endopeptidase


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Related to endopeptidase: neutral endopeptidase

endopeptidase

 [en″do-pep´tĭ-dās]
any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein. Inhibition of the action of endopeptidases (proteases) in viruses causes formation of noninfectious particles; certain antiviral drugs work in this way (see protease inhibitors). Called also protease and proteinase.

en·do·pep·ti·dase

(en'dō-pep'ti-dās),
An enzyme that catalyzes the hydrolysis of a peptide chain at points well within the chain, not near either terminus; for example, pepsin, trypsin. Compare: exopeptidase.
Synonym(s): proteinase

endopeptidase

(ĕn′dō-pĕp′tĭ-dās′, -dāz′)
n.
Any of a large group of enzymes that catalyze the hydrolysis of peptide bonds in the interior of a polypeptide chain or protein molecule.

en·do·pep·ti·dase

(en'dō-pep'ti-dās)
An enzyme catalyzing the hydrolysis of a peptide chain at points well within the chain, not near termini (e.g., pepsin, trypsin).
Compare: exopeptidase

endopeptidase

or

proteinase

a type of PROTEASE (protein-splitting enzyme) that hydrolyses peptide bonds between particular amino acids located inside the chain, but not at the ends. There are three major endopeptidases in the mammalian gut: PEPSIN (stomach); TRYPSIN and CHYMOTRYPSIN (pancreas). Such enzymes are responsible for the first stage of protein digestion; other proteases called EXOPEPTIDASES complete the digestion of protein in the ILEUM.
References in periodicals archive ?
Recombinant SNAP-25 is an effective substrate for Clostridium botulinum type A toxin endopeptidase activity in vitro.
Proteases are generally categorized into two major groups based on their site of action, that is, exopeptidases and endopeptidases. Exopeptidases are those proteases that cleave the peptide bond proximal to the amino or carboxy termini of the substrate (cleave N- or C-terminal peptide bonds of a polypeptide chain), whereas endopeptidases cleave peptide bonds distant from the termini of the substrate (cleave internal peptide bonds) [3, 4].
As mentioned above, NT-proBNP was thought to be more dependent on renal excretion compared to BNP as the latter is also cleared from circulation by natriuretic peptide receptor type C and neutral endopeptidases. However, the recent data does not support this notion.
Gade-Andavolu et al., "Association of the neutral endopeptidase (MME) gene with anxiety," Psychiatric Genetics, vol.
Mougenot et al., "Brief report: Antenatal membranous glomerulonephritis due to anti-neutral endopeptidase antibodies," New England Journal of Medicine, vol.
The report provides comprehensive information on the Neprilysin (Neutral Endopeptidase 24.11 or Atriopeptidase or Common Acute Lymphocytic Leukemia Antigen or CD10 or EC 3.4.24.11), targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type.
Motility-related ultrastructural changes in the flageller membrane of apyrene spermatozoa of the silkworm, Bombyx mori, induced by Arg-C endopeptidase. International Journal of Invertebrate Reproduction and Development 19: 193-201.
Matrix metalloprotease (MMP) is an endopeptidase expressed in human urine whenever cancer is present.
Yorek, "Effect of inhibition of angiotensin converting enzyme and/or neutral endopeptidase on vascular and neural complications in high fat fed/low dose streptozotocin-diabetic rats," European Journal of Pharmacology, vol.
(22) Some of the same substances that induce SP inhibit neutral endopeptidase (NEP), the enzyme that breaks clown SP.
Circulating adhesion molecules and neutral endopeptidase enzymuria in patients with urolithiasis and hydronephrosis.
Flavourzyme that is an exopeptidase, produced the lowest amount of peptide with small molecular size (15.4% and 19.8% of soybean and rice, respectively), whereas Alcalase as the strongest endopeptidase in this study can provide the most amount of peptides with small sizes (<4 kDa) (Figure 1).