Metalloexopeptidase

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).

Enzyme Commission number

Using the Enzyme Commission number (EC number) system, metallocarboxypeptidases fall under EC 3.4.17.[1] Examples of these compounds in the human genome include AGBL1 and AGBL2, known also as ATP/GTP Binding Protein-Like 1 and 2, respectively. The former resides in Chromosome 15 and is made up of 951,392 base pairs (bases) while the latter resides in Chromosome 11 and is made up of 56,221 bases.[2][3]

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gollark: Botania has the Ring of Odin, which gives extra health and such, which is very cool and good if you can get it.
gollark: Never mind, I went to look at it now, and it has begun working inexplicably.
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See also

References
  1. "ENZYME: 3.4.17.-". enzyme.expasy.org. Retrieved 2016-05-21.
  2. "AGBL1". www.genecards.org. Retrieved 2016-05-21.
  3. "AGBL2". www.genecards.org. Retrieved 2016-05-21.


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