Biosynthesis of terpenoids: 1‐deoxy‐D‐xylulose‐5‐phosphate reductoisomerase from Escherichia coli is a class B dehydrogenase

FEBS Letters

Rohdich, Felix¹  Eisenreich, Wolfgang¹  Arigoni, Duilio³  Kis, Klaus¹  Herz, Stefan¹  Bacher, Adelbert¹  Wungsintaweekul, Juraithip²  Zenk, Meinhart H.²  Radykewicz, Tanja¹ 

[1] Lehrstuhl für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr. 4, D-85747 Garching, Germany;Biozentrum, Martin-Luther-Universität Halle-Wittenberg, D-06099 Halle/Saale, Germany;Laboratorium für Organische Chemie, ETH Zürich, Universitätsstr. 16, CH-8092 Zürich, Switzerland

关键词: Deoxyxylulose;    Methylerythritol;    Terpenoid biosynthesis;    Stereochemistry;    Nuclear magnetic resonance;   

DOI  :  10.1016/S0014-5793(99)01743-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

1-Deoxy-D-xylulose-5-phosphate is converted into 2-C-methyl-D-erythritol-4-phosphate by the catalytic action of 1-deoxy-D-xylulose-5-phosphate reductoisomerase (Dxr protein) using NADPH as cofactor. The stereochemical features of this reaction were investigated in in vitro experiments with the recombinant Dxr protein of Escherichia coli using (4R)- or (4S)-[4-²H₁]NADPH as coenzyme. The enzymatically formed 2-C-methyl-D-erythritol-4-phosphate was isolated and converted into 1,2:3,4-di-O-isopropylidene-2-C-methyl-D-erythritol; NMR spectroscopic investigation of this derivative indicated that only (4S)-[4-²H₁]NADPH affords 2-C-methyl-D-erythritol-4-phosphate labelled exclusively in the H_Re position of C-1. Stereospecific transfer of H_Si from C-4 of the cofactor identifies the Dxr protein of E. coli as a class B dehydrogenase.

【 授权许可】

Unknown