ArticleApplied and environmental microbiology2005
A second 5-carboxyvanillate decarboxylase gene, ligW2, is important for lignin-related biphenyl catabolism in Sphingomonas paucimobilis SYK-6.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 50 citations in OpenAlex.
- Fungal-bacterial interaction networks in lignocellulose degradation: an integrated ecological and mechanistic perspective.Biotechnology for biofuels and bioproducts · 2026Review
- Biochemical parallels between catabolic pathways for lignin-associated aromatic dimers.Applied and environmental microbiology · 2026Review
- Engineering a vanillate-producing strain of Pseudomonas sp. NGC7 corresponding to aromatic compounds derived from the continuous catalytic alkaline oxidation of sulfite lignin.Microbial cell factories · 2024Article
- Enzymatic Conversion of COChemical reviews · 2023Review
- Metal Ion Promiscuity and Structure of 2,3-Dihydroxybenzoic Acid Decarboxylase of Aspergillus oryzae.Chembiochem : a European journal of chemical biology · 2021Article
- Mechanisms of metal-dependent non-redox decarboxylases from quantum chemical calculations.Computational and structural biotechnology journal · 2021Review
- Isolation and characterization marine bacteria capable of degrading lignin-derived compounds.PloS one · 2020Article
- Bacterial Valorization of Lignin: Strains, Enzymes, Conversion Pathways, Biosensors, and Perspectives.Frontiers in bioengineering and biotechnology · 2019Review
- DdvK, a Novel Major Facilitator Superfamily Transporter Essential for 5,5'-Dehydrodivanillate Uptake by Sphingobium sp. Strain SYK-6.Applied and environmental microbiology · 2018Article
- 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
- Reaction Mechanism and Substrate Specificity ofFrontiers in chemistry · 2018Article
- Membrane-associated glucose-methanol-choline oxidoreductase family enzymes PhcC and PhcD are essential for enantioselective catabolism of dehydrodiconiferyl alcohol.Applied and environmental microbiology · 2015Article
- Three-Component O-Demethylase System Essential for Catabolism of a Lignin-Derived Biphenyl Compound in Sphingobium sp. Strain SYK-6.Applied and environmental microbiology · 2014Article
- Regulatory system of the protocatechuate 4,5-cleavage pathway genes essential for lignin downstream catabolism.Journal of bacteriology · 2010Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A lignin-related biphenyl compound, 5,5'-dehydrodivanillate (DDVA), is degraded to 5-carboxyvanillate (5CVA) by the enzyme reactions catalyzed by DDVA O-demethylase (LigX), meta-cleavage oxygenase (LigZ), and meta-cleavage compound hydrolase (LigY) in Sphingomonas paucimobilis SYK-6. 5CVA is then transformed to vanillate by a nonoxidative 5CVA decarboxylase and is further degraded through the protocatechuate 4,5-cleavage pathway. A 5CVA decarboxylase gene, ligW, was isolated from SYK-6 (X. Peng, E. Masai, H. Kitayama, K. Harada, Y, Katayama, and M. Fukuda, Appl. Environ. Microbiol. 68:4407-4415, 2002). However, disruption of ligW slightly affected the 5CVA decarboxylase activity and the growth rate on DDVA of the mutant, suggesting the presence of an alternative 5CVA decarboxylase gene. Here we isolated a second 5CVA decarboxylase gene, ligW2, which consists of a 1,050-bp open reading frame encoding a polypeptide with a molecular mass of 39,379 Da. The deduced amino acid sequence encoded by ligW2 exhibits 37% identity with the sequence encoded by ligW. Based on a gas chromatography-mass spectrometry analysis of the reaction product from 5CVA catalyzed by LigW2 in the presence of deuterium oxide, LigW2 was indicated to be a nonoxidative decarboxylase of 5CVA, like LigW. After disruption of ligW2, both the growth rate on DDVA and the 5CVA decarboxylase activity of the mutant were decreased to approximately 30% of the wild-type levels. The ligW ligW2 double mutant lost both the ability to grow on DDVA and the 5CVA decarboxylase activity. These results indicate that both ligW and ligW2 contribute to 5CVA degradation, although ligW2 plays the more important role in the growth of SYK-6 cells on DDVA.
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