Publications by authors named "Wendy L Allan"
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.
Enzymes that reduce the aldehyde chemical grouping (i.e. H-C=O) to its corresponding alcohol are probably crucial in maintaining plant health during stress.
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- Enzymes that convert aldehydes to alcohols play a key role in plant health, and a study identified two variants, AtGR1 and AtGR2, that effectively catalyze this process.
- Recombinant research demonstrated that AtGR2 preferentially converts glyoxylate to glycolate and succinic semialdehyde to gamma-hydroxybutyrate, with a much higher efficiency for glyoxylate.
- The localization of these enzymes differs, with AtGR1 found in the cytosol and AtGR2 in plastids, which may impact their roles in detoxifying aldehydes and the plant's response to stress.
In plants, gamma-aminobutyrate (GABA), a non-protein amino acid, accumulates rapidly in response to a variety of abiotic stresses such as oxygen deficiency. Under normoxia, GABA is catabolized to succinic semialdehyde and then to succinate with the latter reaction being catalyzed by succinic semialdehyde dehydrogenase (SSADH). Complementation of an SSADH-deficient yeast mutant with an Arabidopsis cDNA library enabled the identification of a novel cDNA (designated as AtGH-BDH for Arabidopsis thaliana gamma-hydroxybutyrate dehydrogenase), which encodes a 289-amino acid polypeptide containing an NADP-binding domain.
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