Add time:09/24/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes the synthesis of an affinity column for FARNESYLPYROPHOSPHATE (cas 13058-04-3) synthetase based on the geranyl moiety and a rapid purification of the enzyme from avian liver and yeast. Farnesylpyrophosphate synthetase is a 1'-4 prenyltransferase that produces a key intermediate in the isoprenoid pathway, which is the precursor for a variety of essential metabolites, including sterols, ubiquinones, dolichols, and some hemes. The enzyme synthesizes (E,E)-farnesyl pyrophosphate from dimethylallyl pyrophosphate and two molecules of isopentenyl pyrophosphate in two steps. Beginning with dimethylallyl pyrophosphate, a variety of products that differ in the length of the isoprenoid chain and the stereochemistry of the double bonds can be formed. A family of enzymes catalyzes 1'-4 prenyl transfers. Individual members present different substrate specificities based on chain length and double bond stereochemistry of the allylic substrate and produce five carbon homologs with exclusively E or Z trisubstituted double bonds. In principle, it should be possible to use the different substrate specificities to purify selectively individual members of the family from a crude homogenate by affinity chromatography. The product of the first step, geranyl pyrophosphate, binds to the enzyme more tightly than the other substrates or the final product and is therefore a logical candidate for the ligand in an affinity column to purify the enzyme.

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