Structural investigations and identification of the extracellular bacteriolytic endopeptidase L1 from Lysobacter sp. XL1

Biochemistry (Moscow)

Volumn 69, Issue 5, 2004, Pages 501-505

  Muranova, T A ^a   Krasovskaya, L A ^a   Tsfasman, I M ^b   Stepnaya, O A ^b   Kulaev, I S ^b  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

Author keywords

Lysobacter sp.; Lytic endopeptidase; Primary structure; lytic proteinase

Indexed keywords

CELL CULTURE; DEGRADATION; ENZYMES; HYDROLYSIS; MATHEMATICAL MODELS; MICROORGANISMS; PROTEINS;

LYSOBACTER SP.; LYTIC ENDOPEPTIDASE; PRIMARY STRUCTURE; Α-LYTIC PROTEINASE;

AMINO ACIDS;

ACHROMOBACTER; ACHROMOBACTER LYTICUS; BACTERIA (MICROORGANISMS); LYSOBACTER; LYSOBACTER ENZYMOGENES; LYSOBACTER SP.;

MYXOBACTER ALPHA LYTIC PROTEINASE; MYXOBACTER ALPHA-LYTIC PROTEINASE; PEPTIDE FRAGMENT; SERINE PROTEINASE;

ACHROMOBACTER; AMINO ACID SEQUENCE; ARTICLE; BACTERIOLYSIS; CHEMISTRY; ENZYMOLOGY; MOLECULAR GENETICS; PHYSIOLOGY; XANTHOMONADACEAE;

ACHROMOBACTER; AMINO ACID SEQUENCE; BACTERIOLYSIS; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; SERINE ENDOPEPTIDASES; XANTHOMONADACEAE;

EID: 3042762503     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIRY.0000029847.40511.26     Document Type: Article

References (21)

1. Stepnaya, O. A., Ledova, L. A., and Kulaev, I. S. (1999) Uspekhi Biol. Khim., 39, 327-354.
2. White, D. (1995) The Physiology and Biochemistry of Procaryotes, Oxford University Press, N. Y.
3. Ghusen, J. M. (1968) Bac. Rev., 32, 425-464.
4. Li, S., Norioka, S., and Sakiyama, F. (1997) J. Biochem., 122, 772-778.
5. Lindsay, B., and Glaser, L. (1976) J. Biochem., 127, 803-811.
6. Kulaev, I. S., Naumova, I. B., Streshinskaya, G. M., Tul'skaya, E. M., Stepnaya, O. A., Severin, A. I., and Begunova, E. A. (1996) Mikrobiologiya, 65, 326-332.
7. Sitkin, B. V., Lysanskaya, V. Ya., Tsfasman, I. M., Stepnaya, O. A., and Kulaev, I. S. (2003) Mikrobiologiya, 72, 136-137.
8. Stepnaya, O. A., Begunova, E. A., Tsfasman, I. M., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 471-476.
9. Stepnaya, O. A., Severin, A. I., and Kulaev, I. S. (1986) Biokhimiya, 51, 1117-1123.
10. Stepnaya, O. A., Begunova, E. A., Tsfasman, I. M., and Kulaev, I. S. (1996) Biochemistry (Moscow), 61, 477-482.
11. Begunova, E. A., Stepnaya, O. A., Lysanskaya, V. Ya., and Kulaev, I. S. (2003) Biochemistry (Moscow), 68, 735-739.
12. Kulaev, I. S., Stepnaya, O. A., Tsfasman, I. M., Chermenskaya, T. S., Akimenko, V. K., Ledova, L. A., and Zubritskaya, L. G. (2002) Patent of RF 2193063, Byul. Izobret., No. 32.
13. Laemmli, U. K. (1970) Nature, 227, 680-685.
14. Bradford, M. M. (1976) Analyt. Biochem., 72, 248-254.
15. Friedman, M., Krull, L. H., and Cavins, J. F. (1970) J. Biol. Chem., 245, 3868-3874.
16. Li, S. L., Norioka, S., and Sakiyama, F. (1990) J. Bacteriol., 172, 6506-6511.
17. Epstein, D. M., and Wensink, P. C. (1988) J. Biol. Chem., 263, 16586-16590.
18. Olson, M. O. J., Nagabhushan, N., Dzwiniel, M., and Smillie, L. B. (1970) Nature, 228, 438-442.
19. Brayer, G. D., Delbaere, L. T. J., and James, M. N. G. (1979) J. Mol. Biol., 131, 743-775.
20. Fujinaga, M., Delbaere, L. T. J., Brayer, G. D., and James, M. N. G. (1985) J. Mol. Biol., 183, 479-502.
21. Bone, R., Shenvi, A. B., Kettner, C. A., and Agard, D. A. (1987) Biochemistry, 26, 7609-7614.