A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism

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OriginalspracheEnglisch
Seiten (von - bis)168-176
Seitenumfang9
FachzeitschriftPHYTOCHEMISTRY
Jahrgang95
PublikationsstatusVeröffentlicht - 2 Aug. 2013

Abstract

Glyoxylate is a peroxisomal intermediate of photorespiration, the recycling pathway for 2-phosphoglycolate (2-PG) produced by the oxygenase activity of Rubisco. Under hot and dry growth conditions, photorespiratory intermediates can accumulate and must be detoxified by alternative pathways, including plastidal reactions. Moreover, there is evidence that chloroplasts are capable of actively producing glyoxylate from glycolate. Further metabolic steps are unknown, but probably include a CO2 release step. Here, we report that CO 2 production from glycolate and glyoxylate in isolated tobacco chloroplasts can be inhibited by pyruvate, but not related compounds. We isolated a protein fraction that was enriched for the chloroplast pyruvate dehydrogenase complex (PDC). The fraction contained a protein complex of several MDa in size that included all predicted subunits of the chloroplast PDC and a so far unidentified HSP93-V/ClpC1 heat shock protein. Glyoxylate competitively inhibited NADH formation from pyruvate in this fraction. The Km for pyruvate and the Ki for glyoxylate were 330 and 270 μM, respectively. Glyoxylate decarboxylation was also enriched in this fraction and could be in turn inhibited by pyruvate. Based on these data, we suggest that the chloroplast PDC might be part of a pathway for glycolate and/or glyoxylate oxidation in chloroplasts.

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A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism. / Blume, Christian; Behrens, Christof; Eubel, Holger et al.
in: PHYTOCHEMISTRY, Jahrgang 95, 02.08.2013, S. 168-176.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Blume C, Behrens C, Eubel H, Braun HP, Peterhänsel C. A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism. PHYTOCHEMISTRY. 2013 Aug 2;95:168-176. doi: 10.1016/j.phytochem.2013.07.009
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title = "A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism",
abstract = "Glyoxylate is a peroxisomal intermediate of photorespiration, the recycling pathway for 2-phosphoglycolate (2-PG) produced by the oxygenase activity of Rubisco. Under hot and dry growth conditions, photorespiratory intermediates can accumulate and must be detoxified by alternative pathways, including plastidal reactions. Moreover, there is evidence that chloroplasts are capable of actively producing glyoxylate from glycolate. Further metabolic steps are unknown, but probably include a CO2 release step. Here, we report that CO 2 production from glycolate and glyoxylate in isolated tobacco chloroplasts can be inhibited by pyruvate, but not related compounds. We isolated a protein fraction that was enriched for the chloroplast pyruvate dehydrogenase complex (PDC). The fraction contained a protein complex of several MDa in size that included all predicted subunits of the chloroplast PDC and a so far unidentified HSP93-V/ClpC1 heat shock protein. Glyoxylate competitively inhibited NADH formation from pyruvate in this fraction. The Km for pyruvate and the Ki for glyoxylate were 330 and 270 μM, respectively. Glyoxylate decarboxylation was also enriched in this fraction and could be in turn inhibited by pyruvate. Based on these data, we suggest that the chloroplast PDC might be part of a pathway for glycolate and/or glyoxylate oxidation in chloroplasts.",
keywords = "Heat shock protein Hsp93-V, Photorespiration, Two-dimensional BN/SDS-PAGE",
author = "Christian Blume and Christof Behrens and Holger Eubel and Braun, {Hans Peter} and Christoph Peterh{\"a}nsel",
note = "Funding information: This work was funded by the Deutsche Forschungsgemeinschaft as part of the research network PROMICS ( PE819/4-1 ). We thank Bernhard Huchzermeyer and Markus Niessen for helpful discussions.",
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T1 - A possible role for the chloroplast pyruvate dehydrogenase complex in plant glycolate and glyoxylate metabolism

AU - Blume, Christian

AU - Behrens, Christof

AU - Eubel, Holger

AU - Braun, Hans Peter

AU - Peterhänsel, Christoph

N1 - Funding information: This work was funded by the Deutsche Forschungsgemeinschaft as part of the research network PROMICS ( PE819/4-1 ). We thank Bernhard Huchzermeyer and Markus Niessen for helpful discussions.

PY - 2013/8/2

Y1 - 2013/8/2

N2 - Glyoxylate is a peroxisomal intermediate of photorespiration, the recycling pathway for 2-phosphoglycolate (2-PG) produced by the oxygenase activity of Rubisco. Under hot and dry growth conditions, photorespiratory intermediates can accumulate and must be detoxified by alternative pathways, including plastidal reactions. Moreover, there is evidence that chloroplasts are capable of actively producing glyoxylate from glycolate. Further metabolic steps are unknown, but probably include a CO2 release step. Here, we report that CO 2 production from glycolate and glyoxylate in isolated tobacco chloroplasts can be inhibited by pyruvate, but not related compounds. We isolated a protein fraction that was enriched for the chloroplast pyruvate dehydrogenase complex (PDC). The fraction contained a protein complex of several MDa in size that included all predicted subunits of the chloroplast PDC and a so far unidentified HSP93-V/ClpC1 heat shock protein. Glyoxylate competitively inhibited NADH formation from pyruvate in this fraction. The Km for pyruvate and the Ki for glyoxylate were 330 and 270 μM, respectively. Glyoxylate decarboxylation was also enriched in this fraction and could be in turn inhibited by pyruvate. Based on these data, we suggest that the chloroplast PDC might be part of a pathway for glycolate and/or glyoxylate oxidation in chloroplasts.

AB - Glyoxylate is a peroxisomal intermediate of photorespiration, the recycling pathway for 2-phosphoglycolate (2-PG) produced by the oxygenase activity of Rubisco. Under hot and dry growth conditions, photorespiratory intermediates can accumulate and must be detoxified by alternative pathways, including plastidal reactions. Moreover, there is evidence that chloroplasts are capable of actively producing glyoxylate from glycolate. Further metabolic steps are unknown, but probably include a CO2 release step. Here, we report that CO 2 production from glycolate and glyoxylate in isolated tobacco chloroplasts can be inhibited by pyruvate, but not related compounds. We isolated a protein fraction that was enriched for the chloroplast pyruvate dehydrogenase complex (PDC). The fraction contained a protein complex of several MDa in size that included all predicted subunits of the chloroplast PDC and a so far unidentified HSP93-V/ClpC1 heat shock protein. Glyoxylate competitively inhibited NADH formation from pyruvate in this fraction. The Km for pyruvate and the Ki for glyoxylate were 330 and 270 μM, respectively. Glyoxylate decarboxylation was also enriched in this fraction and could be in turn inhibited by pyruvate. Based on these data, we suggest that the chloroplast PDC might be part of a pathway for glycolate and/or glyoxylate oxidation in chloroplasts.

KW - Heat shock protein Hsp93-V

KW - Photorespiration

KW - Two-dimensional BN/SDS-PAGE

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DO - 10.1016/j.phytochem.2013.07.009

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VL - 95

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JO - PHYTOCHEMISTRY

JF - PHYTOCHEMISTRY

SN - 0031-9422

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