Partial purification and properties of geranyl pyrophosphate synthase from Lithospermum erythrorhizon cell cultures.
A prenyltransferase (EC 2.5.1.1) was isolated from cell cultures of Lithospermum erythrorhizon. The enzyme was purified 92-fold by subsequent chromatography on DEAE-Sephacel, phenyl-Sepharose, and Sephadex G-150. Geranyl pyrophosphate (GPP) was the sole product of the enzymatic reaction with dimethylallyl pyrophosphate and isopentenyl pyrophosphate as the substrates. The enzyme showed a molecular weight of 73,000, estimated by gel chromatography on Sephadex G-150, and an isoelectric point at pH 4.95, determined by analytical isoelectric focusing. It had an absolute requirement for a divalent cation with Mg2+ and Mn2+ being most effective. The enzyme was soluble rather than membrane-bound. The physiological role of this prenyltransferase probably is to supply GPP for the biosynthesis of shikonin. It is the first chain-length specific geranyl pyrophosphate synthase reported from eukaryotic cells.
Institut für Pharmazeutische Biologie, Rheinische Friedrich-Wilhelms-Universität, West Germany.
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D055598:Chemical Phenomena; D002621:Chemistry; D002848:Chromatography, DEAE-Cellulose; D002849:Chromatography, Gas; D004122:Dimethylallyltranstransferase / Q000302:isolation & purification* / Q000378:metabolism; D005459:Fluorides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D009285:Naphthoquinones / Q000378:metabolism; D010946:Plants, Medicinal / Q000201:enzymology*; D014166:Transferases / Q000302:isolation & purification*
D009285:Naphthoquinones; C016101:shikonin; D008345:Manganese; D014166:Transferases; D004122:Dimethylallyltranstransferase; D008274:Magnesium; D005459:Fluorides