Isolation of thedxrgene ofZymomonas mobilisand characterization of the 1-deoxy-D-xylulose 5-phosphate reductoisomerase
Open Access
- 1 October 2000
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 191 (1) , 131-137
- https://doi.org/10.1111/j.1574-6968.2000.tb09329.x
Abstract
The gene encoding the second enzyme of the 2C-methyl-D-erythritol 4-phosphate (MEP) pathway for isopentenyl diphosphate biosynthesis, 1-deoxy-D-xylulose 5-phosphate (DXP) reductoisomerase, was cloned and sequenced from Zymomonas mobilis. The deduced amino acid sequence showed the highest identity (48.2%) to the DXP reductoisomerase of Escherichia coli. Biochemical characterization of the purified DXP reductoisomerase showed a strict dependence of the enzyme on NADPH and divalent cations (Mn2+, Co2+ or Mg2+). The enzyme is a dimer with a molecular mass of 39 kDa per subunit and has a specific activity of 19.5 U mg protein−1. Catalysis of the intramolecular rearrangement and reduction of DXP to MEP is competitively inhibited by the antibiotic fosmidomycin with a Ki of 0.6 μM.Keywords
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