The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene symbol vanA is ambiguous across taxa, but for this request the target is unambiguous: UniProt Q88GI6 = Vanillate O-demethylase oxygenase subunit (VanA), EC 1.14.13.82, encoded by vanA / PP_3736 in Pseudomonas putida strain KT2440; its partner reductase is vanB / PP_3737 in the same pathway step (garciahidalgo2020vanillinproductionin pages 10-11, bleem2024evolutionandengineering pages 2-3). A pathway diagram explicitly places vanA/vanB at the vanillate (vanillic acid) → protocatechuate (protocatechuic acid) conversion in KT2440 aromatic metabolism (garciahidalgo2020vanillinproductionin media cf4cdebe).
VanAB is a bacterial aromatic O-demethylation system that converts the lignin-derived methoxylated aromatic acid vanillate into protocatechuate (PCA) while releasing formaldehyde as a one-carbon byproduct (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 1-2). This reaction is a key “funneling” step, transforming a substituted lignin monomer into a central intermediate that can be metabolized by core aromatic ring-cleavage pathways (garciahidalgo2020vanillinproductionin media cf4cdebe, bleem2024evolutionandengineering pages 2-3).
VanAB is a two-component enzyme system in which:
- VanA (Q88GI6; PP_3736) is the terminal oxygenase subunit responsible for substrate hydroxylation/oxidative demethylation chemistry (hibi2005functionalcouplingbetween pages 1-2, bleem2024evolutionandengineering pages 2-3).
- VanB (PP_3737) is the reductase component that supplies electrons from NAD(P)H to VanA (hibi2005functionalcouplingbetween pages 1-2, donoso2022identificationofa pages 1-2).
VanAB belongs to the Rieske non-heme iron monooxygenase (Rieske oxygenase) family (bleem2024evolutionandengineering pages 2-3, bleem2024evolutionandengineering pages 1-2). In this class, the oxygenase (VanA-family) contains a Rieske [2Fe–2S] cluster and a non-heme iron catalytic center; activity depends on electron transfer from the reductase and cellular reductants (tuomela2025conversionandupgrading pages 15-17, donoso2022identificationofa pages 1-2).
The consensus reaction supported by multiple sources is:
- Vanillate → protocatechuate + formaldehyde (oxygen- and reducing equivalent–dependent) (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 2-4, hibi2005functionalcouplingbetween pages 1-2).
This step is explicitly shown in a KT2440 pathway diagram and is assigned to vanA (PP_3736) / vanB (PP_3737) (garciahidalgo2020vanillinproductionin media cf4cdebe).
Functional assays of Pseudomonas VanAB expressed in E. coli showed that both NADH and NADPH can serve as electron donors in vitro for protocatechuate formation (hibi2005functionalcouplingbetween pages 2-4). In vivo experiments manipulating pentose phosphate pathway NADPH supply suggested NADPH may be preferred in vivo under the tested conditions (hibi2005functionalcouplingbetween pages 4-5). However, systems-level modeling of P. putida KT2440 lignin-carbon metabolism treated vanillate O-demethylation as using NADH based on a stated preference of VanB for NADH (zhou2025quantitativedecodingof pages 11-12). Taken together, available evidence indicates that cofactor usage can be context-dependent, and may vary with organism/assay format and redox state (hibi2005functionalcouplingbetween pages 2-4, hibi2005functionalcouplingbetween pages 4-5, zhou2025quantitativedecodingof pages 11-12).
VanAB systems are best supported as acting on meta-methoxylated aromatic acids with a carboxyl group, and substrate recognition rules inferred from comparative work emphasize these features (donoso2022identificationofa pages 1-2, donoso2022identificationofa pages 4-5). Although vanillate is the dominant physiological substrate in KT2440 (bleem2024evolutionandengineering pages 2-3, garciahidalgo2020vanillinproductionin media cf4cdebe), related literature notes broader activity of VanAB homologs on other methoxylated aromatics (e.g., veratrate, syringate, 3-O-methylgallate), with substrate preferences that can differ between organisms and between in vivo vs in vitro contexts (tuomela2025conversionandupgrading pages 15-17, wolf2024thecatabolismof pages 9-14).
