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Glyceraldehyde 3-Phosphate and Pyruvate as Precursors of Isoprenic Units in an Alternative Non-mevalonate Pathway for Terpenoid Biosynthesis
Incorporation of 13C-labeled glycerol or pyruvate into the ubiquinone Q8 of Escherichia coli mutants lacking enzymes of the triose phosphate metabolism and of (U-13C6)glucose into the triterpenoidsExpand
Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)‐4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe–4S] protein
The last enzyme (LytB) of the methylerythritol phosphate pathway for isoprenoid biosynthesis catalyzes the reduction of (E)‐4‐hydroxy‐3‐methylbut‐2‐enyl diphosphate into isopentenyl diphosphate andExpand
Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga
The biosynthesis of all plastidic isoprenoids investigated, including the carotenoids beta-carotene and lutein, does not proceed via the classical acetate/mevalonate pathway, but via the novel glyceraldehyde 3-phosphate/pyruvate route recently detected in eubacteria. Expand
Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: Direct thylakoid/ferredoxin‐dependent photoreduction of GcpE/IspG
A thylakoid preparation from spinach chloroplasts was capable in the presence of light to act as sole electron donor for the plant GcpE Arabidopsis thaliana in the absence of any pyridine nucleotide and represents the first proof that the electron flow from photosynthesis can directly act in phototrophic organisms as reducer. Expand
Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein.
The enzyme was found to be 95% pure by SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electro-phoresis) and presented an apparent molecular mass of 43kDa, and the purified protein was inactive, even in the presence ofhereducingsystems. Expand
Accumulation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate in illuminated plant leaves at supraoptimal temperatures reveals a bottleneck of the prokaryotic methylerythritol 4-phosphate pathway of
A model wherein GcpE turnover represents a bottleneck of the MEP pathway in plant leaves simultaneously exposed to high irradiance and hot temperature is proposed, which suggests that MEcDP accumulation in leaves may originate from both GCPE sensitivity to oxidative environment and limitations of its repair. Expand
Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis.
Formation of (+)-germacrene A by the various pentalenene synthase mutants is the result of a derailment of the natural anti-Markovnikov cyclization reaction, and not simply the consequence of trapping of a normally cryptic, carbocationic intermediate. Expand
Identification of gcpE as a novel gene of the 2‐C‐methyl‐D‐erythritol 4‐phosphate pathway for isoprenoid biosynthesis in Escherichia coli
The data demonstrate that the gcpE gene is essential for the MEP pathway in Escherichia coli and indicate that this gene is required for the trunk line of the isoprenoid biosynthetic route. Expand
Isoprenoid biosynthesis as a novel target for antibacterial and antiparasitic drugs.
The mevalonate-independent methylerythritol phosphate pathway is a long overlooked metabolic pathway for isoprenoid biosynthesis that is present in most bacteria, including pathogens and opportunistic pathogens, in some unicellular eukaryotes, and in the chloroplasts of all phototrophic organisms. Expand
Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) from Arabidopsis thaliana is a [4Fe–4S] protein
The prosthetic group of GcpE from the plant Arabidopsis thaliana and the bacterium Escherichia coli has been fully characterized by Mössbauer spectroscopy after reconstitution with 57FeCl3, Na2S and dithiothreitol, suggesting that both plant and bacterial enzymes catalyze the reduction of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate. Expand