Enzymatic properties of thiol-dependent serine proteinase of Bacillus intermedius 3-19.
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.
Itskovich
E L
EL
Department of Microbiology, School of Biology, Kazan State University, Kazan, Russia.
Balaban
N P
NP
Mardanova
A M
AM
Shakirov
E V
EV
Sharipova
M R
MR
Leshchinskaya
I B
IB
Ksenofontov
A L
AL
Rudenskaya
G N
GN
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*
D012997:Solvents; D013438:Sulfhydryl Compounds; D012697:Serine Endopeptidases; D002118:Calcium