What question did this study set out to answer?

The research aims to functionally characterize 3-hydroxybenzoate-4-hydroxylase from Pseudarthrobacter phenanthrenivorans.

Revealing 3-hydroxybenzoate-4-hydroxylase from Pseudarthrobacter phenanthrenivorans Sphe3 via In-Cell NMR analysis and molecular cloning

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Reveals enzymatic activity of 3-hydroxybenzoate-4-hydroxylase in a living cellular environment, indicating significant metabolic potential.

The research aims to functionally characterize 3-hydroxybenzoate-4-hydroxylase from Pseudarthrobacter phenanthrenivorans.
Used bioinformatic analyses to identify the Asphe3_36590 gene encoding 3HB4H.
Conducted heterologous expression and in-cell NMR with E. coli to examine enzymatic activity.
Measured Km and Vmax values of the recombinant enzyme for kinetic characterization.
Enzyme displays Michaelis-Menten kinetics with Km of 72.6 µM and Vmax of 42.5 µM × min−1 at pH 8.5 and 25°C.
In-cell NMR showed rapid conversion of 3-hydroxybenzoate to protocatechuate, demonstrating direct enzymatic function.
Represents the first characterized single-subunit FAD-dependent hydroxylase in Actinobacteria.

Asimakoula et al. (2026) studied this question.

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Reveals enzymatic activity of 3-hydroxybenzoate-4-hydroxylase in a living cellular environment, indicating significant metabolic potential.