Journal
FEBS LETTERS
Volume 586, Issue 22, Pages 3944-3950Publisher
WILEY
DOI: 10.1016/j.febslet.2012.09.036
Keywords
Glutathione transferase; LigG; Lignin; X-ray structure; Omega class; Thiol transferase
Funding
- Agence Nationale pour la Recherche [ANR-09-BLAN-0012]
- Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0012] Funding Source: Agence Nationale de la Recherche (ANR)
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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 alpha-glutathionyl-beta-hydroxypropiovanillone, argues for broadening the definition of the omega class. Structured summary of protein interactions: SpLigG and SpLigG bind by X-ray crystallography (View interaction). (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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