Itskovich E L, Balaban N P, Mardanova A M, Shakirov E V, Sharipova M R, Leshchinskaya I B, Ksenofontov A L, Rudenskaya G N
Department of Microbiology, School of Biology, Kazan State University, Kazan, Russia.
Biochemistry (Mosc). 1997 Jan;62(1):49-53.
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.
