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metalloexopeptidase

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Also known as metalloexopeptidases

A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase. These enzymes have a catalytic mechanism involving a metal, often zinc. They function in molecular biology as agents that cut the terminal (or penultimate) peptide bonds ending peptide chains. Analogous to slicing the end off a loaf of bread, the process releases a single amino acid (or dipeptide) for use.

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EC enzyme number
3.4.17.-
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Encyclopedic overview

5 sections
Contents
  • Metallocarboxypeptidase
  • Enzyme Commission number
  • See also
  • References
  • External links

A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase. These enzymes have a catalytic mechanism involving a metal, often zinc. They function in molecular biology as agents that cut the terminal (or penultimate) peptide bonds ending peptide chains. Analogous to slicing the end off a loaf of bread, the process releases a single amino acid (or dipeptide) for use.

== Metallocarboxypeptidase == The terms "metallo carboxypeptidase", "metallo-carboxypeptidase" and "metallocarboxypeptidase" are used to describe a metalloexopeptidase carboxypeptidase. These peptidases specifically target the C-terminus, the unbound carboxyl group (-COOH) at one distinct end of the amino acid chain (cutting one side from a loaf of bread rather than the end).

Excerpted from Wikipedia’s “metalloexopeptidase” article, available under the CC BY-SA 4.0 licence.

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