Regular Article
Phosphorylation of Farnesol by a Cell-Free System from Botryococcus braunii

https://doi.org/10.1006/bbrc.1994.1554Get rights and content

Abstract

Farnesol was incorporated into squalene as well as botryococcenes when the alcohol was fed to the culture of Botryococcus braunii B race strain. In in vitro experiments with a 10,000 × g supernatant of cell homogenate, squalene was synthesized from farnesyl diphosphate in the presence of NADPH or NADH, but botryococcenes were not synthesized under the same conditions. A 100,000 × g pelet fraction was able to phosphorylate farnesol to give its mono- and diphosphate esters in a CTP dependent manner.

References (0)

Cited by (26)

  • High-value chemicals from Botryococcus braunii and their current applications – A review

    2019, Bioresource Technology
    Citation Excerpt :

    The parental C30 botryococcene is further modified by triterpene methyltransferases using S-adenosyl methionine as the methyl donor and converted into a variety of homologues of botryococcenes (Metzger et al., 1986a,b; Niehaus et al., 2012; Wolf et al., 1985). Though most part of farnesyl diphosphate used for biosynthesis of triterpenes such as botryococcene and squalene must be biosynthesized by farnesyl diphosphate synthase using isopentenyl diphosphate and dimethylally diphosphate, B. braunii also possesses kinase activities to convert farnesol into farnesyl diphosphate (Inoue et al., 1994). The roles of such kinases in the triterpene biosynthesis by B. braunii is not known yet.

  • A salvage pathway for phytol metabolism in Arabidopsis

    2006, Journal of Biological Chemistry
    Citation Excerpt :

    Salvage pathways for the reactivation of free isoprenoid alcohols have been identified previously. Phosphorylation of free isoprenoid alcohols was described for farnesol in bacteria (31), rat (32, 33), and in tobacco cell cultures (26). Geranylgeraniol kinase and geranylgeranyl-phosphate kinase activities were detected in the archae-bacterium Sulfolobus and tobacco (26, 27).

  • Characterization of botryococcene synthase enzyme activity, a squalene synthase-like activity from the green microalga Botryococcus braunii, Race B

    2004, Archives of Biochemistry and Biophysics
    Citation Excerpt :

    The nature of the direct precursor for botryococcene biosynthesis has generated much speculation. Previous studies have shown incorporation of radiolabeled farnesol [23,24] and farnesal [23] as well as 3-hydroxy-2,3-dihydrofarnesal [23] into botryococcenes in vivo. However, incorporation of FPP into botryococcenes in vitro was not observed, perhaps as a consequence of the Triton X-100 and BSA used in these assays [24].

View all citing articles on Scopus
View full text