Enzymes of a bacteriolytic lysoamidase preparation. Various properties of bacteriolytic protease L2

Stepanaia, O.A.; Severin, A.I.; Kudriavtseva, A.I.; Krupianko, V.I.; Kozlovskiĭ, A.G.; Kulaev, I.S.; Stepanaia, O.A; Severin, A.I; Kudriavtseva, A.I; Krupianko, V.I; Kozlovskii, A.G; Kulaev, I.S

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Enzymes of a bacteriolytic lysoamidase preparation. Various properties of bacteriolytic protease L2

Stepanaia, O.A.; Severin, A.I.; Kudriavtseva, A.I.; Krupianko, V.I.; Kozlovskiĭ, A.G.; Kulaev, I.S.

Prikladnaia Biokhimiia i Mikrobiologiia 28(5): 666-673

1992

ISSN/ISBN: 0555-1099

PMID: 1475262

Document Number: 405081

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.