exopeptidase

(redirected from Exopeptidases)
Also found in: Medical, Encyclopedia.

ex·o·pep·ti·dase

 (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.
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

exopeptidase

(ˌɛksəʊˈpɛptɪˌdeɪz)
n
(Biochemistry) any proteolytic enzyme, such as erepsin, that acts on the terminal bonds in a peptide chain. Compare endopeptidase
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014
References in periodicals archive ?
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).
Currently, the term "peptidase" is also used equivalently with "protease" and "proteinase." Peptidase was restricted to the enzymes included in subsubclasses EC 3.4.11-19, the exopeptidases in the Enzyme Nomenclature (1984), while the term "proteinases" was previously used for the enzymes included in subsubclasses EC 3.4.21-99 having the same meaning as "endopeptidase." However, the terms "protease" and "proteinase" are still preferred by many scientists [3].
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].
This avoids MS analysis and interpretation of extremely complex peptide mixtures that might otherwise result from degradation by the omnipresent exopeptidases. In addition, the reporter is isotopically labeled with heavy (e.g., [sup.13]C or [sup.15]N) amino acids in various positions to yield intact peptides with identical mass but with distinct fragment ions that can be monitored by tandem MS, a technique termed mass encoding.
Glutalytic contains both endopeptidases and exopeptidases to create the correct endopeptidase cleavage pattern near the long chain amino acids that need to be hydrolyzed by the exopeptidase, producing rapid degradation of gluten."
Non-proteasome proteases have been divided into exopeptidases and endopeptidases depending on the cleavage position of target proteins.
Intracellular proteases are either exopeptidases, which act at the amino- or carboxyl-terminal or endopeptidases, which are capable of clearing peptide bonds in the central region of polypeptides.