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In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
Tryptase is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. Club cells contain tryptase, which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.
Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction
Tissue kallikrein is an enzyme. This enzyme catalyses the following chemical reaction
Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family. Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response.
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.
Cathepsin E is an enzyme that in humans is encoded by the CTSE gene. The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.
Aminopeptidase S is an enzyme. This enzyme catalyses the following chemical reaction
Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Streptogrisin A is an enzyme. This enzyme catalyses the following chemical reaction
Streptogrisin B is an enzyme. This enzyme catalyses the following chemical reaction
Glutamyl endopeptidase II is an enzyme. This enzyme catalyses the following chemical reaction
Scytalidocarboxyl peptidase B, also known as Scytalidoglutamic peptidase and Scytalidopepsin B is a proteolytic enzyme. It was previously thought to be an aspartic protease, but determination of its molecular structure showed it to belong a novel group of proteases, glutamic protease.
Phytepsin is an enzyme. This enzyme catalyses the following chemical reaction
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Vibriolysin is an enzyme. This enzyme catalyses the following chemical reaction
Bacillolysin is an enzyme. This enzyme catalyses the following chemical reaction
Deuterolysin is an enzyme. This enzyme catalyses the following chemical reaction
Snapalysin is an enzyme. This enzyme catalyses the following chemical reaction
Streptomyces cacaoi is a bacterium species from the genus of Streptomyces. Streptomyces cacaoi produces polyoxine.
References
- ↑ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi:10.1016/0003-9861(68)90179-3. PMID 4967801.
- ↑ Hiramatsu A, Ouchi T (May 1972). "A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties". Journal of Biochemistry. 71 (5): 767–81. PMID 5073323.
- ↑ Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of Biochemistry. 136 (1): 151–4. doi:10.1111/j.1432-1033.1983.tb07719.x. PMID 6413206.
- ↑ Chang PC, Kuo TC, Tsugita A, Lee YH (March 1990). "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product". Gene. 88 (1): 87–95. doi:10.1016/0378-1119(90)90063-w. PMID 2341042.
