Optimization of Malonyl Coenzyme A Biosensors in a Reconstituted Cell-Free System for Detecting Acetyl-CoA Carboxylase Activity.

ABSTRACT: Malonyl coenzyme A (malonyl-CoA) is a key precursor in the biosynthesis of fatty acids and polyketides, critical for industrial applications such as biofuel and pharmaceutical productions. Optimizing acetyl-CoA carboxylase (ACC), the enzyme that converts acetyl-CoA to malonyl-CoA, is essential for advancing metabolic engineering. Effective biosensors that detect malonyl-CoA levels are vital for high-throughput screening and directed evolution of ACC. Earlier efforts utilized the Bacillus subtilis FapR/FapO biosensor system in vivo to convert malonyl-CoA concentrations into fluorescent signals. However, B. subtilis biosensors suffered from narrow detection ranges, impeding accurate quantification across the concentrations needed to evaluate ACC activity, and were further limit

SUBMITTER: Ito S 

PROVIDER: S-EPMC12362589 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature