Fig. 3: Bioproduction of mevalonate from formate. | Nature Communications

Fig. 3: Bioproduction of mevalonate from formate.

From: Fast growth and high-titer bioproduction from renewable formate via metal-dependent formate dehydrogenase in Escherichia coli

Fig. 3

a Schematic depicting the mevalonate pathway by which the output metabolite of the rGlyP, pyruvate (left), is transformed into mevalonate (right). Heterologously expressed enzymes catalyzing these reactions are denoted below their respective reactions. b Mixotrophic bioproduction of mevalonate conducted with 100 mM formate and 1 mM glucose to assay differences in bioproduction at small scale in batch mode. All differences between K4e and K4M strains are significant (K4M*_mev p = 0.003, K4Me1_mev p = 0.002, K4Me2_mev p = 0.0002) (n = 4). c Analysis of the proteomic allocation to mevalonate biosynthetic enzymes. The expression of each gene in all K4M strains is significantly higher than in K4e (K4M*_mev p = 0.01, K4Me1_mev p = 0.002, K4Me2_mev p = 0.005) (n = 4). Individual data points are shown as the sum of the mevalonate pathway enzymes within each biological sample. d Fed-batch bioproduction using K4e and the most productive strain from small-scale, batch experimentation (K4Me2). All strains were induced with 0.5 mM IPTG at 65 h post inoculation to induce bioproduction. K4Me2 produced a maximum titer of 3.3 and 3.8 g/L while K4e produced significantly less mevalonate (p = 0.02) with a maximum titer of 1.3 and 1.2 g/L (n = 2). Data represent the mean ± s.d. of biological replicates. All statistical analysis was performed using a two-tailed t-test. Source data are provided as a Source Data file.

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