Format

Send to

Choose Destination
Arch Biochem Biophys. 1989 Sep;273(2):331-8.

Partial purification and properties of geranyl pyrophosphate synthase from Lithospermum erythrorhizon cell cultures.

Author information

1
Institut für Pharmazeutische Biologie, Rheinische Friedrich-Wilhelms-Universität, West Germany.

Abstract

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.

PMID:
2774555
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center