Abstract
Thermitase is a thermostable member of the subtilisin family of serine proteases isolated from Thermoactinomyces vulgaris l. It consists of a single polypeptide chain of 279 amino acid residues2. The degree of sequence homology to subtilisins BPN’ and Carlsberg is 42% and 44%, respectively. Eglin C is a serine protease inhibitor of 70 residues and is isolated from Hirudo medicinalis 3. The three-dimensional structure of eglin C has been determined previously in complex with subtilisin Carlsberg4.5. It was shown that the reactive loop of the inhibitor molecule noncovalently interacts with the enzyme at the binding groove. The inhibition effect of eglin C on subtilisins is ascribed to its ability to preserve the intact reactive loop via intensive intramolecular electrostatic interactions. Due to polypeptide nature, eglin C can be considered as a good model to study substrate recognition by subtilisins.
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© 1996 Plenum Press, New York
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Teplyakov, A., Gros, P., Hol, W.G.J. (1996). Crystallographic Study of Eglin-C Binding to Thermitase. In: Bott, R., Betzel, C. (eds) Subtilisin Enzymes. Advances in Experimental Medicine and Biology, vol 379. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0319-0_2
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DOI: https://doi.org/10.1007/978-1-4613-0319-0_2
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