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.
| Database | Links |
|---|---|
| UniProt | P42785 |
| PDB | 3N2Z |
| BioGrid | 111538 |
| BindingDB | P42785 |
| DrugBank | Not available |
| Guide to PHARMACOLOGY | Not available |
| PharmGKB | PA33705 |
| KEGG | hsa:5547 |
| BioCyc | Not available |
| Entrez Gene (GeneID) | 5547 |
| Metric | Mean Value | Standard Deviation |
|---|---|---|
| AUC | 0.9851 | 0.003 |
| Accuracy | 0.9505 | 0.0066 |
| Sensitivity | 0.9494 | 0.0112 |
| Specificity | 0.9516 | 0.0069 |
| BEDROC | 0.9981 | 0.0012 |
| MCC Threshold | 0.432 | N/A |
| MCC | 0.8948 | N/A |
| F-score Threshold | 0.432 | N/A |
| F-score | 0.9474 | N/A |