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Michel Rohmer - One of the best experts on this subject based on the ideXlab platform.
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on the absence of the Glyceraldehyde 3 Phosphate pyruvate pathway for isoprenoid biosynthesis in fungi and yeasts
Fems Microbiology Letters, 1998Co-Authors: Andrea Disch, Michel RohmerAbstract:The biosynthesis of isopentenyl diPhosphate, the central intermediate of isoprenoid formation, was investigated in the fungus Aschersonia aleyrodis and the yeast Rhodotorula glutinis. The incorporation of 13C-labeled glucose or acetate into their isoprenoids showed that ergosterol in both micro-organisms, ubiquinone in R. glutinis and dihydro-ubiquinone, β-carotene and triterpenes of the hopane series in A. aleyrodis were synthesized via the mevalonate pathway. No evidence for the presence of the alternative mevalonate-independent Glyceraldehyde 3-Phosphate/pyruvate pathway was found.
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distribution of mevalonate and Glyceraldehyde 3 Phosphate pyruvate routes for isoprenoid biosynthesis in some gram negative bacteria and mycobacteria
Fems Microbiology Letters, 1998Co-Authors: Surya Rosa Putra, Andrea Disch, Jean Michel Bravo, Michel RohmerAbstract:Labeling experiments using [1-13C]acetate or [1-13C]glucose were performed with opportunistic pathogenic bacteria, with innocuous bacteria related to pathogenic species or with phytopathogenic species. The labeling pattern was determined in the isoprenic moiety of ubiquinone or menaquinone derivatives. These experiments showed that Acinetobacter, Citrobacter, Erwinia, Pseudomonas, Burkholderia, Ralstonia and Mycobacterium synthesize their isoprenoids via the mevalonate-independent Glyceraldehyde 3-Phosphate/pyruvate route. Enzymes of this novel bacterial metabolic route, which is apparently absent in vertebrates and man, therefore represent potential targets for a novel type of antibacterial drugs.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Myriam Seemann, Hartmut K Lichtenthaler, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids beta-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Hartmut K Lichtenthaler, M Seemann, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13 C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13 C-NMR spectroscopy. According to the 13 C-labelling pattern indicated by the 13 C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids β-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C 2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C 5 skeleton of isoprenic units.
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Glyceraldehyde 3 Phosphate and pyruvate as precursors of isoprenic units in an alternative non mevalonate pathway for terpenoid biosynthesis
Journal of the American Chemical Society, 1996Co-Authors: Michel Rohmer, Myriam Seemann, Silke Horbach, Stephanie Bringermeyer, Hermann SahmAbstract: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 triterpenoids of the hopane series of Zymomonas mobilis showed that Glyceraldehyde 3-Phosphate (or eventually Glyceraldehyde) and a C2 unit derived from pyruvate decarboxylation were the only precursors of the C5 skeleton of isoprenic units in a novel non-mevalonate pathway for isoprenoid biosynthesis in these bacteria.
Jorg Schwender - One of the best experts on this subject based on the ideXlab platform.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Myriam Seemann, Hartmut K Lichtenthaler, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids beta-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Hartmut K Lichtenthaler, M Seemann, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13 C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13 C-NMR spectroscopy. According to the 13 C-labelling pattern indicated by the 13 C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids β-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C 2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C 5 skeleton of isoprenic units.
Michael A Sirover - One of the best experts on this subject based on the ideXlab platform.
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moonlighting Glyceraldehyde 3 Phosphate dehydrogenase posttranslational modification protein and nucleic acid interactions in normal cells and in human pathology
Critical Reviews in Biochemistry and Molecular Biology, 2020Co-Authors: Michael A SiroverAbstract:Moonlighting Glyceraldehyde-3-Phosphate dehydrogenase (GAPDH) exhibits multiple functions separate and distinct from its historic role in energy production. Further, it exhibits dynamic changes in its subcellular localization which is an a priori requirement for its multiple activities. Separately, moonlighting GAPDH may function in the pathology of human disease, involved in tumorigenesis, diabetes, and age-related neurodegenerative disorders. It is suggested that moonlighting GAPDH function may be related to specific modifications of its protein structure as well as the formation of GAPDH protein: protein or GAPDH protein: nucleic acid complexes.
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moonlighting Glyceraldehyde 3 Phosphate dehydrogenase posttranslational modification protein and nucleic acid interactions in normal cells and in human pathology
Critical Reviews in Biochemistry and Molecular Biology, 2020Co-Authors: Michael A SiroverAbstract:Moonlighting Glyceraldehyde-3-Phosphate dehydrogenase (GAPDH) exhibits multiple functions separate and distinct from its historic role in energy production. Further, it exhibits dynamic changes in ...