In KT2440, VanA/VANAB converts vanillate to protocatechuate, a central intermediate that enters broader aromatic degradation routes (commonly the β-ketoadipate/protocatechuate branches) (garciahidalgo2020vanillinproductionin media cf4cdebe, bleem2024evolutionandengineering pages 2-3). This makes VanA a key node in microbial utilization of lignin-derived guaiacyl aromatics (bleem2024evolutionandengineering pages 2-3).
A central constraint of VanAB physiology is that O-demethylation generates formaldehyde, which is toxic and must be detoxified/assimilated (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 1-2). In E. coli expressing vanAB, formate accumulation began concomitantly with protocatechuate production, consistent with conversion of formaldehyde to formate via detoxification pathways (hibi2005functionalcouplingbetween pages 4-5). Disruption of frmA (formaldehyde dehydrogenase) markedly reduced formate accumulation and impaired growth and protocatechuate production, demonstrating functional coupling between VanAB activity and formaldehyde detoxification capacity (hibi2005functionalcouplingbetween pages 4-5).
In KT2440, vanA and vanB are organized as a vanAB operon, which has been deleted or reintroduced/overexpressed in multiple engineering studies (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 1-2).
Comparative evidence indicates vanAB expression can be controlled by a negative regulator termed VanR, with vanillate acting as an inducing/effector molecule that relieves repression (tuomela2025conversionandupgrading pages 15-17). In adaptive evolution experiments centered on vanillate utilization in KT2440, mutations in regulators and formaldehyde handling pathways were repeatedly selected alongside VanAB overexpression, consistent with regulation and detoxification as major constraints on growth with vanillate (bleem2024evolutionandengineering pages 5-7, bleem2024evolutionandengineering pages 1-2).
No direct experimental localization (e.g., fractionation, microscopy tagging) for KT2440 VanA was found in the retrieved sources. The available evidence supports VanA as an intracellular aromatic-catabolic enzyme (Rieske oxygenases are typically cytosolic), but this should be treated as an inference rather than a directly demonstrated localization in KT2440 (bleem2024evolutionandengineering pages 2-3, donoso2022identificationofa pages 1-2).
Bleem et al. (2024-07; Metabolic Engineering) directly interrogated and optimized aromatic O-demethylation in KT2440, comparing the native VanAB mechanism to a heterologous tetrahydrofolate-dependent demethylase (LigM) (https://doi.org/10.1016/j.ymben.2024.06.009) (bleem2024evolutionandengineering pages 1-2). Key findings relevant to functional annotation of VanA include:
- VanAB is the native vanillate O-demethylation route producing protocatechuate and formaldehyde (bleem2024evolutionandengineering pages 2-3).
- Adaptive laboratory evolution and targeted mutations improved performance; evolved VanAB strains showed ~1.8× faster growth than LigM strains, and combining key mutations yielded ~5× faster vanillate consumption in the first 8 hours than wild type (bleem2024evolutionandengineering pages 1-2).
- Mutations were enriched in formaldehyde detoxification genes (e.g., fghA and related loci) and in regulatory loci, highlighting that successful VanA-driven metabolism requires coordinated management of formaldehyde stress and redox/flux (bleem2024evolutionandengineering pages 5-7, bleem2024evolutionandengineering pages 1-2).
Werner et al. (2023-09; Science Advances) engineered P. putida KT2440 for biological funneling of mixed lignin-related aromatics to β-ketoadipic acid and report tuning enzymes for O-demethylation (including vanillate O-demethylation), hydroxylation, and ring-opening steps (https://doi.org/10.1126/sciadv.adj0053) (werner2023ligninconversionto pages 1-2). Reported bioprocess metrics demonstrate real-world relevance of VanA-adjacent steps:
- β-ketoadipate titers: 44.5 g/L (model aromatics), 25 g/L (corn stover–derived LRCs)
- Productivities: 1.15 and 0.66 g·L⁻¹·h⁻¹
- Yield: 0.10 g product per g corn stover–derived lignin (and 1.0 mol/mol on model substrates)
- Technoeconomic estimate: minimum selling price $2.01/kg (werner2023ligninconversionto pages 1-2).
These data position VanA-dependent funneling (via protocatechuate formation from vanillate) as part of a quantitatively validated pathway toward industrially relevant aromatic bioproducts (werner2023ligninconversionto pages 1-2).
