Skip to main content
. Author manuscript; available in PMC: 2019 Mar 13.
Published in final edited form as: ACS Catal. 2018 Oct 31;8(12):11722–11734. doi: 10.1021/acscatal.8b03171

Figure 7.

Figure 7.

Analysis of the interdependence of thioesterase specificity and FabF concentration. (A) Product distributions for modeled FASs (1 μM of each Fab, 10 μM thioesterase, 10 μM holo-ACP, 1 mM NADPH, 1 mM NADH, 0.5 mM malonyl-CoA, and 0.5 mM acetyl-CoA, 12.5 min) containing thioesterases specific for C4 (BfTES), C8 (CpFatB1), C12 (UcFatB), and C14 acyl-ACPs (TesA). (B) Total production by FASs from (A) with varying concentrations of FabF. FASs that contain thioesterases with narrow substrate specificities (e.g., CpFatB1 and UcFatB) show a pronounced sensitivity to FabF concentration. (C) Optimal concentrations of FabF increase with the length of thioesterase targets in both (i) the base model and (ii) a modified model that lacks inhibition of FabH by acyl-ACPs. The similarity in trends generated by these two models suggests that optimal FabF concentrations do not minimize inhibition but, rather, maximize the availability of acyl-ACPs targeted by thioesterases.