Endopeptidase

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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 ?
Cysteine endopeptidases and their inhibitors in malignant progression of rat embryo fibroblasts.
Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic 0 cell via two distinct site specific endopeptidases.
Role of muscle endopeptidases and their inhibitors in meat tenderness.
Non-proteasome proteases have been divided into exopeptidases and endopeptidases depending on the cleavage position of target proteins.
Syntaxin's TSI products are biological molecules synthesized in microbial cell culture, which selectively bind to their chosen targeted cells and become internalised to deliver endopeptidases into the cell's cytoplasm, preventing further vesicular secretion.
The most common form is inherited in an X-linked dominant manner (XLH), associated with mutations in the PHEX gene (Phosphate regulating gene with Homologies to Endopeptidases on the X-chromosome) [Feng, 2006; Lorenz-Depiereux et al.
The function of L chains has been established as zinc dependent endopeptidases (77), and the substrates are one of the three proteins of the docking complex responsible for release of acetylcholine from synaptic vesicles.
Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components.
The whey protein used in the study, however--Optipep--uses specific exo- and endopeptidases to reduce bitterness.
These abnormalities are more prominent in strains lacking DD-carboxypeptidase (PBP 5) along with endopeptidases (PBPs 4 and 7).
Excessive paraneoplastic production of phosphatonin is thought to be involved in the etiology of tumor-induced osteomalacia, whereas impaired degradation and processing of phosphatonin due to endopeptidase mutations (PHEX gene: phosphate-regulating gene with homologies to endopeptidases on the X chromosome) is thought to cause the typical findings in XLH.
The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts: purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate.