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Literature summary for 3.1.1.8 extracted from

  • Katalinic, M.; Rusak, G.; Domacinovic Barovic, J.; Sinko, G.; Jelic, D.; Antolovic, R.; Kovarik, Z.
    Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase (2010), Eur. J. Med. Chem., 45, 186-192.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
apigenin
-
Homo sapiens
fisetin
-
Homo sapiens
galangin
-
Homo sapiens
kaempferol
-
Homo sapiens
luteolin
-
Homo sapiens
additional information docking study show that flavonoids bind to the BChE active site by forming multiple hydrogen bonds and pi-pi interactions Homo sapiens
myricetin
-
Homo sapiens
quercetin
-
Homo sapiens
rutin
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P06276
-
-

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
propionylthiocholine + H2O
-
Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
BChE
-
Homo sapiens
butyrylcholinesterase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0069
-
galangin
-
Homo sapiens
0.0374
-
apigenin
-
Homo sapiens
0.043
-
kaempferol
-
Homo sapiens
0.068
-
quercetin
-
Homo sapiens
0.071
-
myricetin
-
Homo sapiens
0.09
-
fisetin
-
Homo sapiens
0.166
-
luteolin
-
Homo sapiens
0.5
-
rutin
-
Homo sapiens