ENZYME entry: EC 3.4.21.110
| Accepted Name |
| C5a peptidase.
|
| Alternative Name(s) |
| SCP. |
| Streptococcal C5a peptidase. |
| Reaction catalysed |
| The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59 |
| Comment(s) |
- 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.
- Belongs to peptidase family S8A.
|
| Cross-references |
| PROSITE | PDOC00125 |
| BRENDA | 3.4.21.110 |
| EC2PDB | 3.4.21.110 |
| ExplorEnz | 3.4.21.110 |
| PRIAM enzyme-specific profiles | 3.4.21.110 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.21.110 |
| IUBMB Enzyme Nomenclature | 3.4.21.110 |
| IntEnz | 3.4.21.110 |
| MEDLINE | Find literature relating to 3.4.21.110 |
| MetaCyc | 3.4.21.110 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot
entries referenced
in this entry, with possibility to download in different formats, align etc.
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.4.21.-
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-