Gingipain R

Gingipain R
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

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

  1. 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.
  2. 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.
  3. 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

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