exopeptidase


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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.

exopeptidase

(ˌɛksəʊˈpɛptɪˌdeɪz)
n
(Biochemistry) any proteolytic enzyme, such as erepsin, that acts on the terminal bonds in a peptide chain. Compare endopeptidase
References in periodicals archive ?
For dermatophytes, including those causing tinea corporis, amino acids are regarded as a source for growth.16 Under in vivo condition, dermatophytes secret several types of endopeptidase and exopeptidase in the presence of keratin as a sole nitrogen source.17 These enzymes digest proteins into peptides and free amino acids to be used as nutrients by fungi.18 One of these proteins is filaggrin that acts in assembling of keratin bundles.
Serine proteases are found in the exopeptidase, endopeptidase, oligopeptidase, and omegapeptidase groups [4, 5].
The presence of intestinal serine proteases in Oemona hirta Fabricius (Cerambycidae), also was supported by proteolytic assays using a general substrate and specific chemical inhibitors, which showed that only serine protease inhibitors had effect on total proteolytic activity; the predominant endopeptidase activity was attributed to trypsin and chymotrypsin-like proteases while, exopeptidase was related to leucine aminopeptidase.
DPP4 is a serine exopeptidase and processes the substrates that have either N-terminal proline or alanine including glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP) known as incretin hormones.
A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery.
Flavourzyme that is an exopeptidase, produced the lowest amount of peptide with small molecular size (15.4% and 19.8% of soybean and rice, respectively), whereas Alcalase as the strongest endopeptidase in this study can provide the most amount of peptides with small sizes (<4 kDa) (Figure 1).
Flavorpro[TM] 937MDP is an exopeptidase preparation with low levels of endopeptidase activity.
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."
This is because trypsin and potentially other enzymes used for sequencing do not efficiently cleave off a C-terminal lysine or arginine even if the penultimate residue is also a cleavage site; that is, they exhibit poor exopeptidase activity.
Exopeptidases have also been shown to play an important role in petal senescence and the levels of exopeptidase and endopeptidase activities have been found to be developmentally regulated (Mahagamasekera & David, 2001).
Bitterness in cheese occurs when there is an imbalance of the production of bitter peptides by protease and endopeptidase enzymes, and involves their removal by exopeptidase enzymes.