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Exopeptidase

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Class of enzymes
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Anexopeptidase is anypeptidase thatcatalyzes the cleavage of the terminal (or the penultimate)peptide bond; the process releases a singleamino acid,dipeptide or atripeptide from the peptide chain.[1] Depending on whether the amino acid is released from the amino or the carboxy terminal (N-terminus orC-terminus), an exopeptidase is further classified as an aminopeptidase or a carboxypeptidase, respectively. Thus, anaminopeptidase, an enzyme in thebrush border of thesmall intestine, will cleave a single amino acid from the amino terminal, whereascarboxypeptidase, which is adigestive enzyme present inpancreatic juice, will cleave a single amino acid from the carboxylic end of the peptide.

Some examples of exopeptidases include:[1]

See also

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External links

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References

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  1. ^abŠkárka, Bohumil (1992).Biochémia (in Slovak). Bratislava: Alfa. pp. 360, 688.ISBN 80-05-01076-1.
  2. ^"Definition of prolinase | Dictionary.com".www.dictionary.com. Archived fromthe original on 2022-04-09. Retrieved2022-04-09.
  3. ^Namiduru, E. S. (2016)."Prolidase".Bratislavske Lekarske Listy.117 (8):480–485.doi:10.4149/bll_2016_093.ISSN 0006-9248.PMID 27546702.
3.4.11-19:Exopeptidase
3.4.11
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3.4.16
3.4.17
Other/ungrouped
3.4.21-25:Endopeptidase
3.4.99: Unknown
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