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Physarolisin
The sedolisin (MEROPS S53) 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. Their optimal pH is around 3. Most members of the family are produced as a precursor protein with N-terminal () and sometimes C-terminal peptides that need to be cleaved off. Family members Sedolisin Sedolisin (, ''pseudomonapepsin'', ''sedolysin'') is a serine protease. It is secreted by ''Pseudomonas'' sp. 101. It performs hydrolysis of the B chain of insulin at -Glu13-Ala-, -Leu15-Tyr- and -Phe25-T ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MEROPS
MEROPS is an online database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors. The classification scheme for peptidases was published by Rawlings & Barrett in 1993, and that for protein inhibitors by Rawlings ''et al.'' in 2004.Rawlings, N.D., Tolle, D.P. & Barrett, A.J. (2004) "Evolutionary families of peptidase inhibitors." ''Biochem J'' 378, 705-716. The most recent version, MEROPS 12.5, was released in September 2023. Overview The classification is based on similarities at the tertiary and primary structural levels. Comparisons are restricted to that part of the sequence directly involved in the reaction, which in the case of a peptidase must include the active site, and for a protein inhibitor the reactive site. The classification is hierarchical: sequences are assembled into families, and families are assembled into clans. Each peptidase, family, and clan has a unique identifier. Classification Family The families of pe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptidases
A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in numerous biological pathways, including digestion of ingested proteins, protein catabolism (breakdown of old proteins), and cell signaling. In the absence of functional accelerants, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Classification Based on catalytic residue Proteases can be classified into seven broad groups: * Serine proteases - using a serine alcohol * Cysteine proteases ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
