Degradation of (S)-1,3-butanediol in Pseudomonas putida KT2440 reveals a CoA-activation route and enantiomeric crosstalk between (R)- and (S)-3-hydroxybutyrate catabolism.

Pseudomonas putida KT2440 degrades (S)-1,3-butanediol via an ATP-dependent CoA-activation pathway involving enantioselective acyl-CoA synthetase PP_3458.

• Why it matters: Understanding how aerobic bacteria metabolize the (S)-enantiomer of 1,3-butanediol fills a key gap in diol metabolism knowledge and can enable biotechnological applications like chiral resolution and biosensing.
• What they did: The study used transcriptomics, gene deletions, and complementation to reveal that PP_3458 activates (S)-3-hydroxybutyrate to its CoA thioester, with strong enantioselectivity and inhibition by (R)-3-hydroxybutyrate, demonstrating a mechanistically distinct route from anaerobic bacteria.
• The result: This enzymatic insight enables high enantiomeric excess kinetic resolution of racemic 3-hydroxybutyrate and the development of biosensors for detecting 1,3-butanediol, advancing biotechnological tools for chiral compound production and strain screening.