Leucine aminopeptidase
Function
Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
Sequence Similarities
Belongs to the peptidase M17 family.
Cellular localization
- Cytoplasm
Alternative names
Cytosol aminopeptidase, Cysteinylglycine-S-conjugate dipeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase, LAP-3, LAP3