Biology:Gingipain R

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Short description: Class of enzymes
Gingipain R
Identifiers
EC number3.4.22.37
CAS number159745-71-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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 cysteine endopeptidase from the bacterium Porphyromonas gingivalis.

See also

References

  1. "Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis". The Journal of Biological Chemistry 267 (26): 18896–901. September 1992. PMID 1527017. 
  2. "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. doi:10.1006/bbrc.1995.1205. PMID 7857299. 
  3. "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. doi:10.1074/jbc.270.3.1007. PMID 7836351. 

External links