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Literature summary for 3.1.1.7 extracted from

  • Wille, T.; Thiermann, H.; Worek, F.
    Effect of different buffers on kinetic properties of human acetylcholinesterase and the interaction with organophosphates and oximes (2011), Arch. Toxicol., 85, 193-198.
    View publication on PubMed

General Stability

General Stability Organism
compared to phosphate buffer, the inhibition and reactivation kinetics of human erythrocyte AChE are markedly changed by Tris and in part by MOPS, whereas Tyrode buffer shows similar results to phosphate buffer (0.1 M each) Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
paraoxon-ethyl
-
Homo sapiens
sarin
-
Homo sapiens
soman
-
Homo sapiens
VX (nerve agent)
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0714
-
Acetylcholine in 0.1 M MOPS buffer (pH 7.4), at 37°C Homo sapiens
0.0982
-
Acetylcholine in 0.1 M phosphate buffer (pH 7.4), at 37°C Homo sapiens
0.1
-
Acetylcholine in 0.1 M Tyrode buffer (pH 7.4), at 37°C Homo sapiens
0.1215
-
Acetylcholine in 0.1 M Tris buffer (pH 7.4), at 37°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
-
Homo sapiens choline + acetate
-
?

Synonyms

Synonyms Comment Organism
AChE
-
Homo sapiens