C5a peptidase

Identifiers

Databases

PDB structures

C5a peptidase (EC 3.4.21.110, streptococcal C5a peptidase, ScpA, ScpB, SCPA) is an enzyme.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

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

This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate preference.

References

↑ Wexler, D.E.; Chenoweth, D.E.; Cleary, P.P. (1985). "Mechanism of action of the group A streptococcal C5a inactivator". Proc. Natl. Acad. Sci. USA. 82: 8144–8148. doi:10.1073/pnas.82.23.8144. PMC 391459. PMID 3906656.
↑ Bohnsack, J.F.; Mollison, K.W.; Buko, A.M.; Ashworth, J.C.; Hill, H.R. (1991). "Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus". Biochem. J. 273: 635–640. PMC 1149811. PMID 1996961.
↑ Cleary, P.P.; Prahbu, U.; Dale, J.B.; Wexler, D.E.; Handley, J. (1992). "Streptococcal C5a peptidase is a highly specific endopeptidase". Infect. Immun. 60 (12): 5219–5223. PMID 1452354.
↑ Anderson, E.T.; Wetherell, M.G.; Winter, L.A.; Olmsted, S.B.; Cleary, P.P.; Matsuka, Y.V. (2002). "Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes". Eur. J. Biochem. 269 (19): 4839–4851. doi:10.1046/j.1432-1033.2002.03183.x. PMID 12354115.
↑ Stafslien, D.K.; Cleary, P.P. (2000). "Characterization of the streptococcal C5a peptidase using a C5a-green fluorescent protein fusion protein substrate". J. Bacteriol. 182 (11): 3254–3258. doi:10.1128/jb.182.11.3254-3258.2000. PMID 10809707.
↑ Terao, Y.; Yamaguchi, M.; Hamada, S.; Kawabata, S. (2006). "Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils". J. Biol. Chem. 281 (20): 14215–14223. doi:10.1074/jbc.M513408200. PMID 16565520.

C5a peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)

Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic

Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator

Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase

Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin

Venombin	Ancrod Batroxobin

Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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