Gingipain R
Nowadays, Gingipain R is a topic that has captured the attention of many people around the world. From its origin to its impact on today's society, Gingipain R has played an important role in people's lives. In this article, we will thoroughly explore the different aspects and perspectives related to Gingipain R, analyzing its effects in various areas. From its influence on popular culture to its relevance in past, present and future history, we will dive into a detailed analysis of Gingipain R and its role in today's world. With a critical and reflective look, we will examine the different implications and consequences of Gingipain R, trying to better understand its impact on current society and in the future.
| 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 | ||||||||
| |||||||||
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
- ^ 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.
- ^ 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.
- ^ 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
- Gingipain+R at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
