ArticleACS synthetic biology2025
Promiscuity of an Alcohol-Dependent Hemiterpene Pathway for the In Vivo Production of a Non-Natural Alkylated Tryptophan Derivative.
Article in ACS synthetic biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Development of a transcription factor-based biosensor strain for reporting α-terpineol productionRSC chemical biology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The prenyl motif determines the biological activity of many natural products. Yet, structural diversification of the prenyl site has been restricted due to the limitations of native biosynthetic pathways to hemiterpenes, the universal isoprenoid building blocks. Previously, we developed the artificial alcohol dependent hemiterpene (ADH) pathway comprising the acid phosphatase PhoN and the isopentenyl kinase IPK to provide natural isoprenoids assembled from hemiterpenes in vivo. Here, we revealed the broad specificity of the first enzyme of the ADH module, PhoN, and a downstream aromatic prenyltransferase. We then showed that the combined promiscuity of the ADH module and prenyltransferase were sufficient to produce a non-natural-alkylated tryptophan derivative in vivo when coupled with the previously described promiscuity of IPK. The short and modular ADH pathway provides a convenient and scalable approach to alkyl-pyrophosphates and facilitates probing the promiscuity of other downstream enzymes involved in isoprenoid biosynthesis without the tedious in vitro preparation of alkyl-pyrophosphates. This sets the stage to leverage the ADH pathway to forward engineer isoprenoid biosynthesis and expand its chemical space accessible to synthetic biology.
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.