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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
FEBS Lett.
|
| uniprot:author |
Katayama Y.,
Kawai S.,
Kubota S.,
Masai E.,
Morohoshi N.,
Yamasaki M.
|
| uniprot:date |
1993
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| uniprot:pages |
135-140
|
| uniprot:title |
A bacterial enzyme degrading the model lignin compound beta-etherase is a member of the glutathione-S-transferase superfamily.
|
| uniprot:volume |
323
|
| dc-term:identifier |
doi:10.1016/0014-5793(93)81465-C
|