Abstract
The previously unstudied bacteriolytic enzyme L4 was isolated from the culture liquid of the bacterium Lysobacter sp.XL1 in electrophoretically homogeneous state. The enzyme L4 is a diaminopimelinoyl-alanine endopeptidase relative to peptidoglycan of Lysobacter sp. XL1. The enzyme is an alkaline protein of ∼ 21 kD. The N-terminal amino acid sequence of the enzyme has been determined — A V V N G V N Y V Gx T T A ... The maximal activity of the enzyme was observed in 0.05 M Tris-HCl at pH 8.0 and 50-55°C. The half-inactivation temperature of the enzyme is 52°C. The endopeptidase L4 is not a metalloenzyme since it is not affected by EDTA. The enzyme is inhibited by p- chloromercuribenzoic acid by 72% and by phenylmethylsulfonyl fluoride by 43%, which indicates the involvement of serine and thiol groups in its functioning.
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Translated from Biokhimiya, Vol. 70, No. 9, 2005, pp. 1250–1257.
Original Russian Text Copyright © 2005 by Stepnaya, Tsfasman, Logvina, Ryazanova, Muranova, Kulaev.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-290, February 20, 2005.
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Stepnaya, O.A., Tsfasman, I.M., Logvina, I.A. et al. Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1. Biochemistry (Moscow) 70, 1031–1037 (2005). https://doi.org/10.1007/s10541-005-0221-1
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DOI: https://doi.org/10.1007/s10541-005-0221-1