Role of calcium in activity and stability of the Lactococcus lactis cell envelope proteinase

Applied and Environmental Microbiology

Volumn 65, Issue 4, 1999, Pages 1390-1396

  Exterkate, Fred A ^a   Alting, Arno C ^a  

^a NIZO FOOD RESEARCH   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CALCIUM ION; IMIDAZOLE; PROTEINASE;

ARTICLE; BACTERIAL MEMBRANE; CATALYSIS; ENZYME ASSAY; ENZYME SPECIFICITY; LACTOCOCCUS; LACTOCOCCUS LACTIS; NONHUMAN; PROTEIN DEGRADATION;

BACTERIA (MICROORGANISMS); LACTOCOCCUS; LACTOCOCCUS LACTIS; POSIBACTERIA; STREPTOCOCCUS;

EID: 0032962740     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.4.1390-1396.1999     Document Type: Article

References (35)

1. Bajorath, J., W. Hinrichs, and W. Saenger. 1988. The enzymatic activity of proteinase K is controlled by calcium. Eur. J. Biochem. 176:441-447.
2. Bajorath, J., S. Raghunathan, W. Hinrichs, and W. Saenger. 1989. Long-range structural changes in proteinase K triggered by calcium ion removal. Nature 337:481-484.
3. Briedigkeit, L., and C. Frömmel. 1989. Calcium ion binding by thermitase. FEBS Lett. 253:83-87.
4. Bruinenberg, P. G., W. M. de Vos, and R. J. Siezen. 1994. Prevention of C-terminal autoprocessing of Lactococcus lactis SK11 cell-envelope proteinuse by engineering of an essential surface loop. Biochem. J. 302:957-963.
5. Coolbear, T., J. R. Reid, and G. G. Pritchard. 1992. Stability and specificity of the cell wall-associated proteinase from Lactococcus lactis subsp. cremoris H2 released by treatment with lysozyme in the presence of calcium. Appl. Environ. Microbiol. 58:3263-3270.
6. Exterkate, F. A. 1979. Accumulation of proteinase in the cell wall of Streptococcus cremoris AM1 and regulation of its production. Arch. Microbiol. 120:247-254.
7. Exterkate, F. A. 1984. Location of peptidases outside and inside the membrane of Streptococcus cremoris. Appl. Environ. Microbiol. 47:177-183.
8. Exterkate, F. A. 1990. Differences in short peptide-substrate cleavage by two cell-envelope-located serine proteinases of Lactoccus lactis subsp. cremoris are related to secondary binding specificity. Appl. Microbiol. Biotechnol. 33: 401-406.
9. Exterkate, F. A. 1995. The lactococcal cell-envelope proteinases: differences, calcium-binding effects and role in cheese ripening. Int. Dairy J. 5:995-1018.
10. Exterkate, F. A., and G. J. C. M. de Veer. 1985. Partial isolation of and degradation of caseins by cell wall proteinase(s) of Streptococcus, cremoris HP. Appl. Environ. Microbiol. 49:328-332.
11. II of strain HP. Syst. Appl. Microbiol. 11:108-115.
12. s1-casein-(1-23)-fragment by the free and bound form of the cell-envelope proteinase of Lactococcus lactis subsp. cremoris under conditions prevailing in cheese. Syst. Appl. Microbiol. 16:1-8.
13. s1-casein-(1-23)-fragment. Biochem. J. 273:135-139.
14. Exterkate, F. A., A. C. Alting, and P. G. Bruinenberg. 1993. Diversity of cell envelope proteinase specificity among strains of Lactococcus locus and its relationship to charge characteristics of the substrate-binding region. Appl. Environ. Microbiol. 59:3640-3647.
15. Exterkate, F. A. 1996. Unpublished results.
16. Genov, N., B. Filippi, P. Dolashka, K. S. Wilson, and C. Betzel. 1995. Stability of subtilisins and related proteinases (subtilases). Int. J. Pept. Protein Res. 45:391-400.
17. Gros, P., C. Betzel, Z. Dauter, K. S. Wilson, and W. G. J. Hol. 1989. Molecular dynamics refinement of thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content. J. Mol. Biol. 210:347-367.
