期刊
PHYSIOLOGIA PLANTARUM
卷 119, 期 4, 页码 469-479出版社
WILEY
DOI: 10.1046/j.1399-3054.2003.00183.x
关键词
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Glutathione transferases (GSTs) are ubiquitous, multifunctional proteins encoded by large gene families. In different plant species this gene family is comprised of 25-60 members, that can be grouped into six classes on the basis of sequence identity, gene organization and active site residues in the protein. The Phi and Tau classes are the most represented and are plant specific, while Zeta and Theta GSTs are found also in animals. Despite pronounced sequence and functional diversification, GSTs have maintained a highly conserved three-dimensional structure through evolution. Most GSTs are cytosolic and active as dimers, performing diverse catalytic as well as non-catalytic roles in detoxification of xenobiotics, prevention of oxidative damage and endogenous metabolism. Among their catalytic activities are the conjugation of electrophilic substrates to glutathione, glutathione-dependent isomerizations and reductions of toxic organic hydroperoxides. Their main non-catalytic role is as hormone and flavonoid ligandins. GST genes are predominantly organized in clusters non-randomly distributed in the genome. Phylogenetic studies indicate that plant GSTs have mainly evolved after the divergence of plants, the two prevalent Phi and Tau classes being the result of recent, multiple duplication events.
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