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Testing against lignin dimer model compounds revealed that it does not catalyse the previously reported reaction of <jats:italic>Sphingobium<\/jats:italic> SYK\u20106 LigE, but instead shows activity for a \u03b2\u20105 phenylcoumaran lignin dimer. The reaction products did not contain glutathione, indicating a catalytic role for reduced glutathione in this enzyme. Three reaction products were identified: the major product was a <jats:italic>cis<\/jats:italic>\u2010stilbene arising from C\u2212C fragmentation involving loss of formaldehyde; two minor products were an alkene arising from elimination of glutathione, and an oxidised ketone, proposed to arise from reaction of an intermediate with molecular oxygen. Testing of the recombinant enzyme against a soda lignin revealed the formation of new signals by two\u2010dimensional NMR analysis, whose chemical shifts are consistent with the formation of a stilbene unit in polymeric lignin.<\/jats:p>","DOI":"10.1002\/cbic.202400132","type":"journal-article","created":{"date-parts":[[2024,2,28]],"date-time":"2024-02-28T11:49:20Z","timestamp":1709120960000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Ether Bond Cleavage of a Phenylcoumaran \u03b2\u20105 Lignin Model Compound and Polymeric Lignin Catalysed by a LigE\u2010type Etherase from <i>Agrobacterium<\/i> sp."],"prefix":"10.1002","volume":"25","author":[{"given":"Goran M. 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