C5a peptidase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.110 C5a peptidase
C5a peptidase is a surface-associated subtilisin-like serine peptidase in family S8A with very specific substrate specificity; virulent streptococci including Streptococcus pyogenes evade human detection and phagocytosis by destroying the complement chemotaxin C5a, and cleavage of human C5a reduces its ability to bind receptors on polymorphonuclear neutrophils, abolishing chemotaxis; the primary cleavage site is at His67-Lys68 in human C5a, with a minor secondary site at Ala58-Ser59. By destroying C5a it enables streptococcal immune evasion. It appears in viruses and cellular organisms.
C5a peptidase is a surface-associated subtilisin-like serine peptidase in family S8A with very specific substrate specificity; virulent streptococci including Streptococcus pyogenes evade human detection and phagocytosis by destroying the complement chemotaxin C5a, and cleavage of human C5a reduces its ability to bind receptors on polymorphonuclear neutrophils, abolishing chemotaxis; the primary cleavage site is at His67-Lys68 in human C5a, with a minor secondary site at Ala58-Ser59. By destroying C5a it enables streptococcal immune evasion. It appears in viruses and cellular organisms.
References:
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[3]. Tanaka T., et al.
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