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dc.contributor.authorHelmich, Kate E.
Pereira, Jose Henrique
Gall, Daniel L.
Heins, Richard A.
McAndrew, Ryan P.
Bingman, Craig
Deng, Kai
Holland, Keefe C.
Noguera, Daniel R.
Simmons, Blake A.
Sale, Kenneth L.
Ralph, John
Donohue, Timothy J.
Adams, Paul D.
Phillips, George N. Jr.
dc.date.accessioned 2017-01-27T22:23:42Z
dc.date.available 2017-01-27T22:23:42Z
dc.date.issued 2016
dc.identifier.citation Helmich, 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." The Journal of Biological Chemistry, 291, (2016) American Society for Biochemistry and Molecular Biology: 5234-5246. http://dx.doi.org/10.1074/jbc.M115.694307.
dc.identifier.urihttps://hdl.handle.net/1911/93801
dc.description.abstract Lignin 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.
dc.language.iso eng
dc.publisher American Society for Biochemistry and Molecular Biology
dc.rights This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) license.
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/us/
dc.title Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin
dc.type Journal article
dc.citation.journalTitle The Journal of Biological Chemistry
dc.citation.volumeNumber 291
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M115.694307
dc.identifier.pmcid PMC4777856
dc.identifier.pmid 26637355
dc.type.publication publisher version
dc.citation.firstpage 5234
dc.citation.lastpage 5246


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