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Proteinase 3, also known as PRTN3, is an enzyme that in humans is encoded by the PRTN3 gene.
Endopeptidase Clp (EC 3.4.21.92, endopeptidase Ti, caseinolytic protease, protease Ti, ATP-dependent Clp protease, ClpP, Clp protease). This enzyme catalyses the following chemical reaction
Subtilisin is a protease initially obtained from Bacillus subtilis.
The heat shock proteins HslV and HslU are expressed in many bacteria such as E. coli in response to cell stress. The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. HslV is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria. HslV bears high similarity to core subunits of proteasomes.
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.
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]
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.
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Lysyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Endopeptidase La is an enzyme. This enzyme catalyses hydrolysis of proteins in the presence of ATP.
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Pancreatic endopeptidase E is an enzyme. This enzyme catalyses the following chemical reaction
Signal peptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Peptidase Do is an enzyme. This enzyme catalyses the following chemical reaction
Pestivirus NS3 polyprotein peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Nuclear-inclusion-a endopeptidase is a protease enzyme found in potyviruses. This enzyme catalyses the following chemical reaction:
IgA-specific metalloendopeptidase 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.
References
- ↑ Goldberg AL, Swamy KH, Chung CH, Larimore FS (1981). Proteases in Escherichia coli. Methods in Enzymology. Vol. 80 Pt C. pp. 680–702. doi:10.1016/s0076-6879(81)80052-3. PMID 7043205.
- ↑ Chung CH, Goldberg AL (April 1983). "Purification and characterization of protease So, a cytoplasmic serine protease in Escherichia coli". Journal of Bacteriology. 154 (1): 231–8. doi:10.1128/jb.154.1.231-238.1983. PMC 217451 . PMID 6339474.
