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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Binding Sites / genetics
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Biocatalysis
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Crystallography, X-Ray
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Cysteine / chemistry
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Cysteine / genetics
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Cysteine / metabolism
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Glutathione / chemistry
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Glutathione / metabolism
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Glutathione Transferase / classification
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism*
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Isoenzymes / classification
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Isoenzymes / genetics
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Isoenzymes / metabolism
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Lignin / chemistry
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Lignin / metabolism*
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Models, Molecular
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Molecular Structure
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Mutagenesis, Site-Directed
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Phylogeny
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Sphingomonadaceae / enzymology*
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Sphingomonadaceae / genetics
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Substrate Specificity
Substances
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Bacterial Proteins
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Isoenzymes
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Lignin
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Glutathione Transferase
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Glutathione
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Cysteine