Journal
BIOCHEMICAL JOURNAL
Volume 423, Issue -, Pages 15-22Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20090826
Keywords
aldehyde detoxification; glyoxylate reductase; beta-hydroxyacid dehydrogenase; redox balance; succinic semialdehyde reductase
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Funding
- Natural Sciences and Engineering Research Council of Canada
- Ontario Ministry of Agriculture Food and Rural Affairs
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Molecular modelling suggests that a group of proteins in plants known as the beta-hydroxyacid dehydrogenases, or the hydroxyisobutyrate dehydrogenase superfamily, includes enzymes that reduce succinic semialdehyde and glyoxylate to gamma-hydroxybutyrate and glycolate respectively. Recent biochemical and expression studies reveal that NADPH-dependent cytosolic (termed GLYR1) and plastidial (termed GLYR2) isoforms of succinic semialdehyde/glyoxylate reductase exist in Arabidopsis. Succinic semialdehyde and glyoxylate are typically generated in leaves via two distinct metabolic pathways, gamma-aminobutyrate and glycolate respectively. In the present review, it is proposed that the GLYRs function in the detoxification of both aldehydes during stress and contribute to redox balance. Outstanding questions are highlighted in a scheme for the subcellular organization of the detoxification mechanism in Arabidopsis.
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