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Plants Possess a Cyclic Mitochondrial Metabolic Pathway similar to the Mammalian Metabolic Repair Mechanism Involving Malate Dehydrogenase and l-2-Hydroxyglutarate Dehydrogenase.

Plant Cell Physiol.2015 Sep;56(9):1820-30. Epub 2015 Jul 21
Meike Hüdig 1 , Alexander Maier 1 , Isabell Scherrers 1 , Laura Seidel 1 , Erwin E W Jansen 2 , Tabea Mettler-Altmann 3 , Martin K M Engqvist 4 , Veronica G Maurino 5
Meike Hüdig 1 , Alexander Maier 1 , Isabell Scherrers 1 , Laura Seidel 1 , Erwin E W Jansen 2 , Tabea Mettler-Altmann 3 , Martin K M Engqvist 4 , Veronica G Maurino 5
+ et al

[No authors listed]

Author information
  • 1 Institute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences (CEPLAS), Universitätsstraße 1, D-40225 Düsseldorf, Germany.
  • 2 Metabolic Unit, Clinical Chemistry, VU University Medical Centre, De Boelelaan 1117, 1081 HV Amsterdam, The Netherlands.
  • 3 Institute of Plant Biochemistry, Heinrich-Heine-Universität, Universitätsstraße 1, and Cluster of Excellence on Plant Sciences (CEPLAS), D-40225 Düsseldorf, Germany.
  • 4 Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden.
  • 5 Institute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich-Heine-Universität, and Cluster of Excellence on Plant Sciences (CEPLAS), Universitätsstraße 1, D-40225 Düsseldorf, Germany veronica.maurino@uni-duesseldorf.de.

摘要


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.

KEYWORDS: Arabidopsis, Malate dehydrogenase, Metabolite repair, l-2-Hydroxyglutarate, l-2-Hydroxyglutarate dehydrogenase