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FEBS Lett. 1993 May 24;323(1-2):135-40.

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

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Laboratory of Wood Chemistry, Faculty of Agriculture, Tokyo Noko University, Japan.


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.

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