Plant D-2-hydroxyglutarate dehydrogenase participates in the catabolism of lysine especially during senescence
Journal article, 2011

D-2-Hydroxyglutarate dehydrogenase (D-2HGDH) catalyzes the specific and efficient oxidation of D-2-hydroxyglutarate (D-2HG) to 2-oxoglutarate using FAD as a cofactor. In this work, we demonstrate that D-2HGDH localizes to plant mitochondria and that its expression increases gradually during developmental and dark-induced senescence in Arabidopsis thaliana, indicating an enhanced demand of respiration of alternative substrates through this enzymatic system under these conditions. Using loss-of-function mutants in D-2HGDH(d2hgdh1) and stable isotope dilution LC-MS/MS, we found that the D-isomer of 2HG accumulated in leaves of d2hgdh1 during both forms of carbon starvation. In addition to this, d2hgdh1 presented enhanced levels of most TCA cycle intermediates and free amino acids. In contrast to the deleterious effects caused by a deficiency in D-2HGDH in humans, d2hgdh1 and overexpressing lines of D-2HGDH showed normal developmental and senescence phenotypes, indicating a mild role of D-2HGDH in the tested conditions. Moreover, metabolic fingerprinting of leaves of plants grown in media supplemented with putative precursors indicated that D-2HG most probably originates during the catabolism of lysine. Finally, the L-isomer of 2HG was also detected in leaf extracts, indicating that both chiral forms of 2HG participate in plant metabolism.

Author

Martin Engqvist

Chalmers, Chemical and Biological Engineering, Life Sciences, System Biology

A. Kuhn

J. Wienstroer

K. Weber

E.E.W. Jansen

C. Jakobs

A.P.M. Weber

V.G. Maurino

Journal of Biological Chemistry

0021-9258 (ISSN) 1083-351X (eISSN)

Vol. 286 13 11382-11390

Subject Categories

Botany

Biochemistry and Molecular Biology

DOI

10.1074/jbc.M110.194175

More information

Created

10/7/2017