ArticleCommunications biology2025
Discovery of a distinct type of methylenetetrahydrofolate reductase family that couples with tetrahydrofolate-dependent demethylases.
Article in Communications 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
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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
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Who cites it
1 citing paper in PubMed.
- 5,10-Methylenetetrahydrofolate Reductase─the Key Allosteric Regulator in One-Carbon Metabolism.Biochemistry · 2026Review
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Authors and funding
7 authors.
Funding
Abstract
Methylenetetrahydrofolate reductase (MTHFR) is a key enzyme in one-carbon (1C) metabolism, catalyzing the reduction of methylenetetrahydrofolate to methyltetrahydrofolate. Interestingly, Sphingobium lignivorans SYK-6, a model bacterium for the catabolism of lignin-derived aromatic compounds, possesses a unique MTHFR (S6MTHFR) that catalyzes the reverse reaction of typical MTHFRs-namely, the oxidation of methyltetrahydrofolate. However, no direct evidence supports this function. Here, we show that S6MTHFR catalyzes the oxidation of methyltetrahydrofolate and elucidate the molecular mechanism underlying the unique enzymatic properties of S6MTHFR based on its crystal structure. Furthermore, a database search reveals that a group of bacteria, including S. lignivorans SYK-6, utilize tetrahydrofolate-dependent demethylases to produce methyltetrahydrofolate, which is subsequently oxidized by an S6MTHFR-type enzyme. We propose that the combination of a demethylase with an S6MTHFR-type enzyme represents a distinct type of 1C metabolism that may regulate methionine biosynthesis.
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Registered trials
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