ArticleThe Journal of biological chemistry2016
Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of β-Aryl Ether Bonds in Lignin.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- Lignin-Degrading Enzymes and the Potential ofMicroorganisms · 2025Review
- The chemical logic of enzymatic lignin degradation.Chemical communications (Cambridge, England) · 2024Review
- Article
- Article
- Roles of two glutathione S-transferases in the final step of the β-aryl ether cleavage pathway in Sphingobium sp. strain SYK-6.Scientific reports · 2020Article
- Lignin Degradation and Its Use in Signaling Development by the Coprophilous AscomyceteJournal of fungi (Basel, Switzerland) · 2020Article
- Nucleophilic Thiols Reductively Cleave Ether Linkages in Lignin Model Polymers and Lignin.ChemSusChem · 2020Article
- Structural and functional divergence of GDAP1 from the glutathione S-transferase superfamily.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Database Mining for Novel Bacterial β-Etherases, Glutathione-Dependent Lignin-Degrading Enzymes.Applied and environmental microbiology · 2020Article
- AcidicFrontiers in bioengineering and biotechnology · 2020Article
- A heterodimeric glutathioneThe Journal of biological chemistry · 2019Article
- Bacterial Catabolism of β-Hydroxypropiovanillone and β-Hydroxypropiosyringone Produced in the Reductive Cleavage of Arylglycerol-β-Aryl Ether in Lignin.Applied and environmental microbiology · 2018Article
- Article
- Rapid characterization of the activities of lignin-modifying enzymes based on nanostructure-initiator mass spectrometry (NIMS).Biotechnology for biofuels · 2018Article
- Berkeley Screen: a set of 96 solutions for general macromolecular crystallization.Journal of applied crystallography · 2017Article
- Efficient, environmentally-friendly and specific valorization of lignin: promising role of non-radical lignolytic enzymes.World journal of microbiology & biotechnology · 2017Review
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 1 country.
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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.
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