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Aspergillopepsin I is an enzyme. This enzyme catalyses the following 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, an adenosylmethionine-8-amino-7-oxononanoate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a nucleotide diphosphokinase is an enzyme that catalyzes the chemical reaction
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
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
Polyporopepsin is an enzyme. This enzyme catalyses the following chemical reaction
Pycnoporopepsin 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.
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
- ↑ Oda K, Murao S (1974). "Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568". Agric. Biol. Chem. 38: 2435–2444. doi: 10.1271/bbb1961.38.2435 .
- ↑ Oda K, Murao S (1976). "Action of Scytalidium lignicolum acid proteases on insulin B-chain". Agric. Biol. Chem. 40: 1221–1225. doi: 10.1271/bbb1961.40.1221 .
- ↑ Oda K, Torishima H, Murao S (1986). "Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568". Agric. Biol. Chem. 50: 651–658. doi: 10.1271/bbb1961.50.651 .