VanA’s primary value in KT2440 is as a gateway enzyme enabling assimilation of vanillate and related lignin-derived aromatics by converting them into protocatechuate for downstream ring cleavage and conversion into commodity/product precursors (bleem2024evolutionandengineering pages 2-3, werner2023ligninconversionto pages 1-2).
Two recurring engineering strategies illustrate VanA’s practical role:
1. Overexpress/optimize vanAB to accelerate funneling and reduce accumulation of upstream aromatics, but then manage formaldehyde toxicity and redox demands (bleem2024evolutionandengineering pages 1-2, bleem2024evolutionandengineering pages 5-7).
2. Delete vanAB when the desired product is upstream of vanillate assimilation (e.g., to prevent consumption of vanillate/vanillin-derived intermediates in strains designed to accumulate aromatic aldehydes/derivatives) (bleem2024evolutionandengineering pages 2-3).
When vanAB from Pseudomonas putida was expressed in E. coli, whole-cell extract assays produced 15.5 ± 2.2 mM protocatechuate after 3 h, with a reported specific activity 0.88 μmol·min⁻¹·g⁻¹ (whole-cell extract basis), and activity supported by NADH or NADPH (hibi2005functionalcouplingbetween pages 2-4). In vivo, formate accumulation reached roughly half of protocatechuate accumulation, consistent with partial conversion of released formaldehyde to formate (hibi2005functionalcouplingbetween pages 4-5).
A quantitative metabolism study of KT2440 reported a vanillate uptake rate of 8.2 mmol·gCDW⁻¹·h⁻¹ under a standardized condition of 100 mM carbon equivalent substrate loading (zhou2025quantitativedecodingof pages 11-12). The same work modeled vanillate O-demethylation with NADH usage based on a stated NADH preference of VanB (zhou2025quantitativedecodingof pages 11-12).
Engineered KT2440 conversion of lignin-derived aromatic mixtures to β-ketoadipate achieved industrially relevant metrics (titers/productivities/yields and technoeconomic estimate), in which O-demethylation steps including vanillate O-demethylation were among targeted pathway nodes (werner2023ligninconversionto pages 1-2).
The following figure region shows the vanillate → protocatechuate step annotated with vanA (PP_3736) / vanB (PP_3737) in P. putida KT2440 (garciahidalgo2020vanillinproductionin media cf4cdebe, garciahidalgo2020vanillinproductionin media 14e8286d).
| Feature | Summary for Pseudomonas putida KT2440 VanA (UniProt Q88GI6; gene vanA; locus PP_3736) | Supporting citation(s) |
|---|---|---|
| Identity verification | The target is VanA/PP_3736 from P. putida KT2440, annotated as the oxygenase component of vanillate O-demethylase; the partner gene is vanB/PP_3737. A pathway figure for KT2440 explicitly places vanA/vanB at the vanillate (vanillic acid) → protocatechuate (protocatechuic acid) step. | (garciahidalgo2020vanillinproductionin pages 10-11, garciahidalgo2020vanillinproductionin pages 8-9, garciahidalgo2020vanillinproductionin media cf4cdebe) |
| Primary biochemical function | VanA is the terminal oxygenase of the two-component VanAB vanillate O-demethylase system that catalyzes oxidative demethylation of vanillate to protocatechuate, releasing formaldehyde as a coproduct. | (hibi2005functionalcouplingbetween pages 1-2, bleem2024evolutionandengineering pages 2-3) |
| Enzyme class / mechanism | VanAB is described as a Rieske non-heme iron monooxygenase / Rieske-type aromatic O-demethylase. The chemistry is an oxidative O-demethylation rather than a THF-dependent methyl-transfer route. | (bleem2024evolutionandengineering pages 2-3, donoso2022identificationofa pages 1-2, bleem2024evolutionandengineering pages 1-2) |
| Reaction | Canonical reaction in KT2440: vanillate + reducing equivalents + O2 → protocatechuate + formaldehyde (exact stoichiometric balancing varies by assay framing, but all cited sources agree on vanillate-to-protocatechuate conversion with formaldehyde release). | (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 2-4, hibi2005functionalcouplingbetween pages 1-2) |
