Related Research Articles
In biology and biochemistry, protease inhibitors, or antiproteases, are molecules that inhibit the function of proteases. Many naturally occurring protease inhibitors are proteins.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
In enzymology, a glutamate—ethylamine ligase (EC 6.3.1.6) is an enzyme that catalyzes the chemical reaction
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
In enzymology, a nucleotide diphosphokinase is an enzyme that catalyzes the chemical 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
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
Pycnoporopepsin 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
- ↑ Sawada, J. (1963). "Studies on the acid-protease of Paecilomyces varioti Bainier TPR-220. Part I. Crystallization of the acid-protease of Paecilomyces varioti Bainier TPR-220". Agric. Biol. Chem. 27: 677–683. doi:10.1080/00021369.1963.10858167.
- ↑ Sawada, J. (1964). "The acid-protease of Paecilomyces varioti. III. The specificity of the crystalline acid-protease on synthetic substrates". Agric. Biol. Chem. 28: 869–875. doi:10.1080/00021369.1964.10858312.
- ↑ Kamada M, Oda K, Murao S (1972). "The purification of the extracellular acid protease of Rhodotorula glutinis K-24 and its general properties". Agric. Biol. Chem. 36: 1095–1101. doi: 10.1271/bbb1961.36.1095 .
- ↑ Murao S, Funakoshi S, Oda K (1972). "Purification, crystallization and some enzymatic properties of acid protease of Cladosporium sp. No. 45-2". Agric. Biol. Chem. 36: 1327–1333. doi: 10.1271/bbb1961.36.1327 .
- ↑ Oda K, Kamada M, Murao S (1972). "Some physicochemical properties and substrate specificity of acid protease of Rhodotorula glutinis K-24". Agric. Biol. Chem. 36: 1103–1108. doi: 10.1271/bbb1961.36.1103 .
- ↑ Oda K, Funakoshi S, Murao S (1973). "Some physicochemical properties and substrate specificity of acid protease isolated from Cladosporium sp. No. 45-2". Agric. Biol. Chem. 37: 1723–1729. doi: 10.1271/bbb1961.37.1723 .
- ↑ Takahashi K, Chang WJ (September 1976). "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin". Journal of Biochemistry. 80 (3): 497–506. PMID 10290.
- ↑ 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: 787–793. doi: 10.1271/bbb1961.52.787 .
