ArticleProtein science : a publication of the Protein Society2025
Calorimetric characterization of the stability and activity of trimethylamine-N-oxide (TMAO) demethylase from Methylocella silvestris BL2.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Article
- Calorimetric characterization of the stability and activity of trimethylamine-N-oxide (TMAO) demethylase from Methylocella silvestris BL2.Protein science : a publication of the Protein Society · 2025Article
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9 authors.
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Abstract
Trimethylamine-N-oxide (TMAO) is an organic osmolyte found in numerous species and is known to have a range of biological effects. TMAO has recently garnered attention in the medical field due to its association with cardiovascular diseases, underscoring the need for its reliable detection and quantification. Current methods for TMAO analysis often rely on hazardous reagents or costly analytical instrumentation. In this study, we focus on Methylocella silvestris BL2, which produces a TMAO-demethylase (Tdm), with the aim of developing a direct enzymatic assay for TMAO detection. We report on the bioinformatic analysis, expression, purification, and calorimetric characterization of Tdm. Structural predictions generated by AlphaFold suggest that the protein, previously described as hexameric, is organized as a trimer of dimers. The 3D model reveals that the binding sites for the metal cofactors Zn
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