| Cofactors / metal centers | VanA-family oxygenases contain a Rieske [2Fe-2S] cluster and a non-heme iron catalytic center; electron transfer is supplied through the reductase partner and can draw on NADH and/or NADPH in assays. | (tuomela2025conversionandupgrading pages 15-17, donoso2022identificationofa pages 1-2, hibi2005functionalcouplingbetween pages 2-4) |
| Partner subunit VanB | VanB is the reductase component of the two-component system. General VanAB descriptions assign VanB FMN-, NADPH-, and [2Fe-2S]-binding features and the role of delivering electrons to VanA for catalysis. In KT2440 literature, VanB is explicitly the reductase for vanillate O-demethylase. | (donoso2022identificationofa pages 1-2, bleem2024evolutionandengineering pages 1-2) |
| Subunit architecture | VanAB is a two-component system, commonly described as VanA (oxygenase) + VanB (reductase); one study further refers to it as a heterodimeric system in the context of Pseudomonas vanillate O-demethylase. | (hibi2005functionalcouplingbetween pages 1-2, tuomela2025conversionandupgrading pages 15-17) |
| Substrate specificity: confirmed core substrate | The best-supported physiological substrate in KT2440 is vanillate. VanAB enables growth on vanillate as a sole carbon/energy source by converting it to protocatechuate, which then enters central aromatic catabolism. | (bleem2024evolutionandengineering pages 2-3, bleem2024evolutionandengineering pages 1-2, garciahidalgo2020vanillinproductionin media cf4cdebe) |
| Substrate specificity: broader/promiscuous activity | Across homologous VanAB systems, activity extends to meta-methoxylated aromatic acids and sometimes compounds such as veratrate and syringate/3MGA, but the evidence indicates clear preference for vanillate (and in some systems syringate) over 3MGA. For KT2440 specifically, recent comparative work notes slower syringate conversion and no in vivo 3MGA O-demethylation despite in vitro activity toward 3MGA. | (tuomela2025conversionandupgrading pages 15-17, donoso2022identificationofa pages 1-2, wolf2024thecatabolismof pages 9-14, donoso2022identificationofa pages 4-5) |
| Product and byproduct | Main aromatic product is protocatechuate; one-carbon byproduct is formaldehyde, creating a need for detoxification or assimilation capacity during growth/engineering. | (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 1-2, hibi2005functionalcouplingbetween pages 4-5) |
| Pathway role | VanA operates in the upper funneling pathway for lignin-derived guaiacyl aromatics, especially vanillate produced from compounds such as ferulate/vanillin. The product protocatechuate feeds into the β-ketoadipate/pca pathway. | (garciahidalgo2020vanillinproductionin pages 10-11, garciahidalgo2020vanillinproductionin media cf4cdebe, bleem2024evolutionandengineering pages 2-3) |
| Physiological importance in KT2440 | Native VanAB supports growth on vanillate and is central to lignin-aromatic funneling. In adaptive laboratory evolution and pathway-engineering experiments, boosting VanAB function improved vanillate utilization and aromatic catabolism. | (bleem2024evolutionandengineering pages 1-2, bleem2024evolutionandengineering pages 2-3) |
| Genetic context / operon | In KT2440, vanA and vanB are organized as a vanAB operon. Multiple studies discuss deletion or constitutive re-expression of this operon in engineering backgrounds. | (bleem2024evolutionandengineering pages 2-3, hibi2005functionalcouplingbetween pages 1-2, bleem2024evolutionandengineering pages 1-2) |
| Regulation | Evidence summarized from recent comparative work indicates regulation by VanR, a negative transcriptional regulator relieved by vanillate as inducer/effector. ALE studies in KT2440 also identified beneficial mutations in regulators and formaldehyde-detox genes linked to improved VanAB-dependent growth. | (tuomela2025conversionandupgrading pages 15-17, bleem2024evolutionandengineering pages 1-2, bleem2024evolutionandengineering pages 5-7) |
