Endopeptidase


Also found in: Dictionary, Thesaurus, Medical, Wikipedia.
Related to Endopeptidase: neutral endopeptidase

endopeptidase

[¦en·dō′pep·tə‚dās]
(biochemistry)
An enzyme that acts upon the centrally located peptide bonds of a protein molecule.

Endopeptidase

 

an enzyme of the class of hydrolases. Endo-peptidases catalyze the decomposition of internal peptide bonds in proteins and peptides. The speed of hydrolysis of a given peptide bond by different endopeptidases depends on the substrate specificity of the enzyme and the spatial accessibility of the given peptide bond, especially if the substrate is a native, not denatured, protein. It does not depend on the size of the molecules of the substrate, that is, the length of the polypeptide chain. The substrate specificity of an endopeptidase consists in the ability of a given enzyme to hydrolyze the peptide bonds between certain amino acid residues with the greatest speed. For example, chy-motrypsin very rapidly hydrolyzes peptide bonds together with aromatic amino acids; trypsin does the same with diamino acids. Endopeptidases are classified as extracellular or intracellular (tissular). Extracellular endopeptidases are secreted into the digestive cavity of animals (for example, enterokinase) or simply into the external environment (the exo-enzymes of bacteria).

The use of endopeptidases in determining the primary structure of proteins is based on their properties.

References in periodicals archive ?
This protein has serine-type endopeptidase activity and was found to play a role in malignant melanoma progression.
Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon.
The report provides a snapshot of the global therapeutic landscape for Neprilysin (Neutral Endopeptidase 24.
Motility-related ultrastructural changes in the flageller membrane of apyrene spermatozoa of the silkworm, Bombyx mori, induced by Arg-C endopeptidase.
Kos, "Inhibition of endopeptidase and exopeptidase activity of cathepsin B impairs extracellular matrix degradation and tumour invasion," Biological Chemistry, vol.
Neutral endopeptidase and neurogenic inflammation in rats with respiratory infections.
LasA staphylolytic protease is a 20-KDa [beta]-lytic endopeptidase family of protease produced by P.
55) Experiments using a panel of more than 20 peptidase inhibitors highlighted that a neutral endopeptidase family member, similar or identical to neprilysin, appears to play a major role in the A[[beta].
Glutalytic contains both endopeptidases and exopeptidases to create the correct endopeptidase cleavage pattern near the long chain amino acids that need to be hydrolyzed by the exopeptidase, producing rapid degradation of gluten.
Cathepsin L, a lysosomal endopeptidase, is a member of the papain-like family of cysteine proteinases (1).
The expression and catalytic activity of neural endopeptidase (NEP) which is involved in degrading beta amyloid was also measured.
34 Inhibition of the clearance enzyme neutral endopeptidase (NEP) is another promising way for increasing natriuretic peptide level.