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Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19
E L Itskovich1, N P Balaban, A M Mardanova
1Department of Microbiology, School of Biology, Kazan State University, Kazan, Russia.
Biochemistry. Biokhimiia
|January 1, 1997
Abstract:
Effects of a thiol-dependent serine proteinase of Bacillus intermedius on peptide substrates and insulin B-chain were studied. The enzyme preferably splits peptide bonds formed by carboxyl groups of hydrophobic amino acids. Ca2+ increases the thermal stability of the proteinase significantly. The kinetic characteristics of hydrolysis of Z-Ala-Ala-Leu-pNA by this enzyme was determined as K(m) = 1.25 mM and kcat = 0.15 sec-1. The enzyme has high stability to DMFA and isopropanol, and is able to catalyze peptide bond synthesis.