Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins.These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad.. Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya.

A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes (increases reaction rate or "speeds up") 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 …

TEV protease (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). It is a member of the PA clan of chymotrypsin-like proteases. Due to its high sequence specificity it is frequently used for the controlled cleavage of fusion proteins in vitro and in vivo.

In de kern van een protease (het actieve centrum) zit een chemisch actieve groep zoals -OH of -SH. Deze "aanvallende groep" maakt deel uit van een aminozuur zoals serine, cysteïne of aspartaat. De andere aminozuren in het actief centrum helpen mee met het katalyseren van de hydrolysereactie. Er zijn veel verschillende families van proteasen ...

Classification. There are four mammalian members of the protease-activated receptor (PAR) family: PAR1 - encoded by the gene F2R, PAR2 - F2RL1, PAR3 - F2RL2 and PAR4 - F2RL3, all these genes have their locus on chromosome 5 except of PAR4, which is on chromosome 19.They are also members of the seven-transmembrane G-protein-coupled receptor …

A calpain (/ ˈ k æ l p eɪ n /; EC 3.4.22.52, EC 3.4.22.53) is a protein belonging to the family of calcium-dependent, non-lysosomal cysteine proteases (proteolytic enzymes) expressed ubiquitously in mammals and many other organisms.Calpains constitute the C2 family of protease clan CA in the MEROPS database. The calpain proteolytic system includes the …

The main player in the catalytic mechanism in the serine proteases is the catalytic triad. The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all superfamilies of serine protease enzymes. The triad is a coordinated structure consisting of three amino acids: His 57, Ser 195 (hence the name "serine protease") and Asp 102.

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion.. Proteolysis in organisms serves many purposes; for example, digestive enzymes …

Insulin-degrading enzyme, also known as IDE, is an enzyme.. Known alternatively as insulysin or insulin protease, IDE is a large zinc-binding protease of the M16 metalloprotease family known to cleave multiple short polypeptides that vary considerably in sequence. Other members of this family include the mitochondrial processing peptidase and presequence protease.

Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9.It is encoded by the CASP3 gene.CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.. The CASP3 protein is a member of the cysteine-aspartic acid protease family.