Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
Belongs to peptidase family S26.,
Cleaves a single bond -Ala-|-Ala-in M13 phage procoat protein, producing free signal peptide and coat protein.,
Eukaryote signal peptidases that may have somewhat different specificity are known from the endoplasmic reticulum membrane and mitochondrial inner membrane.,
Unaffected by inhibitors of most serine peptidases, but site-directed mutagenesis implicates a Ser/Lys catalytic dyad in activity.
|
| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
Bacterial leader peptidase I,
Phage-procoat-leader peptidase,
SPase I,
Signal peptidase I
|
| uniprot:replaces | |
| uniprot:activity |
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
|