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Fig. 4 | Biotechnology for Biofuels and Bioproducts

Fig. 4

From: Systems metabolic engineering of Escherichia coli for hyper-production of 5‑aminolevulinic acid

Fig. 4

Protein engineering of ALAS for releasing heme inhibition and improving catalytic activity. A Specific activities and residual activities with hemin of ALAS and its double-site mutants. Residual activity was determined after incubating the enzyme with 2.5 µM hemin at 37 ℃ for 1 h. Residual activity was reported as a percentage of the activity measured without hemin. B Inhibition curve of wild-type ALAS and mutant C75A/R365K with different concentration of hemin. C 5-ALA titer, yield and D biomass of strains overexpressing the wild-type ALAS (strain ALA10) and ALASC75A/R365K mutant (strain ALA11): replacement the wild-type hemA gene of ALA10 to mutant hemAC75A/R365K gene. Data are presented as mean values +/− SD (n = 3 independent experiments). **P < 0.01, *P < 0.05, Student’s two-tailed t-test

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