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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.
Pepsin A is an enzyme. This enzyme catalyses the following chemical reaction
Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin.
In molecular biology, Proteinase K is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Parengyodontium album. Proteinase K is able to digest hair (keratin), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity. This enzyme belongs to Peptidase family S8 (subtilisin). The molecular weight of Proteinase K is 28,900 daltons.
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.
Aminopeptidase Ey is an enzyme. This enzyme catalyses differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position
Cucumisin is an enzyme. This enzyme catalyzes hydrolysis of a wide range of proteins. It has been identified as an allergen in humans.
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Aspergilloglutamic peptidase, also called aspergillopepsin II is a proteolytic enzyme. The enzyme was previously thought be an aspartic protease, but it was later shown to be a glutamic protease with a catalytic Glu residue at the active site, and was therefore renamed aspergilloglutamic peptidase.
Penicillopepsin 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
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Rhodotorulapepsin is an enzyme. This enzyme catalyses the following chemical reaction
Acrocylindropepsin (EC 3.4.23.28, Acrocylindrium proteinase, Acrocylindrium acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
Scytalidopepsin A (EC 3.4.23.31, Scytalidium aspartic proteinase A, Scytalidium lignicolum aspartic proteinase, Scytalidium lignicolum aspartic proteinase A-2, Scytalidium lignicolum aspartic proteinase A-I, Scytalidium lignicolum aspartic proteinase C, Scytalidium lignicolum carboxyl proteinase, Scytalidium lignicolum acid proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
Scytalidocarboxyl peptidase B, also known as Scytalidoglutamic peptidase and Scytalidopepsin B is a proteolytic enzyme. It was previously thought to be an aspartic protease, but determination of its molecular structure showed it to belong a novel group of proteases, glutamic protease.
Deuterolysin is an enzyme. This enzyme catalyses the following chemical reaction
Glutamic proteases are a group of proteolytic enzymes containing a glutamic acid residue within the active site. This type of protease was first described in 2004 and became the sixth catalytic type of protease. Members of this group of protease had been previously assumed to be an aspartate protease, but structural determination showed it to belong to a novel protease family. The first structure of this group of protease was scytalidoglutamic peptidase, the active site of which contains a catalytic dyad, glutamic acid (E) and glutamine (Q), which give rise to the name eqolisin. This group of proteases are found primarily in pathogenic fungi affecting plant and human.
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
- ↑ Kovaleva GG, Shimanskaya MP, Stepanov VM (November 1972). "The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergillus awamori--an analog of penicillopepsin and pepsin". Biochemical and Biophysical Research Communications. 49 (4): 1075–81. doi:10.1016/0006-291x(72)90322-1. PMID 4565799.
- ↑ Morihara K, Oka T (August 1973). "Comparative specificity of microbial acid proteinases for synthetic peptides. 3. Relationship with their trypsinogen activating ability". Archives of Biochemistry and Biophysics. 157 (2): 561–72. doi:10.1016/0003-9861(73)90675-9. PMID 4581238.
- ↑ Davidson R, Gertler A, Hofmann T (April 1975). "Aspergillus oryzae acid proteinase. Purification and properties, and formation of pi-chymotrypsin". The Biochemical Journal. 147 (1): 45–53. doi:10.1042/bj1470045. PMC 1165373 . PMID 239702.
- ↑ Chang WJ, Horiuchi S, Takahashi K, Yamasaki M, Yamada Y (November 1976). "The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus". Journal of Biochemistry. 80 (5): 975–81. doi:10.1093/oxfordjournals.jbchem.a131385. PMID 12156.
- ↑ Tanaka N, Takeuchi M, Ichishima E (December 1977). "Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity". Biochimica et Biophysica Acta (BBA) - Enzymology. 485 (2): 406–16. doi:10.1016/0005-2744(77)90176-0. PMID 21699.
- ↑ Ostoslavskaya VI, Kotlova EK, Stepanov VM, Rudenskaya GH, Baratova LA, Belyanova LP (1976). "Aspergillopepsin F-A carboxylic proteinase from Aspergillus foetidus". Bioorg. Khim. 5: 595–603.
- ↑ Panneerselvam M, Dhar SC (1981). "Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus". The Italian Journal of Biochemistry. 30 (3): 207–16. PMID 7024192.
- ↑ Ostoslavskaya VI, Revina LP, Kotlova EK, Surova IA, Levin ED, Timokhima EA, Stepanov VM (1986). "The primary structure of aspergillopepsin A, aspartic proteinase from Aspergillus awamori. IV. Amino acid sequence of the enzyme". Bioorg. Khim. 12: 1030–1047.
- ↑ Yagi F, Fan J, Tadera K, Kobayashi A (1986). "Purification and characterization of carboxyl proteinase from Aspergillus kawachii". Agric. Biol. Chem. 50 (4): 1029–1033. doi: 10.1271/bbb1961.50.1029 .
- ↑ Majima E, Oda K, Murao S, Ichishima E (1988). "Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate". Agric. Biol. Chem. 52 (3): 787–793. doi: 10.1271/bbb1961.52.787 .
