ArticleThe Journal of biological chemistry
Structural and functional analysis of lignostilbene dioxygenases from Sphingobium sp. SYK-6.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Biochemical parallels between catabolic pathways for lignin-associated aromatic dimers.Applied and environmental microbiology · 2026Review
- Elucidation of a bacterial pathway for catabolism of the β-β-linked dilignol pinoresinol.mBio · 2025Article
- Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme FeThe Journal of biological chemistry · 2025Article
- Article
- Engineering a coenzyme-independent dioxygenase for one-step production of vanillin from ferulic acid.Applied and environmental microbiology · 2024Article
- Biochemical and structural characterization of a sphingomonad diarylpropane lyase for cofactorless deformylation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Understanding of bacterial lignin extracellular degradation mechanisms by Pseudomonas putida KT2440 via secretomic analysis.Biotechnology for biofuels and bioproducts · 2022Article
- Preparation of carotenoid cleavage dioxygenases for X-ray crystallography.Methods in enzymology · 2022Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignostilbene-α,β-dioxygenases (LSDs) are iron-dependent oxygenases involved in the catabolism of lignin-derived stilbenes. Sphingobium sp. SYK-6 contains eight LSD homologs with undetermined physiological roles. To investigate which homologs are involved in the catabolism of dehydrodiconiferyl alcohol (DCA), derived from β-5 linked lignin subunits, we heterologously produced the enzymes and screened their activities in lysates. The seven soluble enzymes all cleaved lignostilbene, but only LSD2, LSD3, and LSD4 exhibited high specific activity for 3-(4-hydroxy-3-(4-hydroxy-3-methoxystyryl)-5-methoxyphenyl) acrylate (DCA-S) relative to lignostilbene. LSD4 catalyzed the cleavage of DCA-S to 5-formylferulate and vanillin and cleaved lignostilbene and DCA-S (∼10
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