Deuterolysin | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.4.24.39 | ||||||||
CAS no. | 247028-11-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
Deuterolysin (EC 3.4.24.39, Penicillium roqueforti protease II, microbial neutral proteinase II, acid metalloproteinase, neutral proteinase II, Penicillium roqueforti metalloproteinase) is an enzyme. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction
This enzyme is present in Penicillium roqueforti , P. caseicolum , Pyricularia oryzae , Aspergillus sojae and A. oryzae .
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Microbial collagenase is an enzyme. This enzyme catalyses the following chemical reaction
Thermolysin is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species. These enzymes are also termed 'neutral' proteinases or thermolysin -like proteinases (TLPs).
In enzymology, a secondary-alcohol oxidase (EC 1.1.3.18) is an enzyme that catalyzes the chemical reaction
Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
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.
In enzymology, a glycyrrhizinate β-glucuronidase (EC 3.2.1.128) is an enzyme that catalyzes the chemical reaction
In enzymology, an adenosylmethionine-8-amino-7-oxononanoate transaminase 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
Penicillopepsin is an enzyme. This enzyme catalyses the following chemical reaction
Rhizopuspepsin 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
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
Pseudolysin 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.