A bacterial enzyme degrading the model lignin compound beta-etherase is a member of the glutathione-S-transferase superfamily

FEBS Lett. 1993 May 24;323(1-2):135-40. doi: 10.1016/0014-5793(93)81465-c.

Abstract

Cleavage of beta-aryl ether linkages is essential in lignin degradation. We identified another beta-etherase gene (ligF), which contains an open reading frame of 771 bp and lies between genes coding C alpha-dehydrogenase (ligD) and beta-etherase (ligE). The beta-etherase activity of LigF expressed in Escherichia coli was more than 80 times as high as that of LigE. ligF and ligE are homologous to glutathione-S-transferase, and upon addition of glutathione a remarkable acceleration of beta-etherase activity was found in E. coli carrying ligF. It is concluded that LigF plays a central role in beta-aryl ether cleavage and that glutathione is the hydrogen donor in this reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Base Sequence
  • Cloning, Molecular
  • DNA, Bacterial
  • Deoxyribonucleases, Type II Site-Specific / metabolism
  • Escherichia coli
  • Glutathione / metabolism
  • Glutathione Transferase / metabolism*
  • Lignin / metabolism*
  • Molecular Sequence Data
  • Oxidoreductases / genetics*
  • Oxidoreductases / metabolism
  • Pseudomonas / enzymology*
  • Restriction Mapping
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • Lignin
  • Oxidoreductases
  • aryl ether cleaving enzyme
  • Glutathione Transferase
  • Deoxyribonucleases, Type II Site-Specific
  • GTCGAC-specific type II deoxyribonucleases
  • Glutathione

Associated data

  • GENBANK/D11473