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structural analysis of Glyceraldehyde 3 Phosphate dehydrogenase functional diversity
The International Journal of Biochemistry & Cell Biology, 2014Co-Authors: Michael A SiroverAbstract:Multifunctional proteins provide a new mechanism to expand exponentially cell information and capability beyond that indicated by conventional gene analyses. As such, examination of their structure-function relationships provides a means to define the mechanisms through which cells accomplish critical yet disparate activities required for cell viability and survival. Glyceraldehyde-3-Phosphate dehydrogenase (GAPDH) may be considered the quintessential multidimensional protein which exhibits a variety of functions unrelated to its classical role in energy production. This review discusses new insights into the structure-function mechanisms through which defined GAPDH amino acid domains are utilized for its diverse activities, the importance of its post-translational modification, and, intriguingly, the logic inherent in the presence or the absence of specific signaling domains.
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a human nuclear uracil dna glycosylase is the 37 kda subunit of Glyceraldehyde 3 Phosphate dehydrogenase
Proceedings of the National Academy of Sciences of the United States of America, 1991Co-Authors: Katherine Meyersiegler, David J Mauro, Gita Seal, James C Wurzer, Jon K Deriel, Michael A SiroverAbstract:We have isolated and characterized a plasmid (pChug 20.1) that contains the cDNA of a nuclear uracil DNA glycosylase (UDG) gene isolated from normal human placenta. This cDNA directed the synthesis of a fusion protein (Mr 66,000) that exhibited UDG activity. The enzymatic activity was specific for a uracil-containing polynucleotide substrate and was inhibited by a glycosylase antibody or a beta-galactosidase antibody. Sequence analysis demonstrated an open reading frame that encoded a protein of 335 amino acids of calculated Mr 36,050 and pI 8.7, corresponding to the Mr 37,000 and pI 8.1 of purified human placental UDG. No homology was seen between this cDNA and the UDG of herpes simplex virus, Escherichia coli, and yeast; nor was there homology with the putative human mitochondrial UDG cDNA or with a second human nuclear UDG cDNA. Surprisingly, a search of the GenBank data base revealed that the cDNA of UDG was completely homologous with the 37-kDa subunit of human Glyceraldehyde-3-Phosphate dehydrogenase. Human erythrocyte Glyceraldehyde-3-Phosphate dehydrogenase was obtained commercially in its tetrameric form. A 37-kDa subunit was isolated from it and shown to possess UDG activity equivalent to that seen for the purified human placental UDG. The multiple functions of this 37-kDa protein as here and previously reported indicate that it possesses a series of activities, depending on its oligomeric state. Accordingly, mutation(s) in the gene of this multifunctional protein may conceivably result in the diverse cellular phenotypes of Bloom syndrome.
Hartmut K Lichtenthaler - One of the best experts on this subject based on the ideXlab platform.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Myriam Seemann, Hartmut K Lichtenthaler, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids beta-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Hartmut K Lichtenthaler, M Seemann, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13 C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13 C-NMR spectroscopy. According to the 13 C-labelling pattern indicated by the 13 C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids β-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C 2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C 5 skeleton of isoprenic units.
Myriam Seemann - One of the best experts on this subject based on the ideXlab platform.
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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 scenedesmus obliquus
Biochemical Journal, 1996Co-Authors: Jorg Schwender, Myriam Seemann, Hartmut K Lichtenthaler, Michel RohmerAbstract:Isoprenoid biosynthesis was investigated in the green alga Scenedesmus obliquus grown heterotrophically on 13C-labelled glucose and acetate. Several isoprenoid compounds were isolated and investigated by 13C-NMR spectroscopy. According to the 13C-labelling pattern indicated by the 13C-NMR spectra, the biosynthesis of all plastidic isoprenoids investigated (prenyl side-chains of chlorophylls and plastoquinone-9, and the carotenoids beta-carotene and lutein), as well as of the non-plastidic cytoplasmic sterols, does not proceed via the classical acetate/mevalonate pathway (which leads from acetyl-CoA via mevalonate to isopentenyl diPhosphate), but via the novel Glyceraldehyde 3-Phosphate/pyruvate route recently detected in eubacteria. Formation of isopentenyl diPhosphate involves the condensation of a C2 unit derived from pyruvate decarboxylation with Glyceraldehyde 3-Phosphate and a transposition yielding the branched C5 skeleton of isoprenic units.
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Glyceraldehyde 3 Phosphate and pyruvate as precursors of isoprenic units in an alternative non mevalonate pathway for terpenoid biosynthesis
Journal of the American Chemical Society, 1996Co-Authors: Michel Rohmer, Myriam Seemann, Silke Horbach, Stephanie Bringermeyer, Hermann SahmAbstract: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 triterpenoids of the hopane series of Zymomonas mobilis showed that Glyceraldehyde 3-Phosphate (or eventually Glyceraldehyde) and a C2 unit derived from pyruvate decarboxylation were the only precursors of the C5 skeleton of isoprenic units in a novel non-mevalonate pathway for isoprenoid biosynthesis in these bacteria.