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Literature summary for 3.1.1.8 extracted from

  • Reiner, E.; Simeon-Rudolf, V.; Skrinjaric-Spoljar, M.
    Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera (1995), Toxicol. Lett., 82/83, 447-452.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
4,4'-Bipyridine competitive, reversible Homo sapiens
HI 6 competitive, reversible Homo sapiens
additional information enzyme variants usual, fluoride resistant, and atypical differ in rates of inhibition by the charged organophosphates and carbamates Homo sapiens
PAM-2 competitive, reversible Homo sapiens
phosphostigmine competitive, reversible Homo sapiens
Ro 02-0683 progressive inhibitor Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.56
-
acetylthiocholine usual variant Homo sapiens
0.57
-
propionylthiocholine atypical variant Homo sapiens
0.7
-
propionylthiocholine fluoride resistant variant Homo sapiens
0.71
-
acetylthiocholine fluoride resistant variant Homo sapiens
0.76
-
propionylthiocholine usual variant Homo sapiens
0.96
-
acetylthiocholine atypical variant Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
serum
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylthiocholine + H2O
-
Homo sapiens acetate + thiocholine
-
?
propionylthiocholine + H2O propylthiocholine Homo sapiens propanoate + thiocholine
-
?

Synonyms

Synonyms Comment Organism
butyrylcholinesterase
-
Homo sapiens