Gingipain R
Gingipain R | |||||||||
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Identifiers | |||||||||
EC number | 3.4.22.37 | ||||||||
CAS number | 159745-71-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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.; 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.; 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.; 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
- Gingipain R at the US National Library of Medicine Medical Subject Headings (MeSH)
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