Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin

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dc.citation.firstpage5234en_US
dc.citation.journalTitleThe Journal of Biological Chemistryen_US
dc.citation.lastpage5246en_US
dc.citation.volumeNumber291en_US
dc.contributor.authorHelmich, Kate E.en_US
dc.contributor.authorPereira, Jose Henriqueen_US
dc.contributor.authorGall, Daniel L.en_US
dc.contributor.authorHeins, Richard A.en_US
dc.contributor.authorMcAndrew, Ryan P.en_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorDeng, Kaien_US
dc.contributor.authorHolland, Keefe C.en_US
dc.contributor.authorNoguera, Daniel R.en_US
dc.contributor.authorSimmons, Blake A.en_US
dc.contributor.authorSale, Kenneth L.en_US
dc.contributor.authorRalph, Johnen_US
dc.contributor.authorDonohue, Timothy J.en_US
dc.contributor.authorAdams, Paul D.en_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.date.accessioned2017-01-27T22:23:42Zen_US
dc.date.available2017-01-27T22:23:42Zen_US
dc.date.issued2016en_US
dc.description.abstractLignin is a combinatorial polymer comprising monoaromatic units that are linked via covalent bonds. Although lignin is a potential source of valuable aromatic chemicals, its recalcitrance to chemical or biological digestion presents major obstacles to both the production of second-generation biofuels and the generation of valuable coproducts from lignin's monoaromatic units. Degradation of lignin has been relatively well characterized in fungi, but it is less well understood in bacteria. A catabolic pathway for the enzymatic breakdown of aromatic oligomers linked via β-aryl ether bonds typically found in lignin has been reported in the bacterium Sphingobium sp. SYK-6. Here, we present x-ray crystal structures and biochemical characterization of the glutathione-dependent β-etherases, LigE and LigF, from this pathway. The crystal structures show that both enzymes belong to the canonical two-domain fold and glutathione binding site architecture of the glutathione S-transferase family. Mutagenesis of the conserved active site serine in both LigE and LigF shows that, whereas the enzymatic activity is reduced, this amino acid side chain is not absolutely essential for catalysis. The results include descriptions of cofactor binding sites, substrate binding sites, and catalytic mechanisms. Because β-aryl ether bonds account for 50–70% of all interunit linkages in lignin, understanding the mechanism of enzymatic β-aryl ether cleavage has significant potential for informing ongoing studies on the valorization of lignin.en_US
dc.identifier.citationHelmich, Kate E., Pereira, Jose Henrique, Gall, Daniel L., et al.. "Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin." <i>The Journal of Biological Chemistry,</i> 291, (2016) American Society for Biochemistry and Molecular Biology: 5234-5246. http://dx.doi.org/10.1074/jbc.M115.694307.en_US
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M115.694307en_US
dc.identifier.urihttps://hdl.handle.net/1911/93801en_US
dc.language.isoengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) license.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/us/en_US
dc.titleStructural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Ligninen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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