exopeptidase


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exopeptidase

 [ek″so-pep´tĭ-dās]
a proteolytic enzyme whose action is limited to terminal peptide linkages.

ex·o·pep·ti·dase

(ek'sō-pep'ti-dās),
An enzyme that catalyzes the hydrolysis of the terminal amino acid of a peptide chain; for example, carboxypeptidase. Compare: endopeptidase.

exopeptidase

(ĕk′sō-pĕp′tĭ-dās′, -dāz′)
n.
Any of a group of enzymes that catalyze the hydrolysis of single amino acids from the end of a polypeptide chain.

ex·o·pep·ti·dase

(eks'ō-pep'ti-dās)
An enzyme that catalyzes the hydrolysis of the terminal amino acid of a peptide chain (e.g., carboxypeptidase).
Compare: endopeptidase

exopeptidase

An enzyme that acts to split off AMINO ACIDS or sometimes dipeptides from the ends of a protein molecule.

exopeptidase

a type of protein-splitting ENZYME that hydrolyses the terminal PEPTIDE BONDS rather than those bonds within the chain. There are three main types of exopeptidase in the mammalian gut, each attacking a particular area of the protein: carboxypeptidase attacks the carboxyl end of the chain; aminopeptidase attacks the amino end of the chain; dipeptidase breaks the bond between DIPEPTIDES. Such enzymes complete the digestion of protein prior to absorption into the blood stream. Compare ENDOPEPTIDASE.
References in periodicals archive ?
Proteases are generally categorized into two major groups based on their site of action, that is, exopeptidases and endopeptidases.
Kos, "Inhibition of endopeptidase and exopeptidase activity of cathepsin B impairs extracellular matrix degradation and tumour invasion," Biological Chemistry, vol.
A sequence-specific exopeptidase activity test (SSEAT) for functional biomarker discovery.
Heterogeneity is observed for many components because of exopeptidase action on the peptide chain, sequence variations, and variable modifications of free sulfhydryl groups of unpaired cysteines (19, 20, 28, 65-67).
The PEG component of macrosubstrates also may serve as a highly effective protecting group against exopeptidase action to assure that only endoproteinase activity is measured.
Because of its exopeptidase activity, it has been implicated in the metabolism of metenkephalin (18) and angiotensin (Ang) III (17); its endopeptidase activity is also thought to be involved in neurotensin metabolism (19).
This variation indicates that the appearance of chymotrypsin is differential: it is mainly related to the presence of trypsin and to maximizing activity exopeptidases when the digestive system has matured completely (Suzer et al., 2007; JimenezMartinez et al., 2012).
Protease has been categorized based on several standards, proteases are classified according to the position of the peptide bond cleaved into two major groups as exopeptidases and endopeptidases (El Enshasy et al., 2016; Prassas et al., 2015].
Proteolytic enzymes are classified as endo and exopeptidases. Studies have shown that ultrasound can modify the functional and structural properties of food protein (CHANDRAPALA et al., 2011).
MS/MS analysis of blood plasma of animals intoxicated with RVX revealed fragments of fibrinopeptide A, signifying that exposure to RVX caused inactivation or reduced expression of exopeptidases (aminopeptidases) [192].
It is generally accepted that endopeptidases like trypsin (Try) or chymotrypsin (Chy) initiate the hydrolysis of protein-releasing polypeptides that are further hydrolyzed by other endopeptidases yielding smaller polypeptides available for exopeptidases; Try hydrolyzes the peptide bond formed by the carboxylic side of lysine or arginine, whereas Chy at voluminous hydrophobic amino acids like tyrosine, tryptophan, or phenylalanine.
Moreover, other endopeptidases (e.g., PreScission and Sortase A) and exopeptidases (e.g., DAPase, Aeromonas aminopeptidase, aminopeptidase M, and carboxypeptidase A and B) were described exhaustively for the removal of affinity tags from recombinant proteins [1, 52].