Gingipain K | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.22.47 | ||||||||
CAS no. | 159745-69-4 | ||||||||
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 K (EC 3.4.22.47, Lys-gingipain, PrtP proteinase) is an enzyme. [1] [2] This enzyme catalyses the following chemical reaction
Activity of this enzyme is stimulated by glycine.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Cathelicidin antimicrobial peptide (CAMP) is a polypeptide that is primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs); in humans, the CAMP gene encodes the peptide precursor CAP-18, which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37. LL-37 is the only peptide in the Cathelicidin family found in the human body.
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.
In molecular biology, Proteinase K is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Parengyodontium album. Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons.
Prevotella is a genus of Gram-negative bacteria.
Porphyromonas is a Gram-negative, non-spore-forming, obligately anaerobic and non-motile genus from the family Porphyromonadaceae. There were 16 different Porphyromonas species documented as of 2015, which reside in both animal and human reservoirs. It was discovered more recently that Porphyromonas also exist in the environment, albeit to a lesser extent. This genus is notably implicated in the modulation of oral cavity, respiratory tract, and gastrointestinal tract disease states. It is suggested that Porphyromonas either operate as benign bacteria pertinent to host immunity or are potential pathobionts that opportunistically provoke diseased states when homeostasis is disrupted. Despite its characterization not being fully elucidated due to sparse research, various studies report the prevalence of this genus at 58.7% in healthy states compared with 41.3% in diseased states.
The red complex is a group of bacteria that are categorized together based on their association with severe forms of periodontal disease. The red complex—among a number of other complexes—were classified by Sigmund Socransky in 1998.
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.
Gingipains are a family of proteases secreted by Porphyromonas gingivalis. Among other functions, it works to degrade cytokines, thereby downregulating the host response in the form of reduced inflammation. Gingipain has been studied for its potential role in the development of Alzheimer's disease.
Xaa-Xaa-Pro tripeptidyl-peptidase is an enzyme. It catalyses the following chemical reaction
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Gingipain R is an enzyme. This enzyme catalyses the following chemical reaction:
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Prevotella nigrescens is a species of bacterium. Prevotella nigrescens has a gram negative gram stain. When P. nigrescens microflora colonize they trigger an over-aggressive response from the immune system and increase the incidence of many diseases and infections. One specific type of bacteria that is part of the normal oral flora but leads to disease when it infects the local tissue. This bacteria has no means of motility and has a Bacilli (rod) shape. Prevotella species are part of the human oral and vaginal flora. They play a role in the pathogenesis of periodontal disease, gingivitis, and extraoral infections such as nasopharyngeal and intra-abdominal infections also some odontogenic infections, and strains are usually carried in families, in so-called intrafamilial carriage. It is also associated with carotid atherosclerosis.
Prevotella albensis, previously known as Bacteroides ruminicola subsp. ruminicola, is a species of bacterium.
Prevotella brevis is a species of bacterium.
Prevotella bryantii, previously known as Bacteroides ruminicola ruminicola subsp. brevis biovar 3, is a species of bacterium.
The BANA test is used to determine the proteolytic activity of certain oral anaerobes that contribute to oral malodor. Some bacteria, e.g. Prophyromona gingivalis, Treponema denticola, and Bacteroides forsythus produce waste products that are quite odiferous, and as a result contribute to bad breath.