Open AccessIsolation of the dxr gene of Zymomonas mobilis and characterization of the 1‐deoxy‐ D ‐xylulose 5‐phosphate reductoisomerase
Author(s) -
Grolle Sigrid,
BringerMeyer Stephanie,
Sahm Hermann
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09329.x
Subject(s) - zymomonas mobilis , chemistry , biochemistry , divalent , enzyme , biosynthesis , escherichia coli , stereochemistry , gene , organic chemistry , ethanol fuel , fermentation
The gene encoding the second enzyme of the 2 C ‐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 (Mn 2+ , Co 2+ or Mg 2+ ). 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 K i of 0.6 μM.