| Literature DB >> 8495726 |
E Masai1, Y Katayama, S Kubota, S Kawai, M Yamasaki, N Morohoshi.
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.Entities:
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Year: 1993 PMID: 8495726 DOI: 10.1016/0014-5793(93)81465-c
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124