exopeptidase

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exopeptidase

 [ek″so-pep´tĭ-dās]
a proteolytic enzyme whose action is limited to terminal peptide linkages.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

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.
Farlex Partner Medical Dictionary © Farlex 2012

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.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

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
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

exopeptidase

An enzyme that acts to split off AMINO ACIDS or sometimes dipeptides from the ends of a protein molecule.
Collins Dictionary of Medicine © Robert M. Youngson 2004, 2005

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.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
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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].
The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries
A sequence-specific exopeptidase activity test (SSEAT) for functional biomarker discovery.
Mass-encoded, synthetic biomarkers and multiplexed urinary monitoring: new frontiers in disease monitoring
A sequence-specific exopeptidase activity test (SSEAT) for "functional" biomarker discovery.
Cancer biomarker discovery via low molecular weight serum profiling--are we following circular paths?
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.
Peptides generated ex vivo from serum proteins by tumor-specific exopeptidases are not useful biomarkers in ovarian cancer
These patterns originate from proteolytic processing of high-abundant proteins ex vivo by a multitude of proteases that include endopeptidases and exopeptidases (14).
Endoprotease profiling with double-tagged peptide substrates: a new diagnostic approach in oncology
Peptides of similar antigenicity are often formed by posttranslational modifications essential for physiological function or consecutive peptide chain truncation by exopeptidases.
Simultaneous quantification of ghrelin and desacyl-ghrelin by liquid chromatography--tandem mass spectrometry in plasma, serum, and cell supernatants
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).
The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
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.
Plant protein hydrolysates from soybean and rice grain as a supplement for medium in human skin fibroblast 1184 cell culture
Flavorpro[TM] 937MDP is an exopeptidase preparation with low levels of endopeptidase activity.
Biocatalysts' Flavorpro[TM] 937MDP and Promod[TM] 782MDP

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