title: Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19.
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.
authors.affiliation: Department of Microbiology, School of Biology, Kazan State University, Kazan, Russia.
authors.forename: E L
authors.initials: EL
authors.lastname: Itskovich
authors.forename: N P
authors.initials: NP
authors.lastname: Balaban
authors.forename: A M
authors.initials: AM
authors.lastname: Mardanova
authors.forename: E V
authors.initials: EV
authors.lastname: Shakirov
authors.forename: M R
authors.initials: MR
authors.lastname: Sharipova
authors.forename: I B
authors.initials: IB
authors.lastname: Leshchinskaya
authors.forename: A L
authors.initials: AL
authors.lastname: Ksenofontov
authors.forename: G N
authors.initials: GN
authors.lastname: Rudenskaya
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002118:Calcium / Q000378:metabolism; D002384:Catalysis; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000378:metabolism*; D012997:Solvents; D013438:Sulfhydryl Compounds / Q000378:metabolism*
chemical_list: D012997:Solvents; D013438:Sulfhydryl Compounds; D012697:Serine Endopeptidases; D002118:Calcium