Endopeptidase


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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 ?
In addition to cysteine proteases, other types of endopeptidases have been suggested to be involved in flower senescence.
The additional therapeutic application of AGN-214868 for overactive bladder widens the application of the re-targeted endopeptidase drug candidate across two distinctively separate disease markets of significant unmet medical need.
Therapeutics against BoNT can target any of the three steps of mode of action of BoNT: binding, endocytosis/translocation, and endopeptidase activity.
Delayed metabolism of human brain natriuretic peptide reflects resistance to neutral endopeptidase.
This method is based on both the unusual endopeptidase activities of these enzymes and specific detection of the unique peptide products by mass spectrometry (Endopep-MS).
Preclinical studies have indicated that when prodrug molecules reach the vicinity of a tumor, the peptide is cleaved off by endopeptidase enzymes that are released by the cancer cells, freeing the cytotoxic compound.
Bitterness in cheese occurs when there is an imbalance of the production of bitter peptides by protease and endopeptidase enzymes, and involves their removal by exopeptidase enzymes.
Omapatrilat is an investigational drug in a new class of cardiovascular medications, called vasopeptidase inhibitors (VPIs), which simultaneously inhibits two key enzymes that regulate heart function and blood pressure -- neutral endopeptidase (NEP) and angiotensin-converting enzyme (ACE).
Neutral endopeptidase (NEP) could reduce some of the condition's effects, according to Patrick Ward, professor of physiology, Ohio State University, Columbus.
Since papain is closely related to cathepsin B, a thiol endopeptidase which is released by cells of the inflammatory response, the authors concluded that segmented poly-etherurethanes can be degraded by enzymes which are present during the inflammatory response.
Plasma activity of the enzyme prolyl endopeptidase (PEP) shows significant annual variation.
ALV003 is an orally administered mixture of two recombinant gluten-specific proteases, a cysteine protease (EP-B2) and a prolyl endopeptidase (PEP).