Phytepsin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.40 | ||||||||
CAS no. | 219715-98-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Phytepsin | |
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Identifiers | |
Symbol | phytepsin |
InterPro | IPR033869 |
CDD | cd06098 |
Phytepsin (EC 3.4.23.40) is an enzyme. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction
This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert.
Galactokinase is an enzyme (phosphotransferase) that facilitates the phosphorylation of α-D-galactose to galactose 1-phosphate at the expense of one molecule of ATP. Galactokinase catalyzes the second step of the Leloir pathway, a metabolic pathway found in most organisms for the catabolism of α-D-galactose to glucose 1-phosphate. First isolated from mammalian liver, galactokinase has been studied extensively in yeast, archaea, plants, and humans.
Pepsin A is an enzyme. This enzyme catalyses the following chemical reaction
Aspergillopepsin I 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).
The enzyme α-N-acetylglucosaminidase is a protein associated with Sanfilippo syndrome, with systematic name α-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase. It catalyses the hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-α-D-glucosaminides, and also UDP-N-acetylglucosamine.
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.
Cathepsin E is an enzyme that in humans is encoded by the CTSE gene. The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme.
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.
The plant-specific insert (PSI) or plant-specific sequence (PSS) is an independent domain, exclusively found in plants, consisting of approximately 100 residues, found on the C-terminal lobe on some aspartic proteases (AP) called phytepsins. The PSI, as an independent entity separate from its parent AP, is homologous to saposin and belongs to the saposin-like protein family (SAPLIP).
Glutamyl endopeptidase II is an enzyme. This enzyme catalyses the following chemical reaction
Aqualysin 1 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
Endothiapepsin 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.
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Procollagen C-endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Mycolysin is an enzyme. This enzyme catalyses the following chemical reaction
Saccharolysin is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction
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