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3-Dehydroshikimate (DHS) is a useful starting metabolite for the biosynthesis of muconic acid (MA) and shikimic acid (SA), which are precursors of various valuable polymers and drugs. Although DHS biosynthesis has been previously reported in several bacteria, the engineered strains were far from satisfactory, due to their low DHS titers. Here, we created an engineered  Escherichia coli  cell factory to produce a high titer of DHS as well as an efficient system for the conversion DHS into MA. First, the genes showing negative effects on DHS accumulation in  E. coli , such as  tyrR  (tyrosine dependent transcriptional regulator),  ptsG  (glucose specific sugar: phosphoenolpyruvate phosphotransferase), and  pykA  (pyruvate kinase 2), were disrupted. In addition, the genes involved in DHS biosynthesis, such as  aroB  (DHQ synthase),  aroD  (DHQ dehydratase),  ppsA  (phosphoenolpyruvate synthase),  galP  (D-galactose transporter),  aroG  (DAHP synthase), and  aroF  (DAHP synthase), were overexpressed to increase the glucose uptake and flux of intermediates. The redesigned DHS-overproducing  E. coli  strain grown in an optimized medium produced ~117 g/L DHS in 7-L fed-batch fermentation, which is the highest level of DHS production demonstrated in  E. coli . To accomplish the DHS-to-MA conversion, which is originally absent in  E. coli , a codon-optimized heterologous gene cassette containing  asbF, aroY , and  catA  was expressed as a single operon under a strong promoter in a DHS-overproducing  E. coli  strain. This redesigned  E. coli  grown in an optimized medium produced about 64.5 g/L MA in 7-L fed-batch fermentation, suggesting that the rational cell factory design of DHS and MA biosynthesis could be a feasible way to complement petrochemical-based chemical processes.

Cell Factory Design and Culture Process Optimization for Dehydroshikimate Biosynthesis in Escherichia coli