Expression of prokaryotic 1-deoxy-D-xylulose-5-phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis

FEBS Lett. 1999 Apr 1;448(1):115-9. doi: 10.1016/s0014-5793(99)00360-9.

Abstract

Isopentenyl diphosphate (IPP) acts as the common, five-carbon building block in the biosynthesis of all isoprenoids. The first reaction of IPP biosynthesis in Escherichia coli is the formation of 1-deoxy-D-xylulose-5-phosphate, catalysed by 1-deoxy-D-xylulose-5-phosphate synthase (DXPS). E. coli engineered to produce lycopene, was transformed with dxps genes cloned from Bacillus subtilis and Synechocystis sp. 6803. Increases in lycopene levels were observed in strains expressing exogenous DXPS compared to controls. The recombinant strains also exhibited elevated levels of ubiquinone-8. These increases corresponded with enhanced DXP synthase activity in the recombinant E. coli strains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carotenoids / biosynthesis*
  • Cloning, Molecular
  • Escherichia coli / enzymology
  • Gene Expression
  • Genes, Bacterial
  • Lycopene
  • Molecular Sequence Data
  • Pentosephosphates / biosynthesis*
  • Prokaryotic Cells
  • Sequence Homology, Amino Acid
  • Transferases / biosynthesis*
  • Transferases / genetics
  • Ubiquinone / biosynthesis*

Substances

  • 1-deoxylulose 5-phosphate
  • Pentosephosphates
  • Ubiquinone
  • Carotenoids
  • ubiquinone 8
  • Transferases
  • deoxyxylulose-5-phosphate synthase
  • Lycopene