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, Travis J (September 1992). "Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis". The Journal of Biological Chemistry. 267 (26): 18896–901. PMID 1527017.
  2. ↑ Kirszbaum L, Sotiropoulos C, Jackson C, Cleal S, Slakeski N, Reynolds EC (February 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". Biochemical and Biophysical Research Communications. 207 (1): 424–31. doi:10.1006/bbrc.1995.1205. PMID 7857299.
  3. ↑ Pavloff N, Potempa J, Pike RN, Prochazka V, Kiefer MC, Travis J, Barr PJ (January 1995). "Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein". The Journal of Biological Chemistry. 270 (3): 1007–10. doi:10.1074/jbc.270.3.1007. PMID 7836351.
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