Proteases are generally categorized into two major groups based on their site of action, that is, exopeptidases
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
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].