A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. (Contrast with an aminopeptidase, which cleaves peptide bonds at the other end of the protein.) Humans, animals, and plants contain several types of carboxypeptidases that ha...
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http://en.wikipedia.org/wiki/Carboxypeptidase
(from the article `protein`) ...the enzyme surface and induces a change in its shape that results in the correct alignment of the catalytic groups (indicated by triangles A and ...
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http://www.britannica.com/eb/a-z/c/23
<enzyme> Enzymes (particularly of pancreas) that remove the C terminal amino acid from a protein or peptide. Carboxypeptidase A, will remove any amino acid, carboxypeptidase B is specific for terminal lysine or arginine. ... (18 Nov 1997) ...
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(kahr-bok″se-pep´tĭ-dās) an exopeptidase that acts only on the peptide linkage of a terminal amino acid that has a free carboxyl group.
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Enzyme that cleaves amino acids from a protein chain commencing at the C-terminal
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Enzymes (particularly of pancreas) that remove the C-terminal amino acid from a protein or peptide. Carboxypeptidase A, (EC 3.4.17.1) will remove any amino acid; carboxypeptidase B (EC 3.4.17.2) is specific for terminal lysine or arginine.
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Type: Term Pronunciation: kar-bok′sē-pep′ti-dās Definitions: 1. A hydrolase that removes the amino acid at the free carboxyl end of a polypeptide chain; an exopeptidase.
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