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Literature summary extracted from

  • Weingand-Ziade, A.; Ribes, F.; Renault, F.; Masson, P.
    Pressure- and heat-induced inactivation of butyrylcholinesterase: evidence for multiple intermediates and the remnant inactivation process (2001), Biochem. J., 356, 487-493.
    View publication on PubMedView publication on EuropePMC

General Stability

EC Number General Stability Organism
3.1.1.8 pressure and heat lead to inactivation of the enzyme by irreversible formation of an active intermediate state and a denatured state Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.8 0.021
-
butyryl thiocholine pH 7, 22°C, native and intermediate state of the enzyme Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.8 340000
-
non-denaturing PAGE Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.8 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.8
-
Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.8 115
-
-
Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.8 butyrylthiocholine + H2O
-
Homo sapiens thiocholine + butyrate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.8 tetramer non-denaturing PAGE Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.8 additional information
-
pressure and heat lead to inactivation of the enzyme by irreversible formation of an active intermediate state and a denatured state Homo sapiens