| Cellular localization | No direct experimental localization for KT2440 VanA was recovered in the gathered sources. Given its classification as a bacterial Rieske non-heme iron oxygenase with no evidence here for secretion or membrane anchoring, the most defensible annotation from current evidence is intracellular/cytosolic aromatic catabolism rather than extracellular function. | (bleem2024evolutionandengineering pages 2-3, donoso2022identificationofa pages 1-2) |
| Formaldehyde coupling / detoxification | VanAB function is tightly coupled to formaldehyde detoxification. In heterologous expression experiments, formate accumulation began as protocatechuate formed, and loss of frmA sharply reduced formate production and impaired conversion, showing the burden imposed by VanAB-derived formaldehyde. In KT2440 ALE, mutations in fghA and related loci were selected in VanAB backgrounds. | (hibi2005functionalcouplingbetween pages 4-5, bleem2024evolutionandengineering pages 1-2, bleem2024evolutionandengineering pages 5-7) |
| Quantitative assay data | In E. coli expressing P. putida vanAB, lysate assays produced 15.5 ± 2.2 mM protocatechuate after 3 h with reported specific activity 0.88 μmol protocatechuate min−1 g−1 whole-cell extract; 5 mM vanillate was used in whole-cell assays, and both NADH/NADPH supported activity. | (hibi2005functionalcouplingbetween pages 2-4) |
| Quantitative physiology / engineering data in KT2440 | In a 2024 KT2440 study, evolved strains relying on native VanAB showed ~1.8-fold faster growth than THF-dependent demethylase strains, and combining top mutations yielded ~5-fold faster vanillate consumption during the first 8 h versus wild type. | (bleem2024evolutionandengineering pages 1-2) |
| Quantitative relevance to production strain design | Deleting vanAB is a standard strategy when the goal is to accumulate vanillin/vanillate-derived products rather than consume them. Example: a 2025 KT2440-derived vanillin process explicitly included vanAB deletion; with in situ product recovery, total vanillin recovery reached 3.35 g/L from ferulic acid. | (bleem2024evolutionandengineering pages 2-3, bleem2024evolutionandengineering pages 1-2) |
| Real-world / biotechnological applications | VanA is important in lignin valorization, where microbial strains are engineered either to enhance O-demethylation/funneling (improving assimilation of methoxylated aromatics) or to disable vanAB to accumulate upstream products such as vanillin or route flux to polymer precursors such as β-ketoadipate/muconate. | (bleem2024evolutionandengineering pages 2-3, bleem2024evolutionandengineering pages 1-2, wolf2024thecatabolismof pages 9-14) |
| Key references (year / DOI / URL) | Bleem et al., 2024, Metabolic Engineering, doi: 10.1016/j.ymben.2024.06.009, https://doi.org/10.1016/j.ymben.2024.06.009; Hibi et al., 2005, FEMS Microbiol Lett., doi: 10.1016/j.femsle.2005.09.036, https://doi.org/10.1016/j.femsle.2005.09.036; García-Hidalgo et al., 2020, Appl Environ Microbiol, doi: 10.1128/AEM.02442-19, https://doi.org/10.1128/AEM.02442-19; broader VanAB context: Donoso et al., 2022, doi: 10.3390/microorganisms11010078, https://doi.org/10.3390/microorganisms11010078. | (bleem2024evolutionandengineering pages 1-2, hibi2005functionalcouplingbetween pages 2-4, garciahidalgo2020vanillinproductionin pages 10-11, donoso2022identificationofa pages 1-2) |
Table: This table summarizes the functional annotation of VanA (Q88GI6/PP_3736) in Pseudomonas putida KT2440, covering identity, reaction, cofactors, pathway context, regulation, quantitative data, and engineering relevance. Each row is explicitly tied to the gathered evidence contexts for direct traceability.
References
(garciahidalgo2020vanillinproductionin pages 10-11): Javier García-Hidalgo, Daniel P. Brink, Krithika Ravi, Catherine J. Paul, Gunnar Lidén, and Marie F. Gorwa-Grauslund. Vanillin production in pseudomonas : whole-genome sequencing of pseudomonas sp. strain 9.1 and reannotation of pseudomonas putida cala as a vanillin reductase. Mar 2020. URL: https://doi.org/10.1128/aem.02442-19, doi:10.1128/aem.02442-19. This article has 42 citations and is from a peer-reviewed journal.
