Cloned (Comment) | Organism |
---|---|
expression of a soluble form of signal peptidase, which lacks the two transmembrane domains, SPase I DELTA2-75 | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
additional information | expression of a soluble form of signal peptidase, which lacks the two transmembrane domains, SPase I DELTA2-75 | Escherichia coli |
additional information | variant DELTA2-75 is a soluble form of signal peptidase, which lacks the two transmembrane domains | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | signal peptide substrate remains in the bilayer and the enzyme active site functions at the membrane surface | Escherichia coli | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alkaline phosphatase signal peptide | clear evidence of a weak peptide-enzyme complex formation. The peptide adopts a U-turn shape originating from the proline residues within the primary sequence that is stabilized by its interaction with the peptidase and leaves key residues of the cleavage region exposed for proteolysis. In dodecylphosphocholine micelles the signal peptide also adopts a U-turn shape comparable with that observed in association with the enzyme. In both environments this conformation is stabilized by the signal peptide phenylalanine side chain-interaction with enzyme or lipid mimetic. In the presence of dodecylphosphocholine, the N-terminal core region residues of the peptide adopt a helical motif and are buried within the membrane. This is consistent with proteolysis of the preprotein occurring while the signal peptide remains in the bilayer and the enzyme active site functions at the membrane surface | Escherichia coli | ? | - |
? | |
additional information | binding of the signal petide to the sinal peptidase leads to weak peptide-enzyme complex formation. The peptide adopts a U-turn shape originating from the proline residues within the primary sequence that is stabilized by its interaction with the peptidase and leaves key residues of the cleavage region exposed for proteolysis. In dodecylphosphocholine micelles the signal peptide also adopts a U-turn shape comparable with that observed in association with the enzyme. In both environments this conformation is stabilized by the signal peptide phenylalanine side chain-interaction with enzyme or lipid mimetic. In the presence of dodecylphosphocholine, the N-terminal core region residues of the peptide adopt a helical motif are buried within the membrane | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Spase I | - |
Escherichia coli |