Summary
| Name | LAP3
|
| Full Name | Cytosol aminopeptidase |
| Synonyms | Leucine aminopeptidase 3, LAP-3, Leucyl aminopeptidase, Peptidase S, Proline aminopeptidase, 3.4.11.5, Prolyl aminopeptidase | LAPEP, PEPS |
| Primary ID | P28838 |
| Links | - - ![]() |
| Type | protein |
| Relations | 1 |
| Inhibitors | Tosedostat |
| Function | Cytolosic 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. |
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Relations
| Regulator | Mechanism | target | score ℹ | |
|---|---|---|---|---|
| + | Tosedostat | down-regulates
chemical inhibition
|
LAP3 | 0.8 |
| Publications: | 1 | Organism: | Homo Sapiens | |
4.0
LAP3



chemical inhibition