Sphingobium sp. SYK-6 LigG involved in lignin degradation is structurally and biochemically related to the glutathione transferase ω class

FEBS Lett. 2012 Nov 16;586(22):3944-50. doi: 10.1016/j.febslet.2012.09.036. Epub 2012 Oct 8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Binding Sites / genetics
  • Biocatalysis
  • Crystallography, X-Ray
  • Cysteine / chemistry
  • Cysteine / genetics
  • Cysteine / metabolism
  • Glutathione / chemistry
  • Glutathione / metabolism
  • Glutathione Transferase / classification
  • Glutathione Transferase / genetics
  • Glutathione Transferase / metabolism*
  • Isoenzymes / classification
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Lignin / chemistry
  • Lignin / metabolism*
  • Models, Molecular
  • Molecular Structure
  • Mutagenesis, Site-Directed
  • Phylogeny
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sphingomonadaceae / enzymology*
  • Sphingomonadaceae / genetics
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Isoenzymes
  • Lignin
  • Glutathione Transferase
  • Glutathione
  • Cysteine