Gingipain R Explained

Gingipain R
Ec Number:3.4.22.37
Cas Number:159745-71-8

Gingipain R (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 cysteine endopeptidase from the bacterium Porphyromonas gingivalis.

See also

Notes and References

  1. Chen Z, Potempa J, Polanowski A, Wikstrom M, Travis J . Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis . The Journal of Biological Chemistry . 267 . 26 . 18896–901 . September 1992 . 1527017 .
  2. Kirszbaum L, Sotiropoulos C, Jackson C, Cleal S, Slakeski N, Reynolds EC . 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 . February 1995 . 7857299 . 10.1006/bbrc.1995.1205 .
  3. Pavloff N, Potempa J, Pike RN, Prochazka V, Kiefer MC, Travis J, Barr PJ . 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 . January 1995 . 7836351 . 10.1074/jbc.270.3.1007 . free .

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