| Tissue Specificity | |
| Post Translational Modifications | |
| 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. |
| Protein Name | Cytosol AminopeptidaseCysteinylglycine-S-Conjugate DipeptidaseLeucine Aminopeptidase 3Lap-3Leucyl AminopeptidasePeptidase SProline AminopeptidaseProlyl Aminopeptidase |
| Database Links | |
| Cellular Localisation | Cytoplasm |
| Alternative ELISA Names | Cytosol Aminopeptidase ELISA kitCysteinylglycine-S-Conjugate Dipeptidase ELISA kitLeucine Aminopeptidase 3 ELISA kitLap-3 ELISA kitLeucyl Aminopeptidase ELISA kitPeptidase S ELISA kitProline Aminopeptidase ELISA kitProlyl Aminopeptidase ELISA kitLAP3 ELISA kitLAPEP ELISA kitPEPS ELISA kit |
| output | |
Information sourced from Uniprot.org
