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Literature summary for 3.1.1.8 extracted from

  • Nachon, F.; Nicolet, Y.; Viguie, N.; Masson, P.; Fontecilla-Camps, J.C.; Lockridge, O.
    Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: expression, purification, characterization and crystallization (2002), Eur. J. Biochem., 269, 630-637.
    View publication on PubMed
Search for more literature for 3.1.1.8

Cloned(Commentary)

Cloned (Comment) Organism
monomeric enzyme, lacking four out of nine N-glycosylation sites and the C-terminal oligomerization domain, expressed in CHO cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
monomeric enzyme, lacking four out of nine N-glycosylation sites and the C-terminal oligomerization domain, hanging drop vapor diffusion method Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information mutant with only 5 N-glycosylation sites Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0256
-
 butyryl thiocholine iodide pH 7, mutant with only 5 N-glycosylation sites Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000 75000 SDS-PAGE, recombinant enzyme Homo sapiens
85000
-
 native enzyme, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein nine N-glycosylation sites Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
535
-
 butyryl thiocholine iodide pH 7, mutant with only 5 N-glycosylation sites Homo sapiens