EC 3.4.22.37 - Gingipain R

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IntEnz Enzyme Nomenclature
EC 3.4.22.37

Names

Accepted name:
gingipain R
Other names:
Arg-gingipain
Arg-gingivain-55 proteinase
Arg-gingivain-70 proteinase
Arg-gingivain-75 proteinase
RGP
RGP-1
argingipain
arginine-specific cysteine protease
arginine-specific gingipain
arginine-specific gingivain
gingipain-1
Systematic name:
-

Reaction

Comments:

A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine [1], and stabilized by Ca2+. Precursor molecule contains a hemagglutinin domain [2, 3]. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of family C25.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
CAS Registry Number: 159745-71-8
UniProtKB/Swiss-Prot:

References

  1. Chen, Z., Potempa, J., Polanowski, A., Wikstrom, M. and Travis, J.
    Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis.
    J. Biol. Chem. 267: 18896-18901 (1992). [PMID: 1527017]
  2. Kirszbaum, L., Sotiropoulos, C., Jackson, C., Cleal, S., Slakeski, N. and Reynolds, E.C.
    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 (1995). [PMID: 7857299]
  3. Pavloff, N., Potempa, J., Pike, R.N., Prochazka, V., Kiefer, M.C., Travis, J. and Barr, P.J.
    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 (1995). [PMID: 7836351]

[EC 3.4.22.37 created 1996]