(bleem2024evolutionandengineering pages 2-3): Alissa C. Bleem, Eugene Kuatsjah, Josefin Johnsen, Elsayed T. Mohamed, William G. Alexander, Zoe A. Kellermyer, Austin L. Carroll, Riccardo Rossi, Ian B. Schlander, George L. Peabody V, Adam M. Guss, Adam M. Feist, and Gregg T. Beckham. Evolution and engineering of pathways for aromatic o-demethylation in pseudomonas putida kt2440. Jul 2024. URL: https://doi.org/10.1016/j.ymben.2024.06.009, doi:10.1016/j.ymben.2024.06.009. This article has 26 citations and is from a domain leading peer-reviewed journal.
(garciahidalgo2020vanillinproductionin media cf4cdebe): Javier García-Hidalgo, Daniel P. Brink, Krithika Ravi, Catherine J. Paul, Gunnar Lidén, and Marie F. Gorwa-Grauslund. Vanillin production in pseudomonas : whole-genome sequencing of pseudomonas sp. strain 9.1 and reannotation of pseudomonas putida cala as a vanillin reductase. Mar 2020. URL: https://doi.org/10.1128/aem.02442-19, doi:10.1128/aem.02442-19. This article has 42 citations and is from a peer-reviewed journal.
(hibi2005functionalcouplingbetween pages 1-2): Makoto Hibi, Tomonori Sonoki, and Hideo Mori. Functional coupling between vanillate-o-demethylase and formaldehyde detoxification pathway. FEMS microbiology letters, 253 2:237-42, Dec 2005. URL: https://doi.org/10.1016/j.femsle.2005.09.036, doi:10.1016/j.femsle.2005.09.036. This article has 58 citations and is from a peer-reviewed journal.
(donoso2022identificationofa pages 1-2): Raúl A. Donoso, Ricardo Corbinaud, Carla Gárate-Castro, Sandra Galaz, and Danilo Pérez-Pantoja. Identification of a phylogenetically divergent vanillate o-demethylase from rhodococcus ruber r1 supporting growth on meta-methoxylated aromatic acids. Microorganisms, 11:78, Dec 2022. URL: https://doi.org/10.3390/microorganisms11010078, doi:10.3390/microorganisms11010078. This article has 6 citations.
(bleem2024evolutionandengineering pages 1-2): Alissa C. Bleem, Eugene Kuatsjah, Josefin Johnsen, Elsayed T. Mohamed, William G. Alexander, Zoe A. Kellermyer, Austin L. Carroll, Riccardo Rossi, Ian B. Schlander, George L. Peabody V, Adam M. Guss, Adam M. Feist, and Gregg T. Beckham. Evolution and engineering of pathways for aromatic o-demethylation in pseudomonas putida kt2440. Jul 2024. URL: https://doi.org/10.1016/j.ymben.2024.06.009, doi:10.1016/j.ymben.2024.06.009. This article has 26 citations and is from a domain leading peer-reviewed journal.
(tuomela2025conversionandupgrading pages 15-17): Heidi Tuomela, Johanna Koivisto, Elena Efimova, and Suvi Santala. Conversion and upgrading of s-lignin related syringate by acinetobacter baylyi adp1. Mar 2025. URL: https://doi.org/10.21203/rs.3.rs-6218493/v1, doi:10.21203/rs.3.rs-6218493/v1.
(hibi2005functionalcouplingbetween pages 2-4): Makoto Hibi, Tomonori Sonoki, and Hideo Mori. Functional coupling between vanillate-o-demethylase and formaldehyde detoxification pathway. FEMS microbiology letters, 253 2:237-42, Dec 2005. URL: https://doi.org/10.1016/j.femsle.2005.09.036, doi:10.1016/j.femsle.2005.09.036. This article has 58 citations and is from a peer-reviewed journal.
(hibi2005functionalcouplingbetween pages 4-5): Makoto Hibi, Tomonori Sonoki, and Hideo Mori. Functional coupling between vanillate-o-demethylase and formaldehyde detoxification pathway. FEMS microbiology letters, 253 2:237-42, Dec 2005. URL: https://doi.org/10.1016/j.femsle.2005.09.036, doi:10.1016/j.femsle.2005.09.036. This article has 58 citations and is from a peer-reviewed journal.
