Gingipain R

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Gingipain R
Identifiers
EC no. 3.4.22.37
CAS no. 159745-71-8
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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:

Contents

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

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. doi: 10.1016/S0021-9258(19)37045-0 . 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. Bibcode:1995BBRC..207..424K. 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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