Biology:Glutamyl endopeptidase I
Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been identified in species of Staphylococcus, Bacillus, and Streptomyces, among others. The two former are more closely related, while the Streptomyces-type is treated as a separate family, glutamyl endopeptidase II.[1]
Identified proteases
Staphylococcus
- The first discovered enzyme of this family, and the most well characterized, was isolated from the Staphylococcus aureus strain V8, and hence better known as "V8 protease". Other common references to this protease are staphylococcal serine protease, and SspA from its corresponding gene.[1][2][3]
- S. epidermidis glutamyl endopeptidase GluSE[1][4]
- Also called S. epidermidis serine protease (Esp).[3]
- S. warneri glutamyl endopeptidase GluSW[1]
- Also referred to as PROM.[5]
Bacillus
- B. licheniformis glutamyl endopeptidase GluBL[1]
- B. subtilis glutamyl endopeptidase GluBS[1]
- E. faecalis glutamyl endopeptidase SprE[6]
Function
Glutamyl endopeptidase is in at least some species part of a zymogen activation cascade, with its activity being dependent on proteolytic activation of a pre-form of the protease. GluV8 of S. aureus, for example, is dependent of activation by the metalloprotease aureolysin, and is itself needed for activation of staphopain B. GluSE, GluSW and SprE have been observed to be activated by a metalloprotease in a similar fashion.[7][8]
Proteases of this group hydrolyzes peptide bonds after the negatively charged glutamic acid or aspartic acid, with a higher preference to the former. The pH optimum has been found to lie slightly above neutral pH (7-8) for GluV8 and GluBL.[1]
It has been shown that in spite of their similarities, the proteases from different species may differ in their efficiency in cleaving biological targets. The GluV8 is suggested in several mechanisms of S. aureus immune evasion, and GluV8 and GluSE have shown impact on the regulation of biofilms.[3][9][10][11]
See also
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Stennicke, Henning R.; Breddam, Klaus (2013-01-01). Rawlings, Neil D.. ed. Handbook of Proteolytic Enzymes. Academic Press. pp. 2534–2538. doi:10.1016/b978-0-12-382219-2.00561-5. ISBN 9780123822192.
- ↑ Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases" (in en). Proteolytic Enzymes: Serine and Cysteine Peptidases. Methods in Enzymology. 244. pp. 114–126. doi:10.1016/0076-6879(94)44010-7. ISBN 9780121821456. https://archive.org/details/proteolyticenzym0000unse/page/114.
- ↑ 3.0 3.1 3.2 Dubin, Grzegorz (2002-07-01). "Extracellular proteases of Staphylococcus spp". Biological Chemistry 383 (7–8): 1075–1086. doi:10.1515/BC.2002.116. ISSN 1431-6730. PMID 12437090.
- ↑ Ohara-Nemoto, Yuko; Ikeda, Yoriko; Kobayashi, Masahiko; Sasaki, Minoru; Tajika, Shihoko; Kimura, Shigenobu (2002-07-01). "Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis". Microbial Pathogenesis 33 (1): 33–41. doi:10.1006/mpat.2002.0515. ISSN 0882-4010. PMID 12127798.
- ↑ Yokoi, K.; Kakikawa, M.; Kimoto, H.; Watanabe, K.; Yasukawa, H.; Yamakawa, A.; Taketo, A.; Kodaira, K. I. (2001-12-27). "Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M". Gene 281 (1–2): 115–122. doi:10.1016/S0378-1119(01)00782-X. ISSN 0378-1119. PMID 11750133.
- ↑ Kawalec, Magdalena; Potempa, Jan; Moon, Jonathan L.; Travis, James; Murray, Barbara E. (2005-01-01). "Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities". Journal of Bacteriology 187 (1): 266–275. doi:10.1128/JB.187.1.266-275.2005. ISSN 0021-9193. PMID 15601711.
- ↑ Chao, Yun-Peng; Fu, Hongyong; Wang, Yu-Ling; Huang, Wen-Bin; Wang, Jen-You (2003-09-01). "Molecular cloning of the carboxylesterase gene and biochemical characterization of the encoded protein from Pseudomonas citronellolis ATCC 13674". Research in Microbiology 154 (7): 521–526. doi:10.1016/S0923-2508(03)00144-X. ISSN 0923-2508. PMID 14499938.
- ↑ Yokoi, Ken-Ji; Kuzuwa, Shinya; Iwasaki, Shu-Ichi; Yamakawa, Ayanori; Taketo, Akira; Kodaira, Ken-Ichi (2016-06-01). "Aureolysin of Staphylococcus warneri M accelerates its proteolytic cascade, and participates in biofilm formation". Bioscience, Biotechnology, and Biochemistry 80 (6): 1238–1242. doi:10.1080/09168451.2016.1148576. ISSN 1347-6947. PMID 27008278.
- ↑ Iwase, Tadayuki; Uehara, Yoshio; Shinji, Hitomi; Tajima, Akiko; Seo, Hiromi; Takada, Koji; Agata, Toshihiko; Mizunoe, Yoshimitsu (2010-05-20). "Staphylococcus epidermidis Esp inhibits Staphylococcus aureus biofilm formation and nasal colonization". Nature 465 (7296): 346–349. doi:10.1038/nature09074. ISSN 1476-4687. PMID 20485435. Bibcode: 2010Natur.465..346I.
- ↑ Koziel, Joanna; Potempa, Jan (2013-02-01). "Protease-armed bacteria in the skin". Cell and Tissue Research 351 (2): 325–337. doi:10.1007/s00441-012-1355-2. ISSN 1432-0878. PMID 22358849.
- ↑ Chen, Chen; Krishnan, Vengadesan; Macon, Kevin; Manne, Kartik; Narayana, Sthanam V. L.; Schneewind, Olaf (2013-10-11). "Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus". The Journal of Biological Chemistry 288 (41): 29440–29452. doi:10.1074/jbc.M113.502039. ISSN 1083-351X. PMID 23970550.
External links
- Staphylococcus aureus glutamyl endopeptidase at Universal Protein Resource (UniProt).
- Bacillus licheniformis glutamyl endopeptidase at Universal Protein Resource (UniProt).
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