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Expression of prokaryotic 1‐deoxy‐ d ‐xylulose‐5‐phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis
Author(s) -
Harker M.,
Bramley P.M.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00360-9
Subject(s) - escherichia coli , biosynthesis , bacillus subtilis , lycopene , biochemistry , atp synthase , carotenoid , chemistry , phosphatase , prenyltransferase , recombinant dna , bacteria , biology , enzyme , gene , genetics
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.