Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.58 extracted from

  • Pickett, J.S.; Bowers, K.E.; Fierke, C.A.
    Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand (2003), J. Biol. Chem., 278, 51243-51250.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Dbeta352A drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. The Km(Mg2+) increases 28-fold to 110 mM, and the farnesylation rate constant at saturating Mg2+ decreases 27-fold to 0.30 per s Rattus norvegicus
Dbeta352K drastically alters the Mg2+-dependence of FTase catalysis without dramatically affecting the rate constant of farnesylation minus magnesium or the binding affinity of either substrate. Mutation removes the magnesium activation of farnesylation catalyzed by FTase but does not significantly enhance the rate constant for farnesylation in the absence of Mg2+ Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ enhances activity several hundred-fold, with a Km(Mg2+) value of 4 mM. Mg2+ coordinates the side chain carboxylate of Asp-beta352 and that the role of magnesium in the reaction includes positioning the FPP prior to catalysis. Mg2+ may accelerate catalysis both by stabilizing developing negative charge in the transition state and by stabilizing the active site conformation prior to catalysis Rattus norvegicus
Mn2+ in wild type FTase, Mg2+ can be replaced by Mn2+ with a 2-fold lower KMn2+ 2 mM Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-