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Related to endopeptidase: neutral endopeptidase
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.
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.
endopeptidase/en·do·pep·ti·dase/ (-pep´tĭ-dās) protease; any peptidase that catalyzes the cleavage of internal bonds in a polypeptide or protein.
Any of a large group of enzymes that catalyze the hydrolysis of peptide bonds in the interior of a polypeptide chain or protein molecule.
Etymology: Gk, endon, within + Gk, peptein, to digest + ase, enzyme suffix
any peptidase that catalyzes the cleavage of internal peptide bonds in a polypeptide or protein. Endopeptidases are divided into subclasses on the basis of catalytic mechanism and comprise the serine endopeptidases, cysteine endopeptidases, aspartic endopeptidases, metalloendopeptidases, and other endopeptidases.
An enzyme catalyzing the hydrolysis of a peptide chain at points well within the chain, not near termini (e.g., pepsin, trypsin).
proteinasea 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.
a peptidase capable of acting on any peptide linkage in a peptide chain.