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- Title
LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis
- Authors
Altincicek, Boran; Duin, Evert C.; Reichenberg, Armin; Hedderich, Reiner; Kollas, Ann-Kristin; Hintz, Martin; Wagner, Stefanie; Wiesner, Jochen; Beck, Ewald; Jomaa, Hassan
- Abstract
Recombinant LytB protein from the thermophilic eubacterium Aquifex aeolicus produced in Escherichia coli was purified to apparent homogeneity. The purified LytB protein catalyzed the reduction of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate (HMBPP) in a defined in vitro system. The reaction products were identified as isopentenyl diphosphate and dimethylallyl diphosphate. A spectrophotometric assay was established to determine the steady-state kinetic parameters of LytB protein. The maximal specific activity of 6.6±0.3 μmol min−1 mg−1 protein was determined at pH 7.5 and 60°C. The kcat value of the LytB protein was 3.7±0.2 s−1 and the Km value for HMBPP was 590±60 μM.
- Subjects
RECOMBINANT proteins; THERMOPHILIC bacteria; ESCHERICHIA coli
- Publication
FEBS Letters, 2002, Vol 532, Issue 3, p437
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03726-2