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Literature summary for 3.4.21.89 extracted from

  • Luo, C.; Roussel, P.; Dreier, J.; Page, M.G.; Paetzel, M.
    Crystallographic analysis of bacterial signal peptidase in ternary complex with arylomycin A2 and a beta-sultam inhibitor (2009), Biochemistry, 48, 8976-8984.
    View publication on PubMed

Application

Application Comment Organism
drug development SPase I is a target for development of inhibitors as antibiotics Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
soluble catalytic domain of SSPase I in ternary complex with inhibitors arylomycin A2 and BAL0019193, sitting drop vapor diffusion method at 18°C, mixing of 0.002 ml of protein solution and of reservoir solution, containing 0.2 M ammonium formate, 25% PEG 2000, 0.1 M sodium cacodylate pH 6.5, and 5% tertiary-amyl alcohol, equilibration over 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
arylomycin A2 a lipohexapeptide-based natural product, inhibits SPase I by binding to non-overlapping subsites near the catalytic center in a noncovalent manner, binding mode, overview Escherichia coli
BAL0019193 a morpholino-beta-sultam derivative, inhibits SPase I by binding to non-overlapping subsites near the catalytic center in a noncovalent manner, binding mode, overview Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Escherichia coli 5783
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P00803
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SPase I is an essential membrane-bound endopeptidase with a unique Ser/Lys dyad mechanism Escherichia coli ?
-
?

Synonyms

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