aminopeptidase

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American Heritage Dictionary:

a·mi·no·pep·ti·dase

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(ə-mē'nō-pĕp'tĭ-dās', -dāz', ăm'ə-) pronunciation
n.
Any of various enzymes that catalyze the hydrolysis of the terminal peptide bond at the amino end of a polypeptide.


An enzyme secreted in the pancreatic juice which removes amino acids sequentially from the free amino terminal of a peptide or protein (i.e. the end that has a free amino group exposed), until the final product is a dipeptide. Since it works at the end of the peptide chain, it is an exopeptidase.

(ə-mē'nō-pĕp'tĭ-dās', -dāz', ăm'ə-nō-)
n.

Any of various enzymes that catalyze the hydrolysis of the terminal peptide bond at the amino end of a polypeptide.


any enzyme of sub-subclass EC 3.4.11, α-aminoacylpeptide hydrolases, that hydrolyse N-terminal amino-acid residues from oligopeptides or polypeptides.

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An enzyme produced by the intestinal mucosa which completes the process of protein digestion by hydrolyzing the amino-terminal amino acids of peptides and some proteins, after the initial breakdown of protein to peptides has already taken place, e.g. the enzyme that removes the methionine coded by the initiation codon AUG.

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