ENZYMATIC-PROPERTIES OF THIOL-DEPENDENT SERINE PROTEINASE OF BACILLUS-INTERMEDIUS-3-19

Authors
ITSKOVICH EL BALABAN NP MARDANOVA AM SHAKIROV EV SHARIPOVA MR LESHCHINSKAYA IB KSENOFONTOV AL RUDENSKAYA GN
Citation
El. Itskovich et al., ENZYMATIC-PROPERTIES OF THIOL-DEPENDENT SERINE PROTEINASE OF BACILLUS-INTERMEDIUS-3-19, Biochemistry, 62(1), 1997, pp. 49-53
Citations number
14
Categorie Soggetti
Biology
Journal title
Biochemistry → ACNP
ISSN journal
00062979
Volume
62
Issue
1
Year of publication
1997
Pages
49 - 53
Database
ISI
SICI code
0006-2979(1997)62:1<49:EOTSPO>2.0.ZU;2-N
Abstract
Effects of a thiol-dependent serine proteinase of Bacillus intermedius on peptide substrates and insulin B-chain were studied. The enzyme pr eferably splits peptide bonds formed by carboxyl groups of hydrophobic amino acids. Ca2+ increases the thermal stability of the proteinase s ignificantly. The kinetic characteristics of hydrolysis of Z-Ala-Ala-L eu-pNA by this enzyme was determined as K-m 1.25 mM and k(cat) = 0.15 sec(-1). The enzyme has high stability to DMFA and isopropanol, and is able to catalyze peptide bond synthesis.