Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.7 extracted from

  • Godoy, S.; Violot, S.; Boullanger, P.; Bouchu, M.N.; Leca-Bouvier, B.D.; Blum, L.J.; Girard-Egrot, A.P.
    Kinetics study of Bungarus fasciatus venom acetylcholinesterase immobilised on a Langmuir-Blodgett proteo-glycolipidic bilayer (2005), ChemBioChem, 6, 395-404.
    View publication on PubMed

Application

Application Comment Organism
biotechnology enzyme immobilised on a nanostructured Langmuir-Blodgett proteo-glycolipidic bilayer, directly interfaced with an efficient optical device. Direct investigation of the kinetic behaviour of enzyme Bungarus fasciatus

General Stability

General Stability Organism
enzyme immobilised on a Langmuir-Blodgett proteo-glycolipidic bilayer, stable for several weeks Bungarus fasciatus

Organism

Organism UniProt Comment Textmining
Bungarus fasciatus
-
immobilised on a Langmuir-Blodgett proteo-glycolipidic bilayer
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Bungarus fasciatus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
kinetic analysis of enzyme immobilised on a Langmuir-Blodgett proteo-glycolipidic bilayer Bungarus fasciatus