Gingipain K
| Gingipain K | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.47 | ||||||||
| CAS number | 159745-69-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Gingipain K (EC 3.4.22.47, Lys-gingipain, PrtP proteinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Endopeptidase with strict specificity for lysyl bonds
Activity of this enzyme is stimulated by glycine.
References
- ↑ Pike, R.; McGraw, W.; Potempa, J.; Travis, J. (1994). "Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins". J. Biol. Chem. 269: 406–411. PMID 8276827.
- ↑ Curtis, M.A.; Aduse, O.J.; Rangarajan, M.; Gallagher, A.; Sterne, J.A.; Reid, C.R.; Evans, H.E.; Samuelsson, B. (2002). "Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor 2". Infect. Immun. 70: 6968–6975. doi:10.1128/iai.70.12.6968-6975.2002. PMC 132948. PMID 12438376.
External links
- Gingipain+K at the US National Library of Medicine Medical Subject Headings (MeSH)
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