| Literature DB >> 23058289 |
Edgar Meux1, Pascalita Prosper, Eiji Masai, Guillermo Mulliert, Stéphane Dumarçay, Mélanie Morel, Claude Didierjean, Eric Gelhaye, Frédérique Favier.
Abstract
SpLigG is one of the three glutathione transferases (GSTs) involved in the process of lignin breakdown in the soil bacterium Sphingobium sp. SYK-6. Sequence comparisons showed that SpLigG and several proteobacteria homologues form an independent cluster within cysteine-containing GSTs. The relationship between SpLigG and other GSTs was investigated. The X-ray structure and biochemical properties of SpLigG indicate that this enzyme belongs to the omega class of glutathione transferases. However, the hydrophilic substrate binding site of SpLigG, together with its known ability to stereoselectively deglutathionylate the physiological substrate α-glutathionyl-β-hydroxypropiovanillone, argues for broadening the definition of the omega class.Entities:
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Year: 2012 PMID: 23058289 DOI: 10.1016/j.febslet.2012.09.036
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124