Lysyl endopeptidase (R) | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.21.50 | ||||||||
CAS no. | 123175-82-6 | ||||||||
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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Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase, and caseinase) is an enzyme. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction
This enzyme is isolated from Lysobacter enzymogenes .
It is produced by the human body and by Achromobacter lyticus [7] that can help break down the protein casein in milk into smaller peptides and amino acids. [8]
Enteropeptidase is an enzyme produced by cells of the duodenum and is involved in digestion in humans and other animals. Enteropeptidase converts trypsinogen into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment.
Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.
N-acetyllactosamine synthase is a galactosyltransferase enzyme. It is a component of lactose synthase This enzyme modifies the connection between two molecule UDP-galactose and N-actyl-D-glucosamine and generates two different molecules UDP and N-acetyllactosamine as products. The main function of the enzyme is associated with the biosynthesis of glycoproteins and glycolipids in both human and animals. In human, the activity of this enzyme can be found in Golgi apparatus.
In enzymology, a 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-mercaptopyruvate sulfurtransferase is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.
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 X is an enzyme. This enzyme catalyses the following chemical reaction
Sucrose α-glucosidase is an enzyme with systematic name sucrose-α-D-glucohydrolase. It catalyses the hydrolysis of sucrose and maltose by an α-D-glucosidase-type action.
Aminopeptidase I is an enzyme. This enzyme catalyses the following chemical reaction
Alpha-lytic endopeptidase or Alpha-lytic protease is an enzyme isolated from the myxobacterium Lysobacter enzymogenes. This enzyme is a serine protease that catalyses the breakage of peptide bonds using a hydrolysis chemical reaction. Alpha-lytic protease was named based on the observed cleavage specificity for the α position of the tetrapeptide component in gram-positive bacterial cell walls (alanine). Alpha-lytic protease is also capable of digesting elastin and other proteins.
Glutamyl endopeptidase is an extracellular bacterial serine protease of the glutamyl endopeptidase I family that was initially isolated from the Staphylococcus aureus strain V8. The protease is, hence, commonly referred to as "V8 protease", or alternatively SspA from its corresponding gene.
Cerevisin is an enzyme. This enzyme catalyses the following chemical reaction
Endopeptidase La is an enzyme. This enzyme catalyses hydrolysis of proteins in the presence of ATP.
Oryzin is an enzyme. This enzyme catalyses the following chemical reaction
Glycyl endopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Candidapepsin is an enzyme. This enzyme catalyses the following chemical reaction
Serralysin is an enzyme. This enzyme catalyses the following chemical reaction
Peptidyl-Lys metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Beta-lytic metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Peptidyl-Asp metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction