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Cloning and heterologous expression of a cDNA encoding l-deoxy-D-xylulose-5-phosphate reductoisomerase of Arabidopsis thaliana1

Tipo de material: TextoTextoSeries ; FEBS Letters, 455, p.140-144, 1999Trabajos contenidos:
  • Schwender, J
  • Muller, Ch
  • Zeidler, J
  • Lichtenthaler, H.K
Tema(s): Recursos en línea: Resumen: Various plant isoprenoids are synthesized via the nonmevalonate 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 pecifically inhibits this DXR enzyme activity.
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Various plant isoprenoids are synthesized via the nonmevalonate 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 pecifically inhibits this DXR enzyme activity.

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