Journal
PLANT SIGNALING & BEHAVIOR
Volume 6, Issue 8, Pages 1223-1227Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/psb.6.8.16253
Keywords
glutathione-dependent reductase; flavonol; tocopherol; anthocyanidin; ascorbic acid; ligand fishing; global metabolite profiling; mass spectrometry
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Funding
- Biotechnology and Biological Sciences Research Council [BBG0017661]
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Uniquely among the plant glutathione transferases, two classes possess a catalytic cysteine capable of performing glutathione-dependent reductions. These are the dehydroascorbate reductases (DHARs) and the lambda-class glutathione transferases (GSTLs). Using immobilized GSTLs probed with crude plant extracts we have identified flavonols as high affinity ligands and subsequently demonstrated a novel glutathione-dependent role for these enzymes in recycling oxidized quercetin. By comparing the activities of DHARs and GSTLs we now propose a unified catalytic mechanism that suggests oxidized anthocyanidins and tocopherols may be alternative polyphenolic substrates of GSTLs.
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