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Cloning and heterologous expression of a cDNA encoding 1‐deoxy‐ D ‐xylulose‐5‐phosphate reductoisomerase of Arabidopsis thaliana 1
Author(s) -
Schwender Jörg,
Müller Christian,
Zeidler Johannes,
Lichtenthaler Hartmut K.
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)00849-2
Subject(s) - escherichia coli , heterologous expression , arabidopsis thaliana , complementary dna , biochemistry , cloning (programming) , biology , heterologous , microbiology and biotechnology , chemistry , gene , recombinant dna , mutant , computer science , programming language
Various plant isoprenoids are synthesized via the non‐mevalonate pathway of isopentenyl diphosphate formation. In this pathway, 1‐deoxy‐ D ‐xylulose 5‐phosphate (DOXP), the first intermediate, is transformed to 2‐ C ‐methyl‐ D ‐erythritol 4‐phosphate (MEP) by an enzyme which was recently cloned from Escherichia coli . In order to find a plant homologue of this 1‐deoxy‐ D ‐xylulose 5‐phosphate reductoisomerase (DXR) we cloned a cDNA fragment from Arabidopsis thaliana which has high homology to the E. coli DXR. By expression of this fragment in E. coli we could demonstrate that it encodes a protein which transforms DOXP to MEP. The antibiotic fosmidomycin specifically inhibits this DXR enzyme activity.