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

FEBS Letters

Kawai, Shinya¹  Yamasaki, Makari²  Kubota, Sachiko¹  Katayama, Yoshihiro³  Morohoshi, Noriyuki¹  Masai, Eiji¹ 

[1] Laboratory of Wood Chemistry, Faculty of Agriculture, Tokyo Noko University, Fuchu, Tokyo 183, Japan;The University of Tokyo, Bunkyo-ku, Tokyo 113,Japan;Cooperative Research Center, Tokyo Noko University, Koganei, Tokyo 184, Japan

关键词: Lignin degradation;    Arylglycerol-β-aryl ether linkage;    β-Etherase;    Glutathione-S-transferase;    Pseudomonas paucimobilis;    IPTG;    isopropyl-β-D-thiogalactopyranoside;    NADH;    reduced nicotinamide adenine dinucleotide;    NADPH;    reduced nicotinamide adenine dinucleotide phosphate;   

DOI  :  10.1016/0014-5793(93)81465-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown