thermal denaturation. On the other hand, the enzyme stability is not influenced by the binding of reversible inhibitors. The stabilizing effect of calcium ions is not dependent on the inhibitor binding. The importance of bivalent interaction (bridge formation) in the active site region of the enzyme for its thermal stability is discussed.
D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D008848:Micromonosporaceae / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology*; D011485:Protein Binding; D011489:Protein Denaturation; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship
D011480:Protease Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; C022728:thermitase