From Wikipedia, the free encyclopedia
Gingipain R
Identifiers
EC no. 3.4.22.37
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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. ^ 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. 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. 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.

External links

From Wikipedia, the free encyclopedia
Gingipain R
Identifiers
EC no. 3.4.22.37
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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. ^ 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. 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. 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.

External links


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