endopeptidase

en·do·pep·ti·dase

E0136200 (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.

endopeptidase

(ˌɛndəʊˈpɛptɪˌdeɪz) n (Biochemistry) any proteolytic enzyme, such as pepsin, that splits a protein into smaller peptide fragments. Also called: proteinase Compare exopeptidase

Translations

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.

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 inhibitors" >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

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.

单词	endopeptidase
释义	endopeptidase en·do·pep·ti·dase E0136200 (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. endopeptidase (ˌɛndəʊˈpɛptɪˌdeɪz) n (Biochemistry) any proteolytic enzyme, such as pepsin, that splits a protein into smaller peptide fragments. Also called: proteinase Compare exopeptidase Translations 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. 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 inhibitors" >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. ThesaurusSeeprotease
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