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In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
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.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
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.
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.
The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction
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.
Rhizopuspepsin is an enzyme. This enzyme catalyses the following chemical reaction
Mucorpepsin is an enzyme. This enzyme catalyses the following chemical reaction
Saccharopepsin 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
Polyporopepsin 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
Pseudolysin is an enzyme. This enzyme catalyses the following chemical reaction
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
- ↑ Tomoda K, Shimazono H (1964). "Acid protease produced by Trametes sanguinea a wood-destroying fungus. Part I. Purification and crystallization of the enzyme". Agric. Biol. Chem. 28: 770–773. doi: 10.1271/bbb1961.28.770 .
- ↑ Tsuru D, Hattori A, Tsuji H, Yamamoto T, Fukumoto J (1969). "Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419–1426. doi:10.1080/00021369.1969.10859482.
- ↑ Ichishima E, Kumagai H, Tomoda K (1980). "Substrate specificity of carboxyl proteinase from Pycnoporus coccineus, a wood-deteriorating fungus". Curr. Microbiol. 3: 333–337. doi:10.1007/bf02601897.
