Title:
Integrating assembly-line retrobiosynthesis and enzyme mining for scalable industrial chemical synthesis
Abstract:
Our society requires a drastic shift from the fossil fuel-based industry to a biosustainable economy. Engineering assembly-line or multi-domain megasynthases, such as modular nonribosomal peptide synthetases (NRPS) and type I polyketide synthases (PKS), offers significant potential for replacing parts of petroleum-based chemical synthesis. In one case, a fungal NRPS system enabled the biosynthesis of complex indole alkaloids, identifying key stereoselective enzymes for anthelmintic production. In another, a modular PKS-based platform was engineered to produce industrially relevant diols and amino alcohols, utilizing specific thioreductases for high yields and efficient product control. Additionally, iterative PKS pathways were employed to design and synthesize polycyclopropanated fatty acids with optimized freezing point and energy density properties for aviation biofuels. These recent advancements highlight the versatility of assembly-line enzymes in addressing challenges across biomanufacturing, renewable energy and sustainable development.
Bio:
Qingyun Dan received his B.S. degree in Biology from the School of Life Sciences, Peking University. After that he received his Ph.D. training at the University of Michigan Ann Arbor and obtained Ph.D. in Biochemistry under the mentorship of Professor Janet Smith. His Ph.D. work focused on biochemical and structural elucidation of fungal indole alkaloid biosynthesis, during which he identified and characterized the reduction-dependent Diels-Alder cyclase. After staying in the Smith lab for a short term of postdoc, He then arrived at the University of California Berkeley, working with Professor Jay Keasling on building polyketide synthase-based biosynthetic platforms. His work largely expanded current polyketide synthase design space illustrated by bioproduction of previously inaccessible industrial diols and amino alcohols in high titers
10:30am, Shaffer 3