Bioprocess Biosyst Eng
March 2022
This study aimed to improve the catalytic activity of aspartate kinase (AK), the first key rate-limiting enzyme in the aspartic acid metabolism pathway, by site-directed saturation mutagenesis, and to weaken the synergistic feedback inhibition of metabolites and analyze its mechanism using molecular dynamics simulation (MD). The key residual sites around the inhibitor lysine (Lys) were selected to construct the mutant strains. The mutant A380M with significantly increased enzyme activity was obtained through enzyme activity screening.
View Article and Find Full Text PDFIn microorganisms and plants, aspartate kinase (AK) is the initial committed enzyme of the biosynthesis of the aspartate acid family amino acids and is inhibited by end products. In the paper, we mutated the key allosteric regulatory site A380 around the binding site of the Lys inhibitor in AK (AK). A single-mutant A380C was obtained with 12.
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