ExplorEnz: EC 3.4.21.110

Your query returned 1 entry. Printable version

3.4.21.110

Accepted name:

C5a peptidase

Reaction:

The primary cleavage site is at His⁶⁷┼Lys⁶⁸ in human C5a with a minor secondary cleavage site at Ala⁵⁸┼Ser⁵⁹

Other name(s):

streptococcal C5a peptidase; ScpA; ScpB; SCPA

Comments:

This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate specificity. Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties [1,4]. Belongs in peptidase family S8A.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 100179-39-3

References:

1.	Wexler, D.E., Chenoweth, D.E. and Cleary, P.P. Mechanism of action of the group A streptococcal C5a inactivator. Proc. Natl. Acad. Sci. USA 82 (1985) 8144–8148. [DOI] [PMID: 3906656]
2.	Bohnsack, J.F., Mollison, K.W., Buko, A.M., Ashworth, J.C. and Hill, H.R. Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus. Biochem. J. 273 (1991) 635–640. [PMID: 1996961]
3.	Cleary, P.P., Prahbu, U., Dale, J.B., Wexler, D.E. and Handley, J. Streptococcal C5a peptidase is a highly specific endopeptidase. Infect. Immun. 60 (1992) 5219–5223. [PMID: 1452354]
4.	Anderson, E.T., Wetherell, M.G., Winter, L.A., Olmsted, S.B., Cleary, P.P. and Matsuka, Y.V. Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes. Eur. J. Biochem. 269 (2002) 4839–4851. [DOI] [PMID: 12354115]
5.	Stafslien, D.K. and Cleary, P.P. Characterization of the streptococcal C5a peptidase using a C5a-green fluorescent protein fusion protein substrate. J. Bacteriol. 182 (2000) 3254–3258. [DOI] [PMID: 10809707]
6.	Terao, Y., Yamaguchi, M., Hamada, S. and Kawabata, S. Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J. Biol. Chem. 281 (2006) 14215–14223. [DOI] [PMID: 16565520]

[EC 3.4.21.110 created 2006]