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Literature summary for 3.4.21.89 extracted from

  • Musial-Siwek, M.; Kendall, D.A.; Yeagle, P.L.
    Solution NMR of signal peptidase, a membrane protein (2008), Biochim. Biophys. Acta, 1778, 937-944.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.89

Activating Compound

Activating Compound Comment Organism Structure
dodecylphosphocholine at 37°C, degradation occurs to a lesser extent in dodecylphosphocholine micelles than in Triton X-100 or n-octyl-beta-D-glucopyranoside Escherichia coli
additional information no significant difference in expression levels in the presence and absence of deuterium oxide. Elevated temperature enhances enzyme degradation, at 37°C, the protein is autolysed and degraded more than at 22°C Escherichia coli
n-octyl-beta-D-glucopyranoside
-
 Escherichia coli
Triton X-100
-
 Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) cells transfected with the pET23b-coding SPase I plasmid Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane domain Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by centrifugation, gel filtration and on Ni-agarose resin Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cleaves the signal peptide of the GST-SP-AP-His construct into two fragments, the GST protein plus the signal peptide (28 kDa), and the first 30 amino acids of the mature region 6-His-tagged (4 kDa) Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Spase I
-
 Escherichia coli
type I signal peptidase
-
 Escherichia coli