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In this study, a novel enzymatic approach to transform levulinic acid (LA), which can be obtained from biomass, into value-added ( R )-4-aminopentanoic acid using an engineered glutamate dehydrogenase from  Escherichia coli  ( Ec GDH) was developed. Through crystal structure comparison, two residues (K116 and N348), especially residue 116, were identified to affect the substrate specificity of  Ec GDH. After targeted saturation mutagenesis, the mutant  Ec GDH K116C , which was active toward LA, was identified. Screening of the two-site combinatorial saturation mutagenesis library with  Ec GDH K116C  as positive control, the  k  cat / K  m  of the obtained  Ec GDH K116Q/N348M  for LA and NADPH were 42.0- and 7.9-fold higher, respectively, than that of  Ec GDH K116C . A molecular docking investigation was conducted to explain the catalytic activity of the mutants and stereoconfiguration of the product. Coupled with formate dehydrogenase,  Ec GDH K116Q/N348M  was found to be able to convert 0.4 M LA by more than 97% in 11 h, generating ( R )-4-aminopentanoic acid with &amp;gt;99% enantiomeric excess ( ee ). This dual-enzyme system used sustainable raw materials to synthesize ( R )-4-aminopentanoic acid with high atom utilization as it utilizes cheap ammonia as the amino donor, and the inorganic carbonate is the sole by-product.

A Sustainable Approach for Synthesizing (R)-4-Aminopentanoic Acid From Levulinic Acid Catalyzed by Structure-Guided Tailored Glutamate Dehydrogenase