[Secreted serine proteinase from the spore-forming bacteria Bacillus intermedius 3-19].
Extracellular serine proteinase has been isolated from the cultural medium of Bacillus intermedius 3-19 using CM-cellulose chromatography and affinity chromatography on bacitracin-Sepharose. The specificity of the proteinase with a wide range of natural and synthetic substrates has been investigated. The greatest activity was observed with tripeptides containing C-terminal Leu or Phe. The enzyme was completely inhibited by diisopropylfluorophosphate and partly inhibited by thiol-specific reagents. It is concluded that B. intermedius proteinase is a thiol-dependent serine proteinase pertaining to the subtilisin group. The amino acid composition of the enzyme has been determined. The enzyme contains one to three 1/2 cysteine residues, one of which is supposedly a Cys residue. The N-terminal amino acid sequences of the protein is AQTVPYGIPQIKAPA-.
Balaban
N P
NP
Sharipova
M R
MR
Itskovich
E L
EL
Leshchinskaia
I B
IB
Rudenskaia
G N
GN
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000502:physiology; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013171:Spores, Bacterial; D013379:Substrate Specificity
D012697:Serine Endopeptidases
Sekretiruemaia serinovaia proteinaza sporoobrazuiushchikh bakteriĭ Bacillus intermedius 3-19.