ArticleMicrobial cell factories2026
Biocatalytic synthesis of alkoxylated phenazine derivatives using methyltransferases.
Article in Microbial cell factories, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPhenazines are important nitrogen-containing heterocycles with diverse applications in the chemical and pharmaceutical industry. Alkoxylated phenazines, in particular, exhibit promising acaricidal and fungicidal properties. Currently, chemical synthesis is the main approach for alkoxylated phenazines and derivatives production. However, these processes are associated with harsh reaction conditions, accumulation of chemical waste (e.g., organic solvents, noble metal catalysts), and environmental concerns.
resultsIn this study, we developed biocatalytic systems for the synthesis of alkoxylated phenazines by designing enzymatic systems and de novo biosynthetic pathways. The O-methyltransferase LaphzM from Lysobacter antibioticus OH13 was shown to catalyze the alkoxylation of phenazines using SAM analogs generated in situ by halide methyltransferases (HMTs) from Burkholderia xenovorans and Arabidopsis thaliana. Using these enzymatic systems, we successfully synthesized six alkoxylated phenazine derivatives, including three novel compounds. We further established de novo biosynthetic pathways for 1-ethoxyphenazine and 2-ethoxyphenazine in Pseudomonas chlororaphis via the direct sulfurylation pathway from S. cerevisiae. To improve production, we optimized whole-cell systems, achieving 486.3 mg/L (54% yield) of 2-ethoxyphenazine, 218.1 mg/L (22.8% yield) of 2-propoxyphenazine and 378.2 mg/L (78.4% yield) of 1-ethoxyphenazine-N'10-oxide within 7 h using microbially produced 2-hydroxyphenazine (for 2-ethoxyphenazine and 2-propoxyphenazine) or 1-hydroxyphenazine (for 1-ethoxyphenazine-N'10-oxide) as the substrate, along with ethyl iodide (EtI) or propyl iodide (PrI) accordingly.
conclusionsOverall, we successfully established biocatalytic platforms for alkoxylated phenazines through enzymatic catalysis and de novo biosynthetic pathways. Methyltransferases derived from diverse species, including LaphzM and HMTs, play key roles in the SAM-analog-mediated alkylation of phenazines. This study provides a promising alternative to conventional chemical synthesis, with significant potential for the manufacturing of alkoxylated phenazine derivatives.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.