Abstract
An enzyme exhibiting yeast-lytic activity has been isolated from the culture liquid of the bacterium Lysobacter sp. XL. 1. The optimal conditions for the hydrolysis of Saccharomyces cerevisiae cells by the enzyme have been established: 0.15 M sodium acetate buffer, pH 6.0, 50°C. The yeast-lytic activity of the enzyme is inhibited by EDTA, p-chloromercuribenzoate, and phenylmethylsulfonyl fluoride. According to the data of SDS-PAGE, the molecular weight of the protein is 36 kD. The enzyme hydrolyzes casein, hemoglobin, and synthetic peptide Abz-Ala-Ala-Phe-pNA, i.e. it exhibits proteolytic activity. The properties of the enzyme and its molecular weight correspond to those of a previously isolated extracellular metalloproteinase. The N-terminal amino acid sequence of the protein exhibits 67% homology with the N-terminal sequence of achromolysine of Achromobacter lyticus (EC 3.4.24.-).
Similar content being viewed by others
Abbreviations
- Abz:
-
o-aminobenzoate
- pNA:
-
p-nitroaniline
References
Marfenina, O. E. (2002) Priroda, 11, 33–38.
Klis, F. M. (1994) Yeast, 10, 851–869.
Kapteyn, J. C., van den Ende, H., and Klis, F. M. (1999) Biochim. Biophys. Acta, 1426, 373–383.
Kalebina, T. S., and Kulaev, I. S. (2001) Uspekhi Biol. Khim., 41, 105–130.
Iranzo, M., Aguado, C., Palotti, C., Canizares, J. V., and Vormeneo, S. (2000) Res. Microbiol., 4, 227–232.
Obata, T., Iwata, H., and Namba, Y. (1977) Agric. Biol. Chem., 41, 2387–2394.
Phaff, H. J. (1977) in Advances in Chemistry (Feeney, R. E., and Whitaker, J. R., eds.) Vol. 160, American Chemical Society, Washington, pp. 244–282.
Kalebina, T. S., Rudenskaya, G. N., Selyakh, I. O., Khodova, O. M., Chestukhina, G. G., Stepanov, V. M., and Kulaev, I. S. (1988) Appl. Microbiol. Biotechnol., 28, 531–536.
Sivan, A., and Chet, I. (1989) J. Gen. Microbiol., 135, 675–682.
Van Tilburg, A.-U. B., and Thomas, M. D. (1993) Appl. Environ. Microbiol., 59, 236–242.
Velazhahan, R., Samiyappan, R., and Vidhysekaran, P. (2000) Phytoparasitica, 28, 131–139.
Melent’ev, A. I., Aktuganov, G. E., and Galimzyanova, N. F. (2001) Mikrobiologiya, 70, 548–552.
Taira, T., Ohnuma, T., Yamagami, T., and Aso, Y. (2002) Biosci. Biotechnol. Biochem., 66, 970–977.
Bacteriolytic Complex, Method of Its Isolation, and Strain for Realization of the Method, RF Patent No. 2193063; Byul. Izobret. (2002) No. 32.
Stepnaya, O. A., Ledova, L. A., and Kulaev, I. S. (1999) Uspekhi Biol. Khim., 39, 327–354.
Stepnaya, O. A., Begunova, E. A., Tsfasman, I. M., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 471–476.
Stepnaya, O. A., Begunova, E. A., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 477–482.
Begunova, E. A., Lysanskaya, V. Ya., Stepnaya, O. A., and Kulaev, I. S. (2003) Biochemistry (Moscow), 68, 735–739.
Stepnaya, O. A., Tsfasman, I. M., Logvina, I. A., Ryazanova, L. P., Muranova, T. A., and Kulaev, I. S. (2005) Biochemistry (Moscow), 70, 1031–1037.
Ryazanova, L. P., Stepnaya, O. A., Suzina, N. E., and Kulaev, I. S. (2005) Proc. Biochem., 40, 557–564.
Krupyanko, V. I., Kudryavtseva, A. I., Valiakhmetov, A. Ya., Severin, A. I., Abramochkin, G. V., Zyakun, A. M., Lysogorskaya, E. N., Filippova, I. Yu., Kulaev, I. S., and Stepanov, V. M. (1989) Biokhimiya, 54, 1140–1149.
Nelson, N. J. (1944) J. Biol. Chem., 153, 375–380.
Laemmli, U. K. (1970) Nature, 227, 680–685.
Bradford, M. M. (1976) Analyt. Biochem., 72, 248–254.
Severin, A. I., Stepnaya, O. A., and Kulaev, I. S. (1986) Biokhimiya, 51, 748–753.
Kitamura, K. (1982) Agric. Biol. Chem., 46, 2093–2099.
Stepanov, V. M., Rudenskaya, G. N., Nesterova, N. G., Kupriyanova, T. I., Khokhlova, Yu. M., Usaite, I. A., Loginova, L. G., and Timokhina, E. A. (1980) Biokhimiya, 45, 1871–1880.
Funatsu, M., Oh, H., Aizono, J., and Shimoda, T. (1978) Agric. Biol. Chem., 42, 1975–1977.
Author information
Authors and Affiliations
Corresponding author
Additional information
Original Russian Text © O.A. Stepnaya, I.M. Tsfasman, I.A. Chaika, T.A. Muranova, I.S. Kulaev, 2008, published in Biokhimiya, 2008, Vol. 73, No. 3, pp. 381–387.
Rights and permissions
About this article
Cite this article
Stepnaya, O.A., Tsfasman, I.M., Chaika, I.A. et al. Extracellular yeast-lytic enzyme of the bacterium Lysobacter sp. XL 1. Biochemistry Moscow 73, 310–314 (2008). https://doi.org/10.1134/S0006297908030115
Received:
Revised:
Published:
Issue Date:
DOI: https://doi.org/10.1134/S0006297908030115