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Literature summary for 3.4.23.49 extracted from

  • Vandeputte-Rutten, L.; Kramer, R.A.; Kroon, J.; Dekker, N.; Egmond, M.R.; Gros, P.
    Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site (2001), EMBO J., 20, 5033-5039.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
lipopolysaccharide displays enzymatic activity in vitro only in presence Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed without its signal sequence in Escherichia coli K-12 strain DH5alpha using a T7 system Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, space group P3(2)21, unit cell parameters a : B : 98.39 A, c : 165.70 A Escherichia coli

Protein Variants

Protein Variants Comment Organism
G216K/K217G recombinant ompT variant in order to abolish autoproteolysis Escherichia coli
S99A/G216K/K217G recombinant ompT variant in order to abolish autoproteolysis Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protease, outer membrane, membrane bound Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Synonyms

Synonyms Comment Organism
ompT
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Escherichia coli