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:
This enzyme is secreted cysteine endopeptidase from the bacterium Porphyromonas gingivalis .
Cathepsin S is a protein that in humans is encoded by the CTSS gene. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
Clostripain is a proteinase that cleaves proteins on the carboxyl peptide bond of arginine. It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9, and optimum pH is 7.4~7.8. The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.
Porphyromonas gingivalis belongs to the phylum Bacteroidota and is a nonmotile, Gram-negative, rod-shaped, anaerobic, pathogenic bacterium. It forms black colonies on blood agar.
Kexin is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast. It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes. The enzyme is encoded by the yeast gene KEX2, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease subtilisin. The first mammalian homologue of this protein to be identified was furin. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.
In enzymology, arginine kinase is an enzyme that catalyzes the chemical reaction
Nepenthesin is an aspartic protease of plant origin that has so far been identified in the pitcher secretions of Nepenthes and in the leaves of Drosera peltata. It is similar to pepsin, but differs in that it also cleaves on either side of Asp residues and at Lys┼Arg. While more pH and temperature stable than porcine pepsin A, it is considerably less stable in urea or guanidine hydrochloride. It is the only known protein with such a stability profile.
IgA protease is an enzyme. This enzyme catalyses the following chemical reaction[reaction equation needed]
Xaa-Xaa-Pro tripeptidyl-peptidase is an enzyme. It catalyses the following chemical reaction
Glutamyl endopeptidase is an extracellular bacterial serine protease of the glutamyl endopeptidase I family that was initially isolated from the Staphylococcus aureus strain V8. The protease is, hence, commonly referred to as "V8 protease", or alternatively SspA from its corresponding gene.
Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Kallikrein 13 is an enzyme. This enzyme catalyses hydrolyses mouse Ren2 protein on the carboxy side of the arginine residue at the Lys-Arg- pair in the N-terminus, to yield mature renin.
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Gingipain K is an enzyme. This enzyme catalyses the following chemical reaction
Staphopain is an enzyme. This enzyme catalyses the following chemical reaction
Procollagen C-endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Proteasome endopeptidase complex is an enzyme. This enzyme catalyses the following chemical reaction
The PA clan is the largest group of proteases with common ancestry as identified by structural homology. Members have a chymotrypsin-like fold and similar proteolysis mechanisms but can have identity of <10%. The clan contains both cysteine and serine proteases. PA clan proteases can be found in plants, animals, fungi, eubacteria, archaea and viruses.
Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been identified in species of Staphylococcus, Bacillus, and Streptomyces, among others. The two former are more closely related, while the Streptomyces-type is treated as a separate family, glutamyl endopeptidase II.
Staphopain A is a secreted cysteine protease produced by Staphylococcus aureus. It was first identified in the S. aureus V8 strain as a papain-like cysteine protease. The protease distinguishes itself from the other major proteases of S. aureus in its very broad specificity and its ability to degrade elastin.
Asparagine endopeptidase is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN, vicilin peptidohydrolase and bean endopeptidase. In humans it is encoded by the LGMN gene.