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Literature summary extracted from

  • Pickett, J.S.; Bowers, K.E.; Hartman, H.L.; Fu, H.W.; Embry, A.C.; Casey, P.J.; Fierke, C.A.
    Kinetic studies of protein farnesyltransferase mutants establish active substrate conformation (2003), Biochemistry, 42, 9741-9748.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.5.1.58 medicine
-
 Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.58 wild-type enzyme and mutant enzymes expressed in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.58 H248A beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 10fold decreased in comparison of wild-type, the rate constant by chemical step using farnesyl monophosphate 5fold decreased Rattus norvegicus
2.5.1.58 K164A alpha-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 30fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate unaffected Rattus norvegicus
2.5.1.58 additional information mutations have a little effect on the pH and magnesium dependence: side chains K164alpha, H248beta and Y300beta not function either as general acid-base catalyst or as magnesium ligands Rattus norvegicus
2.5.1.58 Y300F beta-subunit, mutation has no effect on substrate binding affinity, the farnesylation rate constant is 500fold decreased in comparison of wild-type enzyme, the rate constant by chemical step using farnesyl monophosphate 300fold decreased. Transition state for farnesylation is stabilized by interactions between the alpha-phosphate of the isoprenoid substrate and the side chains of Y300beta Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.58 Zn2+ zinc metalloenzyme Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.58 Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.58 farnesyl diphosphate + protein-cysteine prenylation, farnesylation, substrates are Ras, nuclear lamins, transducin gamma subunit, protein substrate motif: Cys-aliphatic-aliphatic-X, X: M, S, Q, A, F Rattus norvegicus diphosphate + S-farnesyl protein
-
 ?
2.5.1.58 farnesyl monophosphate + Gly-Cys-Val-Leu-Ser
-
 Rattus norvegicus phosphate + Gly-S-farnesyl-Cys-Val-Leu-Ser
-
 ?