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

ABSTRACT: 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 (EcGDH) was developed. Through crystal structure comparison, two residues (K116 and N348), especially residue 116, were identified to affect the substrate specificity of EcGDH. After targeted saturation mutagenesis, the mutant EcGDH^K116C, which was active toward LA, was identified. Screening of the two-site combinatorial saturation mutagenesis library with EcGDH^K116C as positive control, the k _cat/K _m of the obtained EcGDH^K116Q/N348M for LA and NADPH were 4

SUBMITTER: Zhou F 

PROVIDER: S-EPMC8784811 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature