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A bacterial enzyme degrading the model lignin compound β‐etherase is a member of the glutathione‐ S ‐transferase superfamily
Author(s) -
Masai Eiji,
Katayama Yoshihiro,
Kubota Sachiko,
Kawai Shinya,
Yamasaki Makari,
Morohoshi Noriyuki
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81465-c
Subject(s) - glutathione , biochemistry , escherichia coli , chemistry , glutathione s transferase , transferase , lignin , enzyme , open reading frame , gene , beta (programming language) , mutant , ether , peptide sequence , organic chemistry , computer science , programming language
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.