AI Article Synopsis
- A group of plant proteins known as beta-hydroxyacid dehydrogenases includes enzymes that convert succinic semialdehyde to gamma-hydroxybutyrate and glyoxylate to glycolate.
- Recent studies identify two isoforms of these enzymes (GLYR1 and GLYR2) in Arabidopsis that rely on NADPH for their functions.
- The review suggests that these enzymes help detoxify aldehydes during stress and maintain redox balance, while also addressing outstanding questions about how this detoxification mechanism is organized within plant cells.
Article Abstract
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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762691 | PMC |
| http://dx.doi.org/10.1042/BJ20090826 | DOI Listing |
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