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A protease 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 many biological functions, including digestion of ingested proteins, protein catabolism, and cell signaling.
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.
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.
The Japanese rice fish, also known as the medaka, is a member of genus Oryzias (ricefish), the only genus in the subfamily Oryziinae. This small native of Japan is a denizen of rice paddies, marshes, ponds, slow-moving streams and tide pools. It is euryhaline, occurring in both brackish and freshwater. It became popular as an aquarium fish because of its hardiness and pleasant coloration: its coloration varies from creamy-white to yellowish in the wild to white, creamy-yellow, or orange in aquarium-bred individuals. Bright yellow, red or green transgenic populations, similar to GloFish, have also been developed, but are banned from sale in the EU. The medaka has been a popular pet since the 17th century in Japan. After fertilization, the female carries her eggs attached anterior to the anal fin for a period before depositing them on plants or similar things.
TEV protease 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, TEV protease is frequently used for the controlled cleavage of fusion proteins in vitro and in vivo.
Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene.
Many major physiological processes depend on regulation of proteolytic enzyme activity and there can be dramatic consequences when equilibrium between an enzyme and its substrates is disturbed. In this prospective, the discovery of small-molecule ligands, like protease inhibitors, that can modulate catalytic activities has an enormous therapeutic effect. Hence, inhibition of the HIV protease is one of the most important approaches for the therapeutic intervention in HIV infection and their development is regarded as major success of structure-based drug design. They are highly effective against HIV and have, since the 1990s, been a key component of anti-retroviral therapies for HIV/AIDS.
Intramembrane proteases (IMPs), also known as intramembrane-cleaving proteases (I-CLiPs), are enzymes that have the property of cleaving transmembrane domains of integral membrane proteins. All known intramembrane proteases are themselves integral membrane proteins with multiple transmembrane domains, and they have their active sites buried within the lipid bilayer of cellular membranes. Intramembrane proteases are responsible for proteolytic cleavage in the cell signaling process known as regulated intramembrane proteolysis (RIP).
Brachyurin is an enzyme. This enzyme catalyses the Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus.
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Spermosin is an enzyme. This enzyme catalyses the following chemical reaction
Mannan-binding lectin-associated serine protease-2 is an enzyme. This enzyme catalyses the following chemical reaction
Ulp1 peptidase is an enzyme. This enzyme catalyses the following chemical reaction
Rhizopuspepsin is an enzyme. This enzyme catalyses the following chemical reaction
Endothiapepsin is an enzyme. This enzyme catalyses the following chemical reaction
Envelysin is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
Choriolysin L is an enzyme. This enzyme catalyses the following chemical reaction
The sedolisin 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.
References
- ↑ Yasumasu S, Iuchi I, Yamagami K (February 1989). "Purification and partial characterization of high choriolytic enzyme (HCE), a component of the hatching enzyme of the teleost, Oryzias latipes". Journal of Biochemistry. 105 (2): 204–11. PMID 2656664.
- ↑ Yasumasu S, Katow S, Umino Y, Iuchi I, Yamagami K (July 1989). "A unique proteolytic action of HCE, a constituent protease of a fish hatching enzyme: tight binding to its natural substrate, egg envelope". Biochemical and Biophysical Research Communications. 162 (1): 58–63. doi:10.1016/0006-291x(89)91961-x. PMID 2751672.
- ↑ Yasumasu S, Yamada K, Akasaka K, Mitsunaga K, Iuchi I, Shimada H, Yamagami K (October 1992). "Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development". Developmental Biology. 153 (2): 250–8. doi:10.1016/0012-1606(92)90110-3. PMID 1397682.
- ↑ Lee KS, Yasumasu S, Nomura K, Iuchi I (February 1994). "HCE, a constituent of the hatching enzymes of Oryzias latipes embryos, releases unique proline-rich polypeptides from its natural substrate, the hardened chorion". FEBS Letters. 339 (3): 281–4. doi: 10.1016/0014-5793(94)80431-1 . PMID 8112467.
- ↑ Yamagami K (November 1972). "Isolation of a choriolytic enzyme (hatching enzyme) of the teleost, Oryzias latipes". Developmental Biology. 29 (3): 343–8. doi:10.1016/0012-1606(72)90074-7. PMID 4652273.
