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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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Human liver prenyltransferase and its characterization

Biochimica Et Biophysica Acta - Biomembranes, 1981
Prenyltransferase (dimethylallydiphosphate: isopentenyldiphosphate dimethylallytransferase, EC 2.5.1.1) has been purified to homogeneity from human liver obtained at autopsy. The enzyme is a dimer with a native molecular weight of 74 000 +/- 1 400. The amino acid composition is reported.
G Popják
exaly   +3 more sources

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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Reactivity of artificial substrates for prenyltransferase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Four compounds out of 6 new allylic pyrophosphates synthesized were found to act as artificial substrates for pig liver prenyltransferase (dimethylallylpyrophosphate:isopentenylpyrophosphate dimethylallyltransferase, EC 2.5.1.1). These were cyclopentylideneethyl, cyclohexylideneethyl, trans-3-ethyl-2-hexenyl, and cis-3-ethyl-2-hexenyl pyrophosphates. 2-
T, Nishino, K, Ogura, S, Seto
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