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Literature summary extracted from

  • Armah, D.A.; Mensa-Wilmot, K.
    S-myristoylation of a glycosylphosphatidylinositol-specific phospholipase C in Trypanosoma brucei (1999), J. Biol. Chem., 274, 5931-5938.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.14 expression in Escherichia coli Trypanosoma brucei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.14 0.0017 0.002 Variant-surface-glycoprotein 37°C, deacylated enzyme Trypanosoma brucei
4.6.1.14 0.0026 0.0027 Variant-surface-glycoprotein 37°C, acylated enzyme Trypanosoma brucei

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.14 Trypanosoma brucei
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
4.6.1.14 side-chain modification co- and posttranslational thioacylation with myristate and palmitate Trypanosoma brucei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.14 variant-surface-glycoprotein
-
 Trypanosoma brucei 1,2-didecanoylglycerol + soluble variant-surface-glycoprotein
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.6.1.14 0.65 1.48 Variant-surface-glycoprotein 37°C, deacylated enzyme Trypanosoma brucei
4.6.1.14 19.8 27.3 Variant-surface-glycoprotein 37°C, acylated enzyme Trypanosoma brucei