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Role of plant glyoxylate reductases during stress: a hypothesis.

Wendy L WL Allan, Shawn M SM Clark, Gordon J GJ Hoover, and Barry J BJ Shelp

Biochem J 423(1):15-22 (2009) PMID 19740079

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.

DOI: 10.1042/BJ20090826
Version: za2963e q8za7 q8zb6 q8zce q8zd5 q8zef q8zff q8zga

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