Work

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

Year: 1993

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(93)81465-c

Authors: Eiji Masai, Yoshihiro Katayama, Sachiko Kubota, Shinya Kawai, Makari Yamasaki, Noriyuki Morohoshi

Institution: The University of Tokyo

Language: English

Topic: Lignin and Wood Chemistry

Subfield: Process Chemistry and Technology

Field: Chemical Engineering

Domain: Physical Sciences

Open Access status: bronze

Funder: Japan Society for the Promotion of Science

Award: The development of a new method for specific cleavage of lignin beta-ether linkage by genetic engineering.