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Literature summary for 3.4.21.89 extracted from

  • De Bona, P.; Deshmukh, L.; Gorbatyuk, V.; Vinogradova, O.; Kendall, D.A.
    Structural studies of a signal peptide in complex with signal peptidase I cytoplasmic domain: The stabilizing effect of membrane-mimetics on the acquired fold (2011), Proteins, 80, 807-817.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.89

Cloned(Commentary)

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

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

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
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

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 ?
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 ?
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 ?
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 ?

Synonyms

Synonyms Comment Organism
Spase I
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 Escherichia coli