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Plants Possess a Cy...
Plants Possess a Cyclic Mitochondrial Metabolic Pathway similar to the Mammalian Metabolic Repair Mechanism Involving Malate Dehydrogenase and l-2-Hydroxyglutarate Dehydrogenase
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- Hüdig, M. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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- Maier, A. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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- Scherrers, I. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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- Seidel, L. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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Jansen, E. E. W. (author)
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- Mettler-Altmann, T. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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- Engqvist, Martin, 1983 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Maurino, V. G. (author)
- Heinrich Heine Universität Düsseldorf,Heinrich Heine University Düsseldorf
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(creator_code:org_t)
- 2015-07-21
- 2014
- English.
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In: Plant and Cell Physiology. - : Oxford University Press (OUP). - 1471-9053 .- 0032-0781. ; 56:9, s. 1820-1830
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Abstract
Subject headings
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- Enzymatic side reactions can give rise to the formation of wasteful and toxic products that are removed by metabolite repair pathways. In this work, we identify and characterize a mitochondrial metabolic repair mechanism in Arabidopsis thaliana involving malate dehydrogenase (mMDH) and l-2-hydroxyglutarate dehydrogenase (l-2HGDH). We analyze the kinetic properties of both A. thaliana mMDH isoforms, and show that they produce l-2-hydroxyglutarate (l-2HG) from 2-ketoglutarate (2-KG) at low rates in side reactions. We identify A. thaliana l-2HGDH as a mitochondrial FAD-containing oxidase that converts l-2HG back to 2-KG. Using loss-of-function mutants, we show that the electrons produced in the l-2HGDH reaction are transferred to the mitochondrial electron transport chain through the electron transfer protein (ETF). Thus, plants possess the biochemical components of an l-2HG metabolic repair system identical to that found in mammals. While deficiencies in the metabolism of l-2HG result in fatal disorders in mammals, accumulation of l-2HG in plants does not adversely affect their development under a range of tested conditions. However, orthologs of l-2HGDH are found in all examined genomes of viridiplantae, indicating that the repair reaction we identified makes an essential contribution to plant fitness in as yet unidentified conditions in the wild. © 2015 The Author 2015.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
Keyword
- l-2-Hydroxyglutarate
- Arabidopsis
- l-2-Hydroxyglutarate dehydrogenase
- Malate dehydrogenase
- Metabolite repair
Publication and Content Type
- art (subject category)
- ref (subject category)
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