Pohang University of Science and Technology · 生化学・遺伝学・分子生物学
Professor Gyoo Yeol Jung's research lab specializes in synthetic biology and metabolic engineering, focusing on the rational design and optimization of microbial metabolic pathways for sustainable production of biochemicals. The lab integrates molecular evolution, systems biology, and advanced screening technologies to engineer enzymes and regulatory circuits with enhanced functionality and efficiency. Key research directions include the rational redesign of allosteric regulation in enzymes, development of high-throughput single-cell screening platforms, and in vitro pathway reconstruction using mRNA-enzyme fusion systems. The lab also explores the metabolic potential of alternative carbon sources like acetate and enhances NADPH production for efficient bioproduction.
Figures are computed from collected data and may differ slightly.
Control of enzyme allosteric regulation is required to drive metabolic flux toward desired levels. Although the three-dimensional (3D) structures of many enzyme-ligand complexes are available, it is still difficult to rationally engineer an allosterically regulatable enzyme without decreasing its catalytic activity. Here, we describe an effective strategy to deregulate the allosteric inhibition of enzymes based on the molecular evolution and physicochemical characteristics of allosteric ligand-b
One of the great advantages of microbial fermentation is the capacity to convert various carbon compounds into value-added chemicals. In this regard, there have been many efforts to engineer microorganisms to facilitate utilization of abundant carbon sources. Recently, the potential of acetate as a feedstock has been discovered; efforts have been made to produce various biochemicals from acetate based on understanding of its metabolism. In this review, we discuss the potential sources of acetate
Pathway optimization is difficult to achieve owing to complex, nonlinear, and largely unknown interactions of enzymes, regulators, and metabolites. We report a pathway reconstruction using RNA display–derived messenger RNA–enzyme fusion molecules. These chimeras are immobilized by hybridization of their messenger RNA end with homologous capture DNA spotted on a substrate surface. Enzymes thus immobilized retain activity proportional to the amount of capture DNA, allowing modulation of the relati
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