[Enzymes of a bacteriolytic lysoamidase preparation. Various properties of bacteriolytic protease L2].
Bacteriolytic proteinase L2 is able to cleave fluorogenic synthetic tripeptide anthranoyl-alanyl-alanyl-phenylalanyl-nitroanilide (Abz-Ala-Ala-Phe-pNA) at the bond between phenylalanine and p-nitroaniline. Optimal conditions of the tripeptide cleavage have been determined: pH 6.7 + 0.1; mu = 2 (by NaCl); t = 40 degrees C; KM = 2.6 x 10(-5) M. Metal cations reduced the enzyme activity. The enzyme was inhibited by EDTA, p-CMB, DIF. The synthetic tripeptide can be used to determine the activity of the L2 enzyme.
Stepanaia
O A
OA
Severin
A I
AI
Kudriavtseva
A I
AI
Krupianko
V I
VI
Kozlovskiĭ
A G
AG
Kulaev
I S
IS
D000595:Amino Acid Sequence; D002412:Cations; D002729:Chloromercuribenzoates / Q000737:chemistry; D004492:Edetic Acid / Q000737:chemistry; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007531:Isoflurophate / Q000737:chemistry; D008670:Metals / Q000378:metabolism; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D009994:Osmolar Concentration; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors; D013696:Temperature; D020245:p-Chloromercuribenzoic Acid
D002412:Cations; D002729:Chloromercuribenzoates; D008670:Metals; D009842:Oligopeptides; D011480:Protease Inhibitors; C060332:lysoamidase; D007531:Isoflurophate; D020245:p-Chloromercuribenzoic Acid; D004492:Edetic Acid; D010450:Endopeptidases; D010447:Peptide Hydrolases; C078955:proteinase L2
Fermenty bakterioliticheskogo preparata lizoamidaza. Nekotorye svoĭstva bakterioliticheskoĭ proteinazy L2.