| Literature DB >> 21778824 |
David P Dixon1, Patrick G Steel, Robert Edwards.
Abstract
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.Entities:
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Year: 2011 PMID: 21778824 PMCID: PMC3260729 DOI: 10.4161/psb.6.8.16253
Source DB: PubMed Journal: Plant Signal Behav ISSN: 1559-2316