| Literature DB >> 12482607 |
Ann-Kristin Kollas1, Evert C Duin, Matthias Eberl, Boran Altincicek, Martin Hintz, Armin Reichenberg, Dajana Henschker, Anke Henne, Irina Steinbrecher, Dmitry N Ostrovsky, Reiner Hedderich, Ewald Beck, Hassan Jomaa, Jochen Wiesner.
Abstract
The gcpE gene product controls one of the terminal steps of isoprenoid biosynthesis via the mevalonate independent 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway. This pathway is utilized by a variety of eubacteria, the plastids of algae and higher plants, and the plastid-like organelle of malaria parasites. Recombinant GcpE protein from the hyperthermophilic bacterium Thermus thermophilus was produced in Escherichia coli and purified under dioxygen-free conditions. The protein was enzymatically active in converting 2-C-methyl-D-erythritol-2,4-cyclodiphosphate (MEcPP) into (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate (HMBPP) in the presence of dithionite as reductant. The maximal specific activity was 0.6 micromol x min(-1) x mg(-1) at pH 7.5 and 55 degrees C. The kcat value was 0.4 s(-1) and the K(m) value for HMBPP 0.42 mM.Entities:
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Year: 2002 PMID： 12482607 DOI： 10.1016/s0014-5793(02)03725-0
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124