Natural enzyme variants often exhibit suboptimal conversion rates and feedback inhibition during industrial fermentation. Enhancing metabolic flux through polypeptide engineering overcomes bottlenecks in amino acid and dipeptide biosynthesis.

Wild-type citrate synthase activity often diverts carbon precursors away from desired amino acid pathways toward the TCA cycle. Attenuating this enzyme resolves the bottleneck of substrate competition to maximize biosynthetic yields.

High citrate synthase activity competes with the desired biosynthetic pathways for carbon precursors. Reducing this enzymatic bottleneck redirects metabolic resources toward target L-amino acid production.