A bacterial enzyme degrading the model lignin compound β‐etherase is a member of the glutathione‐S‐transferase superfamily
Open Access
- 24 May 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 323 (1-2), 135-140
- https://doi.org/10.1016/0014-5793(93)81465-c
Abstract
Cleavage of β‐aryl ether linkages is essential in lignin degradation. We identified another β‐etherase gene (ligF), which contains an open reading frame of 771 bp and lies between genes coding Cα‐dehydrogenase (ligD) and β‐etherase (ligE). The β‐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 β‐etherase activity was found in E. coli carrying ligF. It is concluded that LigF plays a central role in β‐aryl ether cleavage and that glutathione is the hydrogen donor in this reaction.Keywords
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