ArticleScience advances2026
A programmable bifunctional flavoenzyme for direct amine-to-ester conversion.
Article in Science advances, 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
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unification of mechanistically distinct oxidative transformations within a single enzyme active site represents a long-standing challenge in biocatalysis. In particular, flavin-dependent oxidative deamination and Baeyer-Villiger oxidation have remained evolutionarily and mechanistically segregated, raising fundamental questions as to whether their catalytic cycles can be coherently integrated without mutual interference. Here, we report a bifunctional ancestral flavoenzyme, AncFO-221, reconstructed using a function-oriented ancestral sequence reconstruction strategy, which enables direct amine-to-ester conversion within a single active site. Combined experimental and computational analyses reveal a unified catalytic framework in which histidine-assisted proton and hydride transfer during amine oxidation is intrinsically coupled to C
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.