Steen et al. (2010) have made the following modifications to overproduce fatty acyl-coAs in E. coli:
- Overexpression of a leaderless thioesterase A (‘tesA): E. coli naturally produces fatty acyl-ACPs from sugars via fatty acid biosynthesis (FAB) pathways. E. coli uses a native thioesterase A (tesA) enzyme to convert these fatty acyl-ACPs into free fatty acids. Others have shown that overexpressing a leaderless version of tesA, designated ‘tesA, which is targeted to the cytosol instead of the periplasm, causes a buildup of free fatty acids by disrupting regulation of fatty-acid synthesis (Cho and Cronan 1995; Liu et al. 2012).
- Overexpression of fatty acid degradation D (fadD): in E. coli, fatty acid degradation D (fadD) enzyme catalyses the first step in E. coli beta-oxidation, the conversion of free fatty acids into fatty acyl-coA’s. By overexpressing this gene, one can increase the production of fatty acyl-coAs from the free fatty acids produced by ‘tesA (Steen et al. 2010).
- Knockout of fatty acid degradation E (ΔfadE): fadE catalyzes the second step in fatty acid degradation and uses fatty acyl-CoA’s as substrates. In order to prevent the to prevent the degradation of fatty acyl-CoAs, the β-oxidation pathway was blocked by deleting the fadE gene (Steen et al. 2010).
Next, Steen et al. (2010) have made the following modifications to overproduce ethanol in E. coli:
- Insertion of pyruvate decarboxylase (pdc): pdc is an enzyme from Zymomonas mobilis that converts pyruvate into acetaldehyde. E. coli naturally produces pyruvate from simple sugars.
- Insertion of alcohol dehydrogenase (adhB): adhB is an enzyme from Zymomonas mobilis that converts acetaldehyde into ethanol.