18. Gros, P., K. H. Kalk, and W. G. J. Hol. 1991. Calcium binding to thermitase. Cristallographic studies of thermitase at 0. 5 and 100 mM calcium. J. Biol. Chem. 266:2953-2961.
19. Hugenholtz, J., H. Veldkamp, and W. N. Konings. 1987. Detection of specific strains and variants of Streptococcus cremoris in mixed cultures by immunofluorescence. Appl. Environ. Microbiol. 53:149-155.
20. 2+-binding site of subtilisin J by site-directed mutagenesis on heat stability. Biochem. Biophys. Res. Commun. 188:184-189.
21. Kok, J. 1990. Genetics of the proteolytic system of lactic acid bacteria. FEMS Microbiol. Rev. 87:15-42.
22. Kok, J., and W. M. de Vos. 1994. The proteolytic system of lactic acid bacteria, p. 169-210. In M. J. Gasson and W. M. de Vos (ed.), Genetics and biotechnology of lactic acid bacteria. Blackie Academic and Professional, Glasgow, United Kingdom.
23. Kok, J., D. Hill, A. J. Haandrikman, M. J. B. de Reuver, H. Laan, and G. Venema. 1988. Deletion analysis of the proteinase gene of Streptococcus cremoris Wg2. Appl. Environ. Microbiol. 54:239-244.
24. Laan, H., and W. N. Konings. 1989. Mechanism of proteinase release from Lactococcus lactis subsp. cremoris. Appl. Environ. Microbiol. 55:3101-3106.
25. Meloun, B., M. Baudjš, V. Kostka, G. Hausdorf, C. Frömmel, and W. E. Höhne. 1985. Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-like proteinases. FEBS Lett. 183:195-200.
26. Mills, O. E., and T. D. Thomas. 1978. Release of cell wall-associated proteinase(s) from lactic streptococci. N. Z. J. Dairy Sci. Technol. 13:209-215.
27. Nissen-Meyer, J., and K. Sletten. 1991. Purification and characterization of the free form of the lactococcal extracellular proteinase and its autoproteolytic cleavage products. J. Gen. Microbiol. 137:1611-1618.
28. Pantoliano, M. W., M. Whitlow, J. F. Wood, M. L. Rollence, B. C. Finzel, G. L. Gilliland, T. L. Poulos, and P. N. Bryan. 1988. The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case. Biochemistry 27:8311-8317.
29. Pritchard, G. G., and T. Coolbear. 1993. The physiology and biochemistry of the proteolytic system in lactic acid bacteria. FEMS Microbiol. Rev. 12:179-206.
30. Siezen, R. J., W. M. de Vos, J. A. M. Leunissen, and B. W. Dijkstra. 1991. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4:719-737.
31. Siezen, R. J., P. G. Bruinenberg, P. Vos, I. van Alen-Boerrigter, M. Nijhuis, A. C. Alting, F. A. Exterkate, and W. M. de Vos. 1993. Engineering of the substrate-binding region of the subtilisin-like cell-envelope proteinase of Lactococcus lactis. Protein Eng. 6:927-937.
32. Stuart, D. I., K. R. Acharya, N. P. C. Walker, S. G. Smith, M. Lewis, and D. C. Phillips. 1986. α-Lactalbumin possesses a novel calcium binding loop. Nature (London) 324:84-87.
33. Vos, P., G. Simons, R. J. Siezen, and W. M. de Vos. 1989. Primary structure and organization of the gene for a procaryotic cell-envelope-located serine proteinase. J. Biol. Chem. 264:13579-13585.
34. Vos, P., I. J. Boerrigter, G. Buist, A. J. Haandrikman, M. Nijhuis, M. B. de Reuver, R. J. Siezen, G. Venema, W. M. de Vos, and J. Kok. 1991. Engineering of the Lactococcus lactis serine proteinase by construction of hybrid enzymes. Protein Eng. 4:479-484.
35. Wells, J. A., and D. A. Estell. 1988. Subtilisin - an enzyme designed to be engineered. Trends Biochem. Sci. 13:291-297.