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Gene Review

SAB1253  -  peptidase

Staphylococcus aureus RF122

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Disease relevance of SAB1253


High impact information on SAB1253

  • Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan [6].
  • The NH2 terminus of bLPL was determined to be Asp by sequencing the intact protein with a gas phase sequencer for up to 30 residues, whereas the COOH terminus was identified as Gly through, carboxyl peptidase Y cleavage [7].
  • Sortase acts on surface proteins that are initiated into the secretion (Sec) pathway and have their signal peptide removed by signal peptidase [8].
  • Mutations were also obtained in recA and lsp (encoding the S. aureus prolipoprotein signal peptidase) [9].
  • Although lysostaphin, the prototypical peptidase in the group, is widely used as a tool in biotechnology and developed as an antistaphylococcal agent, the detailed structure of this enzyme is unknown [10].

Chemical compound and disease context of SAB1253


Biological context of SAB1253


Anatomical context of SAB1253

  • Lysostaphin, a peptidase produced by Staphylococcus simulans, specifically cleaves the glycine-glycine bonds unique to the interpeptide cross-bridge of the S. aureus cell wall [16].

Associations of SAB1253 with chemical compounds

  • The NH2 terminus of the thioesterase domain was determined to be lysine by sequencing the whole domain up to 20 residues while the COOH terminus was identified as serine through carboxyl peptidase Y cleavage [17].
  • The biosynthetic incorporation of selenomethionine and telluromethionine into pyrrolidone carboxyl peptidase (PYRase) from S. aureus [13].

Analytical, diagnostic and therapeutic context of SAB1253


  1. Discovery of substrate for type I signal peptidase SpsB from Staphylococcus aureus. Sharkov, N.A., Cai, D. J. Biol. Chem. (2002) [Pubmed]
  2. Papillon-Lefèvre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans. Pham, C.T., Ivanovich, J.L., Raptis, S.Z., Zehnbauer, B., Ley, T.J. J. Immunol. (2004) [Pubmed]
  3. Regulated expression of the Escherichia coli lepB gene as a tool for cellular testing of antimicrobial compounds that inhibit signal peptidase I in vitro. Barbosa, M.D., Lin, S., Markwalder, J.A., Mills, J.A., DeVito, J.A., Teleha, C.A., Garlapati, V., Liu, C., Thompson, A., Trainor, G.L., Kurilla, M.G., Pompliano, D.L. Antimicrob. Agents Chemother. (2002) [Pubmed]
  4. Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus. Cregg, K.M., Wilding, I., Black, M.T. J. Bacteriol. (1996) [Pubmed]
  5. Staphylolytic enzyme from Pseudomonas aeruginosa: characterization and immunocytochemical localization. Carnicero, A., Mansito, T.B., Roldán, J.M., Falcón, M.A. Arch. Microbiol. (1990) [Pubmed]
  6. Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan. Odintsov, S.G., Sabała, I., Bourenkov, G., Rybin, V., Bochtler, M. J. Biol. Chem. (2005) [Pubmed]
  7. Structure of bovine milk lipoprotein lipase. Yang, C.Y., Gu, Z.W., Yang, H.X., Rohde, M.F., Gotto, A.M., Pownall, H.J. J. Biol. Chem. (1989) [Pubmed]
  8. Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mazmanian, S.K., Ton-That, H., Schneewind, O. Mol. Microbiol. (2001) [Pubmed]
  9. Identification of Staphylococcus aureus virulence genes in a murine model of bacteraemia using signature-tagged mutagenesis. Mei, J.M., Nourbakhsh, F., Ford, C.W., Holden, D.W. Mol. Microbiol. (1997) [Pubmed]
  10. Crystal structures of active LytM. Firczuk, M., Mucha, A., Bochtler, M. J. Mol. Biol. (2005) [Pubmed]
  11. Isolation and characterization of pcp, a gene encoding a pyrrolidone carboxyl peptidase in Staphylococcus aureus. Patti, J.M., Schneider, A., Garza, N., Boles, J.O. Gene (1995) [Pubmed]
  12. Synthesis and antimicrobial activity of novel globomycin analogues. Kiho, T., Nakayama, M., Yasuda, K., Miyakoshi, S., Inukai, M., Kogen, H. Bioorg. Med. Chem. Lett. (2003) [Pubmed]
  13. The biosynthetic incorporation of selenomethionine and telluromethionine into pyrrolidone carboxyl peptidase (PYRase) from S. aureus. Boles, J.O., Yu, H.N., Patti, J.M. SAAS Bull. Biochem. Biotechnol. (1997) [Pubmed]
  14. Pyrrolidone carboxyl peptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: cloning and overexpression in Escherichia coli of the gene, and its application to protein sequence analysis. Tsunasawa, S., Nakura, S., Tanigawa, T., Kato, I. J. Biochem. (1998) [Pubmed]
  15. Purification and peptidase activity of a bacteriolytic extracellular enzyme from Pseudomonas aeruginosa. Brito, N., Falcón, M.A., Carnicero, A., Gutiérrez-Navarro, A.M., Mansito, T.B. Res. Microbiol. (1989) [Pubmed]
  16. Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis. Climo, M.W., Patron, R.L., Goldstein, B.P., Archer, G.L. Antimicrob. Agents Chemother. (1998) [Pubmed]
  17. Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase. Yang, C.Y., Huang, W.Y., Chirala, S., Wakil, S.J. Biochemistry (1988) [Pubmed]
  18. Amino acid sequence and post-translational modification of stem cell factor isolated from buffalo rat liver cell-conditioned medium. Lu, H.S., Clogston, C.L., Wypych, J., Fausset, P.R., Lauren, S., Mendiaz, E.A., Zsebo, K.M., Langley, K.E. J. Biol. Chem. (1991) [Pubmed]
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