Gingipain R
Gingipain R (EC 3.4.22.37, Arg-gingipain, gingipain-1, argingipain, Arg-gingivain-55 proteinase, Arg-gingivain-70 proteinase, Arg-gingivain-75 proteinase, arginine-specific cysteine protease, arginine-specific gingipain, arginine-specific gingivain, RGP-1, RGP) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction:
- Hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1 (position 1)
This enzyme is secreted endopeptidase from the bacterium Porphyromonas gingivalis.
References
- ↑ Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M. and Travis, J. (1992). "Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis". J. Biol. Chem. 267: 18896–18901. PMID 1527017.
- ↑ Kirszbaum, L., Sotiropoulos, C., Jackson, C., Cleal, S., Slakeski, N. and Reynolds, E.C. (1995). "Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain". Biochem. Biophys. Res. Commun. 207: 424–431. doi:10.1006/bbrc.1995.1205. PMID 7857299.
- ↑ Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. and Barr, P.J. (1995). "Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein". J. Biol. Chem. 270: 1007–1010. doi:10.1074/jbc.270.3.1007. PMID 7836351.
External links
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|