Calorimetric characterization of the stability and activity of trimethylamine-N-oxide (TMAO) demethylase from Methylocella silvestris BL2.

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,

SUBMITTER: Cappa F 

PROVIDER: S-EPMC12560246 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature