Gingipain R

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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[edit]

  1. ^ 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. 
  2. ^ 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. PMID 7857299. doi:10.1006/bbrc.1995.1205. 
  3. ^ 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. PMID 7836351. doi:10.1074/jbc.270.3.1007. 

External links[edit]