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Literature summary for 3.1.1.7 extracted from

  • Komersova, A.; Kovarova, M.; Komers, K.; Lochar, V.; Cegan, A.
    Why is the hydrolytic activity of acetylcholinesterase pH dependent? Kinetic study of acetylcholine and acetylthiocholine hydrolysis catalyzed by acetylcholinesterase from electric eel (2018), Z. Naturforsch. C, 73, 345-351 .
No PubMed abstract available
Search for more literature for 3.1.1.7

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetic analysis and modelling with increasing pH of the reaction mixture with substrate acetlycholine and acetylthiocholine, deteiled overview Electrophorus electricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylcholine + H2O Electrophorus electricus
-
 choline + acetate
-
 ?

Organism

Organism UniProt Comment Textmining
Electrophorus electricus O42275
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Electrophorus electricus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylcholine + H2O
-
 Electrophorus electricus choline + acetate
-
 ?
acetylthiocholine + H2O
-
 Electrophorus electricus thiocholine + acetate
-
 ?

Synonyms

Synonyms Comment Organism
AChE
-
 Electrophorus electricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Electrophorus electricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9.5
-
 Electrophorus electricus

pH Range

pH Minimum pH Maximum Comment Organism
4.8 9.8 at this pH range, the enzyme activity forms a sigmoid increasing curve with maximum catalytic activity at pH 8.0-9.5 Electrophorus electricus