| Gingipain K | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.22.47 | ||||||||
| CAS no. | 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. This enzyme catalyses the following chemical reaction:
- Endopeptidase with strict specificity for lysyl bonds
Activity of this enzyme is stimulated by glycine.
See also
References
- Pike R, McGraw W, Potempa J, Travis J (January 1994). "Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins". The Journal of Biological Chemistry. 269 (1): 406–11. PMID 8276827.
- Curtis MA, Aduse Opoku J, Rangarajan M, Gallagher A, Sterne JA, Reid CR, Evans HE, Samuelsson B (December 2002). "Attenuation of the virulence of Porphyromonas gingivalis by using a specific synthetic Kgp protease inhibitor". Infection and Immunity. 70 (12): 6968–75. doi:10.1128/iai.70.12.6968-6975.2002. PMC 132948. PMID 12438376.
External links
- Gingipain+K at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Proteases: cysteine proteases (EC 3.4.22) | |
|---|---|
| Caspase | |
| Fruit-derived | |
| Calpain | |
| Cathepsin | |
| Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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