Lysosomal Pro-X carboxypeptidase
Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH (By similarity).
| Database | Links |
|---|---|
| UniProt | Q7TMR0 |
| PDB | Not available |
| BioGrid | Not available |
| BindingDB | Q7TMR0 |
| DrugBank | Not available |
| Guide to PHARMACOLOGY | Not available |
| PharmGKB | Not available |
| KEGG | mmu:72461 |
| BioCyc | Not available |
| Entrez Gene (GeneID) | 72461 |
| Metric | Mean Value | Standard Deviation |
|---|---|---|
| AUC | 0.9817 | 0.0029 |
| Accuracy | 0.9653 | 0.0038 |
| Sensitivity | 0.9711 | 0.0058 |
| Specificity | 0.96 | 0.0061 |
| BEDROC | 0.9971 | 0.0016 |
| MCC Threshold | 0.486 | N/A |
| MCC | 0.9204 | N/A |
| F-score Threshold | 0.486 | N/A |
| F-score | 0.959 | N/A |