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Literature summary for 3.4.23.49 extracted from

  • Baaden, M.; Sansom, M.S.
    OmpT: molecular dynamics simulations of an outer membrane enzyme (2004), Biophys. J., 87, 2942-2953.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.49

Activating Compound

Activating Compound Comment Organism Structure
lipopolysaccharides required for activity, protein-lipid interactions, overview Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
PDB 1I78 crystal structure analysis with reversal of mutations A99S, K261G, and G217K required for crystallization Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane dimyristoylphosphatidylcholine lipid bilayer embedded beta-barrel Escherichia coli 19867
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val. active site structure, catalytic residues are Asp210 an His212, molecular dynamic simulations reveal substrate binding structure and structural requirements for the catalytic mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala-L-Arg-L-Arg-L-Ala + H2O model peptide substrate Escherichia coli L-Ala-L-Arg + L-Arg-L-Ala
-
 ?

Subunits

Subunits Comment Organism
More conformational flexibility of the outer membrane embedded enzyme, molecular dynamic simulation, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ompT
-
 Escherichia coli