EC 3.4.22

Caspases (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death. They are named caspases due to their specific cysteine protease activity – a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 12 confirmed caspases in humans and 10 in mice, carrying out a variety of cellular functions.

Papain, also known as papaya proteinase I, is a cysteine protease () enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). It is the namesake member of the papain-like protease family.

Bromelain is an enzyme extract derived from the stems of pineapples, although it exists in all parts of the fresh plant and fruit. The extract has a history of folk medicine use. As a culinary ingredient, it may be used as a meat tenderizer.

class of enzymes

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

Actinidain (, actinidin, Actinidia anionic protease, proteinase A2 of Actinidia chinensis) is a type of cysteine protease enzyme found in fruits, including kiwifruit (genus Actinidia), pineapple, mango, banana, figs, and papaya. It is part of the peptidase C1 family of papain-like proteases.

protein-coding gene in the species Homo sapiens

Separase, also known as separin, is a cysteine protease responsible for triggering anaphase by hydrolysing cohesin, which is the protein responsible for binding sister chromatids during the early stage of anaphase. In humans, separin is encoded by the ESPL1 gene.

protein-coding gene in the species Homo sapiens

Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene. It is an initiator caspase, critical to the apoptotic pathway found in many tissues. Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.

protein-coding gene in the species Homo sapiens

A calpain (; , ) 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 calpain proteases, the small regulatory subunit CAPNS1, also known as CAPN4, and the endogenous calpain-specific inhibitor, calpastatin.

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

class of enzymes

protein-coding gene in the species Homo sapiens

Ficain also known as ficin, debricin, or higueroxyl delabarre () is a proteolytic enzyme extracted from the latex sap from the stems, leaves, and unripe fruit of the American wild fig tree Ficus insipida.

protein-coding gene in the species Homo sapiens (Humans)

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

highly specific protease

mammalian protein found in Homo sapiens

class of enzymes

mammalian protein found in Homo sapiens

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

protein-coding gene in the species Homo sapiens

Clostripain (, clostridiopeptidase B, clostridium histolyticum proteinase B, alpha-clostridipain, clostridiopeptidase, Endoproteinase Arg-C) is a cysteine protease that cleaves proteins on the carboxyl peptide bond of arginine. It was isolated from Clostridium histolyticum. The isoelectric point of the enzyme is 4.8-4.9 (at 8 °C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). The composition of the enzyme is indicated to be of two chains of relative molecular mass 45,000 and 12,500.

Chymopapain (, chymopapain A, chymopapain B, chymopapain S, brand name Chymodiactin) is a proteolytic enzyme isolated from the latex of papaya (Carica 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.

enzyme found in the fruit of the pineapple plant

Calpain-2 (, calcium-activated neutral protease II, m-calpain, milli-calpain) is an intracellular heterodimeric calcium-activated cysteine protease. This enzyme catalyses the following chemical reaction

Ananain (, stem bromelain, fruit bromelain) is an enzyme. This enzyme catalyses the following chemical reaction

bovine protein