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Literature summary extracted from

  • Nachon, F.; Stojan, J.; Fournier, D.
    Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel (2008), FEBS J., 275, 2659-2664.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.7 W83A mutational enlarging of a channel located at the bottom of the active site gorge in the Drosophila enzyme. Mutation of Trp83 to Ala or Glu widens the channel from 5 A to 9 A. The kinetics of substrate hydrolysis and the effect of ligands that close the main entrance, overview. In mutant W83A ligands that close the main entrance do not inhibit substrate hydrolysis because the traffic can pass via an alternative route Drosophila melanogaster
3.1.1.7 W83E mutational enlarging of a channel located at the bottom of the active site gorge in the Drosophila enzyme. Mutation of Trp83 to Ala or Glu widens the channel from 5 A to 9 A. The kinetics of substrate hydrolysis and the effect of ligands that close the main entrance, overview. In mutant W83E ligands that close the main entrance do not inhibit substrate hydrolysis because the traffic can pass via an alternative route Drosophila melanogaster

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.7 additional information
-
additional information substrate binding kinetics of wild-type and mutant enzymes, overview Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.7 Drosophila melanogaster P07140
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.7 acetylthiocholine iodide + H2O detection with 5,5'-dithio-bis-2-nitrobenzoic acid, i.e. DTNB Drosophila melanogaster acetate + thiocholine iodide
-
?
3.1.1.7 additional information active site structure and substrate channels of wild-type and mutant enzymes, overview Drosophila melanogaster ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.7 25
-
assay at Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.7 7
-
assay at Drosophila melanogaster