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Literature summary for 3.1.1.8 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
Search for more literature for 3.1.1.8

General Stability

General Stability Organism
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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer non-denaturing PAGE Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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