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 ?
A total of about 30 families of metalloproteases have been documented, out of which 17 contain only endopeptidases, 12 contain only exopeptidases, and 1 (M3) contains both endo- and exopeptidases [4, 5] (Table 1).
Serine proteases are found in the exopeptidase, endopeptidase, oligopeptidase, and omegapeptidase groups [4, 5].
A sequence-specific exopeptidase activity test (SSEAT) for functional biomarker discovery.
A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery.
It was hypothesized that these are derived ex vivo during clotting, representing surrogate markers generated by alterations in serum concentrations or activities of the tumor-derived exopeptidases.
These patterns originate from proteolytic processing of high-abundant proteins ex vivo by a multitude of proteases that include endopeptidases and exopeptidases (14).
Peptides of similar antigenicity are often formed by posttranslational modifications essential for physiological function or consecutive peptide chain truncation by exopeptidases.
Fibrinopeptide A is released faster than fibrinopeptide B, and the fibrinopeptides are trimmed by exopeptidases; hence, the amounts and molecular forms of these short peptides depend on the extent and duration of clotting of an individual specimen (38-40).
Multiple molecular forms of serum amyloid A, related to trimming of the peptide chain by exopeptidase, have been noted by MALDI- or SELDI-TOF MS (30, 46-50).
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).
Addition of plant protein hydrolysates into the medium without FBS had shown a slight improvement in the cell growth (cell died after 4 to 5 days) with hydrolysates from Alcalase for both soybean and rice hydrolysates (Figure 2A and 2B).The protein extracts by Flavourzyme as an exopeptidase did not have significant effect on cell culture.
Flavorpro[TM] 937MDP is an exopeptidase preparation with low levels of endopeptidase activity.