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. 2020 May 13;5(2):62–80. doi: 10.1016/j.synbio.2020.04.001

Fig. 5.

Fig. 5

A) Overview of the ability of KS1 to extend unnatural N-acetyl cysteamine substrates. B) Panel of substrates tested. C) Structure of EryKS3 (pdb code 2QO3) with the residues mutated to explore the sequence space divergence in the mycolactone KSs. D) Sequence alignment of the KSs within DEBS and the those within the mycolactone PKS. The residue found by our laboratory in a common assembly of DEBS1-TE is highlighted (mutated to histidine to introduce a restriction site). The alignment was performed with MUSCLE.