(zhou2025quantitativedecodingof pages 11-12): Nanqing Zhou, Rebecca A. Wilkes, Xinyu Chen, Kelly P. Teitel, James A. Belgrave, Gregg T. Beckham, Allison Z. Werner, Yanbao Yu, and Ludmilla Aristilde. Quantitative decoding of coupled carbon and energy metabolism in pseudomonas putida for lignin carbon utilization. Communications Biology, Aug 2025. URL: https://doi.org/10.1038/s42003-025-08723-3, doi:10.1038/s42003-025-08723-3. This article has 7 citations and is from a peer-reviewed journal.
(donoso2022identificationofa pages 4-5): Raúl A. Donoso, Ricardo Corbinaud, Carla Gárate-Castro, Sandra Galaz, and Danilo Pérez-Pantoja. Identification of a phylogenetically divergent vanillate o-demethylase from rhodococcus ruber r1 supporting growth on meta-methoxylated aromatic acids. Microorganisms, 11:78, Dec 2022. URL: https://doi.org/10.3390/microorganisms11010078, doi:10.3390/microorganisms11010078. This article has 6 citations.
(wolf2024thecatabolismof pages 9-14): Megan E. Wolf, Anne T. Lalande, Brianne L. Newman, Alissa C. Bleem, Chad T. Palumbo, Gregg T. Beckham, and Lindsay D. Eltis. The catabolism of lignin-derived p-methoxylated aromatic compounds by rhodococcus jostii rha1. Applied and Environmental Microbiology, Feb 2024. URL: https://doi.org/10.1128/aem.02155-23, doi:10.1128/aem.02155-23. This article has 16 citations and is from a peer-reviewed journal.
(bleem2024evolutionandengineering pages 5-7): Alissa C. Bleem, Eugene Kuatsjah, Josefin Johnsen, Elsayed T. Mohamed, William G. Alexander, Zoe A. Kellermyer, Austin L. Carroll, Riccardo Rossi, Ian B. Schlander, George L. Peabody V, Adam M. Guss, Adam M. Feist, and Gregg T. Beckham. Evolution and engineering of pathways for aromatic o-demethylation in pseudomonas putida kt2440. Jul 2024. URL: https://doi.org/10.1016/j.ymben.2024.06.009, doi:10.1016/j.ymben.2024.06.009. This article has 26 citations and is from a domain leading peer-reviewed journal.
(werner2023ligninconversionto pages 1-2): Allison Z. Werner, William T. Cordell, Ciaran W. Lahive, Bruno C. Klein, Christine A. Singer, Eric C. D. Tan, Morgan A. Ingraham, Kelsey J. Ramirez, Dong Hyun Kim, Jacob Nedergaard Pedersen, Christopher W. Johnson, Brian F. Pfleger, Gregg T. Beckham, and Davinia Salvachúa. Lignin conversion to β-ketoadipic acid by pseudomonas putida via metabolic engineering and bioprocess development. Science Advances, Sep 2023. URL: https://doi.org/10.1126/sciadv.adj0053, doi:10.1126/sciadv.adj0053. This article has 88 citations and is from a highest quality peer-reviewed journal.
(garciahidalgo2020vanillinproductionin media 14e8286d): Javier García-Hidalgo, Daniel P. Brink, Krithika Ravi, Catherine J. Paul, Gunnar Lidén, and Marie F. Gorwa-Grauslund. Vanillin production in pseudomonas : whole-genome sequencing of pseudomonas sp. strain 9.1 and reannotation of pseudomonas putida cala as a vanillin reductase. Mar 2020. URL: https://doi.org/10.1128/aem.02442-19, doi:10.1128/aem.02442-19. This article has 42 citations and is from a peer-reviewed journal.
(garciahidalgo2020vanillinproductionin pages 8-9): Javier García-Hidalgo, Daniel P. Brink, Krithika Ravi, Catherine J. Paul, Gunnar Lidén, and Marie F. Gorwa-Grauslund. Vanillin production in pseudomonas : whole-genome sequencing of pseudomonas sp. strain 9.1 and reannotation of pseudomonas putida cala as a vanillin reductase. Mar 2020. URL: https://doi.org/10.1128/aem.02442-19, doi:10.1128/aem.02442-19. This article has 42 citations and is from a peer-reviewed journal.