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Prenyltransferase: the mechanism of the reaction

Biochemistry, 1976
The enzyme, prenyltransferase, which normally catalyzes the addition of an allylic pyrophosphate to isopentenyl pyrophosphate, has been found to catalyze the hydrolysis of its allylic substrate. The rate of this hydrolysis is markedly stimulated by inorganic pyrophosphate.
C D, Poulter, H C, Rilling
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Understanding and Exploiting Protein Prenyltransferases

ChemBioChem, 2010
(Chemical Equation Presented) Lipidating proteins: Protein prenylation is catalyzed by protein prenyltransferases, and enables proteins to reversibly associate with intracellular membranes. The mechanisms of protein prenylation and the recent developments in analysis and biotechnological exploitation of these modifications are reviewed.
Nguyen, Uyen T. T.   +2 more
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Natural Inhibitors for Protein Prenyltransferase

Planta Medica, 1998
Farnesyl protein transferase (FPT) catalyzes the posttranslational farnesylation of the cysteine residue located in the carboxyl-terminal tetrapeptide of the Ras oncoprotein. Prenylation of this residue is essential for membrane association and cell transforming activities of Ras.
S, Lee, S, Park, J W, Oh, C, Yang
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Geranylation of Chalcones by a Fungal Aromatic Prenyltransferase

Journal of Agricultural and Food Chemistry, 2023
Geranylated chalcones mainly exist in plants, and many of them have attracted attention because of their diverse pharmacological and biological activities. Herein, we report geranylation of eight chalcones by the Aspergillus terreus aromatic prenyltransferase AtaPT.
Qianqian Ran   +6 more
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An affinity column for the purification of prenyltransferases

Analytical Biochemistry, 1985
Farnesyl pyrophosphate synthetase (EC 2.5.1.1) from chicken liver, pig liver, and yeast has been purified to homogeneity in a single chromatographic step by affinity chromatography. The affinity ligand, geranylmethylphosphonophosphate, is linked to Affi-Gel 10 through the phosphonophosphate moiety. The affinity gel is stable chemically and the internal
D L, Bartlett, C H, King, C D, Poulter
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Prenyltransferase from Gossypium hirsutum

Archives of Biochemistry and Biophysics, 1980
Abstract A protein fraction has been purified from Gossypium hirsutum var. Coker 413 which synthesized all four geometrical isomers of farnesyl pyrophosphate from isopentenyl pyrophosphate alone, from isopentenyl pyrophosphate and geranyl or neryl pyrophosphate. Electrophoretic analysis showed that this protein fraction consisted of three proteins.
R, Widmaier, J, Howe, P, Heinstein
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