Biology:Gingipain R
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Short description: Class of enzymes
| Gingipain R | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.37 | ||||||||
| CAS number | 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 | ||||||||
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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:
- 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
- ↑ "Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis". The Journal of Biological Chemistry 267 (26): 18896–901. September 1992. doi:10.1016/S0021-9258(19)37045-0. PMID 1527017.
- ↑ "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. Bibcode: 1995BBRC..207..424K.
- ↑ "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
- Gingipain+R at the US National Library of Medicine Medical Subject Headings (MeSH)
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