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Literature summary for 2.5.1.58 extracted from

  • Cui, G.; Merz, K.M.
    Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate (2007), Biochemistry, 46, 12375-12381.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.58

Protein Variants

Protein Variants Comment Organism
Y300F the mutation adversely affects the reaction rate constant by 500fold under optimal catalytic conditions Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens
Zn2+ zinc metalloenzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + Ras-Cys-Val-Ile-Met
-
 Homo sapiens diphosphate + Ras-S-farnesyl-Cys-Val-Ile-Met
-
 ?
farnesyl diphosphate + Ras-Cys-Val-Leu-Met
-
 Homo sapiens diphosphate + Ras-S-farnesyl-Cys-Val-Leu-Met
-
 ?
farnesyl triphosphate + [Ras]-Cys-Val-Ile-Met
-
 Homo sapiens triphosphate + [Ras]-S-farnesyl-Cys-Val-Ile-Met
-
 ?

Synonyms

Synonyms Comment Organism
farnesyltransferase ternary complex part II
-
 Homo sapiens
FTase
-
 Homo sapiens