Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases

Biological Chemistry

Volumn 390, Issue 3, 2009, Pages 277-285

  Nemoto, Takayuki K ^a   Ono, Toshio ^a   Shimoyama, Yu ^b   Kimura, Shigenobu ^b   Ohara Nemoto, Yuko ^a  

^a NAGASAKI UNIVERSITY GRADUATE SCHOOL OF BIOMEDICAL SCIENCES   (Japan)

^b IWATE MEDICAL UNIVERSITY   (Japan)

Author keywords

Glutamyl endopeptidase; Staphylococcus aureus; Staphylococcus epidermidis; Substrate binding pocket; V8 protease

Indexed keywords

AMINO ACID; GLUTAMYL ENDOPEPTIDASE; PROTEIN GLUSE; PROTEIN GLUSW; PROTEIN GLUV8; PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CHIMERA; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; STAPHYLOCOCCUS WARNERI;

AMINO ACID SEQUENCE; AMINO ACIDS; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; STAPHYLOCOCCUS;

STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; STAPHYLOCOCCUS WARNERI;

EID: 62249170043     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.027     Document Type: Article

References (24)

1. Breddam, K. and Meldal, M. (1992). Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biol. 206, 103-107.
2. Carmona, C. and Gray, G.L. (1987). Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8. Nucleic Acids Res. 15, 6757.
3. Coulter, S.N., Schwan, W.R., Ng, E.Y., Langhorne, M.H., Ritchie, H.D., Westbrock-Wadman, S., Hufnagle, W.O., Folger, K.R., Bayer, A.S., and Stover, C.K. (1998). Staphylococcus aureus genetic loci impacting growth and survival in multiple infection environments. Mol. Microbiol. 30, 393-404.
4. Demidyuk, I.V., Romanova, D.V., Nosovskaya, E.A., Chestukhina, G.G., Kuranova, I.P., and Kostrov, S.V. (2004) Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius. Protein Eng. Des. Sel. 17, 411-416.
5. Drapeau, G.R. (1978). Role of a metalloprotease in activation of the precursor of Staphylococcal protease. J. Bacteriol. 136, 607-613.
6. Drapeau, G.R., Boily, Y., and Houmard, J. (1972). Purification and properties of an extracellular protease of Staphylococcus aureus. J. Biol. Chem. 247, 6720-6726.
7. Fontana, A. (1988). Structure and stability of thermophilic enzymes: studies on thermolysin. Biophys. Chem. 29, 181-193.
8. Kakudo, S., Kikuchi, N., Kitadokoro, K., Fujiwara, T., Nakamura, E., Okamoto, H., Shin, M., Tamaki, M., Teraoka, H., Tsuzuki, H., et al. (1992). Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCC 14580. J. Biol. Chem. 267, 23782-23788.
9. Karlsson, A., Saravia-Otten, P., Tegmark, K., Morfeldt, E., and Arvidson, S. (2001). Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases. Infect. Immun. 69, 4742-4748.
10. Meijers, R., Blagova, E.V., Levdikov, V.M., Rudenskaya, G.N., Chestukhina, G.G., Akimkina, T.V., Kostrov, S.V., Lamzin, V.S., and Kuranova, I.P. (2004). The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation. Biochemistry 43, 2784-2791.
11. Nemoto, T.K., Ohara-Nemoto, Y., Ono, T., Kobayakawa, T., Shimoyama, Y., Kimura, S., and Takagi, T. (2008). Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. FEBS J. 275, 573-587.
12. Nickerson, N.N., Prasad, L., Jacob, L., Delbaere, L.T., and McGavin, M.J. (2007). Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing. J. Biol. Chem. 282, 34129-34138.
13. Ohara-Nemoto, Y., Ikeda, Y., Kobayashi, M., Sasaki, M., Tajika, S., and Kimura, S. (2002). Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. Microb. Pathog. 33, 33-41.
14. Ohara-Nemoto, Y., Ono, T., Shimoyama, Y., Kimura, S., and Nemoto, T.K. (2008). Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis. Biol. Chem. 389, 1207-1219.
15. Ono, T., Nemoto, T.K., Shimoyama, Y., Kimura, S., and Ohara-Nemoto, Y. (2008). An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation. Anal. Biochem. 381, 74-80.
16. Prasad, L., Leduc, Y., Hayakawa, K., and Delbaere, L.T. (2004). The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus. Acta Cryst. 60, 256-259.
17. Rebrikov, D.V., Akimkina, T.V., Shevelev, A.B., Demidyuk, I.V., Bushueva, A.M., Kostrov, S.V., Chestukhina, G.G., and Stepanov, V.M. (1999). Bacillus intermedius glutamyl endopeptidase. Molecular cloning and nucleotide sequence of the structural gene. J. Protein Chem. 18, 21-27.
18. Rice, K., Peralta, R., Bast, D., Azavedo, J., and McGavin, M. (2001). Description of Staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. Infect. Immun. 69, 159-169.
19. Stennicke, H.R. and Breddam, K. (1998). Glutamyl endopeptidase I. In: Handbook of Proteolytic Enzymes, A.J. Barrett, N.D. Rawlings and F.F. Woessner, Jr. eds. (San Diego, CA, USA: Academic Press), pp. 243-246.
20. Suzuki, Y., Yabuta, M., and Ohsuye, K. (1994). Cloning and expression of the gene encoding the glutamic acid-specific protease from Streptomyces griseus ATCC10137. Gene 150, 149-151.
21. Svendsen, I. and Breddam, K. (1992). Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. Eur. J. Biochem. 204, 165-171.
22. Svendsen, I., Jensen, M.R., and Breddam, K. (1991). The primary structure of the glutamic acid-specific protease of Streptomyces griseus. FEBS Lett. 292, 165-167.
23. Yabuta, M., Ochi, M., and Ohsuye, K. (1995). Hyperproduction of a recombinant fusion protein of Staphylococcus aureus V8 protease in Escherichia coli and its processing by OmpT protease to release an active V8 protease derivative. Appl. Microbiol. Biotech. 44, 118-125.
24. Yokoi, K., Kakikawa, M., Kimoto, H., Watanabe, K., Yasukawa, H., Yamakawa, A., Taketo, A., and Kodaira, K. (2001). Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M. Gene 281, 115-122.