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Entamoeba is a genus of Amoebozoa found as internal parasites or commensals of animals.
Entamoeba histolytica is an anaerobic parasitic amoebozoan, part of the genus Entamoeba. Predominantly infecting humans and other primates causing amoebiasis, E. histolytica is estimated to infect about 35-50 million people worldwide. E. histolytica infection is estimated to kill more than 55,000 people each year. Previously, it was thought that 10% of the world population was infected, but these figures predate the recognition that at least 90% of these infections were due to a second species, E. dispar. Mammals such as dogs and cats can become infected transiently, but are not thought to contribute significantly to transmission.
Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.
Cathepsin S is a protein that in humans is encoded by the CTSS gene. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
Fruit bromelain is an enzyme. This enzyme catalyses the following chemical reaction
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
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, an oligosaccharide 4-alpha-D-glucosyltransferase is an enzyme that catalyzes the chemical reaction in which the non-reducing terminal alpha-D-glucose residue is transferred from a 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan. This enzyme is useful in hydrolyzing oligosaccharides.
Amoebiasis, or amoebic dysentery, is an infection of the intestines caused by a parasitic amoeba Entamoeba histolytica. Amoebiasis can be present with no, mild, or severe symptoms. Symptoms may include lethargy, loss of weight, colonic ulcerations, abdominal pain, diarrhea, or bloody diarrhea. Complications can include inflammation and ulceration of the colon with tissue death or perforation, which may result in peritonitis. Anemia may develop due to prolonged gastric bleeding.
Amoebic brain abscess is an affliction caused by the anaerobic parasitic protist Entamoeba histolytica. It is extremely rare; the first case being reported in 1849. Brain abscesses resulting from Entamoeba histolytica are difficult to diagnose and very few case reports suggest complete recovery even after the administration of appropriate treatment regimen.
Dipeptidyl peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Chymopapain is a proteolytic enzyme isolated from the latex of papaya. It is a cysteine protease which belongs to the papain-like protease (PLCP) group. Because of its proteolytic activity, it is the main molecule in the process of chemonucleolysis, used in some procedures like the treatment of herniated lower lumbar discs in the spine by a nonsurgical method.
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.
Hathewaya histolytica is a species of bacteria found in feces and the soil. It is a motile, gram-positive, aerotolerant anaerobe. H. histolytica is pathogenic in many species, including guinea pigs, mice, and rabbits, and humans. H. histolytica has been shown to cause gas gangrene, often in association with other bacteria species.
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Glycyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
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
Ananain is an enzyme. This enzyme catalyses the following chemical reaction
Gingipain R is an enzyme. This enzyme catalyses the following chemical reaction:
The sedolisin family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
References
- ↑ Lushbaugh WB, Hofbauer AF, Pittman FE (June 1985). "Entamoeba histolytica: purification of cathepsin B". Experimental Parasitology. 59 (3): 328–36. doi:10.1016/0014-4894(85)90088-8. PMID 2860002.
- ↑ Luaces AL, Barrett AJ (March 1988). "Affinity purification and biochemical characterization of histolysin, the major cysteine proteinase of Entamoeba histolytica". The Biochemical Journal. 250 (3): 903–9. doi:10.1042/bj2500903. PMC 1148941 . PMID 2898937.
