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Papain, also known as papaya proteinase I, is a cysteine protease enzyme present in papaya and mountain papaya. It is the namesake member of the papain-like protease family.
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.
Cathepsin S is a protein that in humans is encoded by the CTSS gene. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. In humans, it is encoded by the CTSC gene.
The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. The family is subdivided as described below.
Tissue kallikrein is an enzyme. This enzyme catalyses the following chemical reaction
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.
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 L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a major role in intracellular protein catabolism.
Cystatin-B is a protein that in humans is encoded by the CSTB gene.
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.
Chymopapain is a proteolytic enzyme isolated from the latex of 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.
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.
Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC 3.4.24.11) and determined by the presence of peptidase family M13 as a neutral endopeptidase inhibited by phosphoramidon. Ecadotril is the (S)-enantiomer of racecadotril. NEP-like enzymes include the endothelin-converting enzymes. The peptidase M13 family believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides, neprilysin is another member of this group, in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water molecule. The peptidase domain for members of this family also contains a bacterial member and resembles that of thermolysin the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH. Thermolysin complexed with the inhibitor (S)-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase").
Glutamyl endopeptidase II is an enzyme. This enzyme catalyses the following chemical reaction
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Ananain is an enzyme. This enzyme catalyses the following chemical reaction
Signal peptidase II is an enzyme.
HIV-2 retropepsin is an enzyme. This enzyme catalyses the following chemical reaction
Asparagine endopeptidase is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN, vicilin peptidohydrolase and bean endopeptidase. In humans it is encoded by the LGMN gene.
References
- ↑ Polgár L (April 1981). "Isolation of highly active papaya peptidases A and B from commercial chymopapain". Biochimica et Biophysica Acta (BBA) - Enzymology. 658 (2): 262–9. doi:10.1016/0005-2744(81)90296-5. PMID 7018581.
- ↑ Buttle DJ, Kembhavi AA, Sharp SL, Shute RE, Rich DH, Barrett AJ (July 1989). "Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex". The Biochemical Journal. 261 (2): 469–76. doi:10.1042/bj2610469. PMC 1138849 . PMID 2505761.
- ↑ Ritonja A, Buttle DJ, Rawlings ND, Turk V, Barrett AJ (November 1989). "Papaya proteinase IV amino acid sequence". FEBS Letters. 258 (1): 109–12. doi: 10.1016/0014-5793(89)81627-8 . PMID 2591528.
- ↑ Buttle DJ, Ritonja A, Pearl LH, Turk V, Barrett AJ (January 1990). "Selective cleavage of glycyl bonds by papaya proteinase IV". FEBS Letters. 260 (2): 195–7. doi: 10.1016/0014-5793(90)80101-n . PMID 2404797.
- ↑ Buttle DJ, Ritonja A, Dando PM, Abrahamson M, Shaw EN, Wikstrom P, Turk V, Barrett AJ (March 1990). "Interactions of papaya proteinase IV with inhibitors". FEBS Letters. 262 (1): 58–60. doi: 10.1016/0014-5793(90)80153-a . PMID 1690669.
