Fig. 4: Statistical analysis of the fatty alcohol production landscape.
From: Machine learning-guided acyl-ACP reductase engineering for improved in vivo fatty alcohol production
a Contributions of each sequence block to the alcohol production of chimeras. b Mapping of the contributions to the structural model of MA-ACR. Blocks with strong effects (either positive or negative) line up with key structural features such as the NADPH binding site, the active site and the ACP binding site. c Correlation between net charge near the binding site and fatty alcohol titer of chimeras. Chimeras with higher net charges tend to produce more alcohols. In addition, three key blocks were found to correlate with both activity and with charge. Combining all three of these blocks results in highly active enzymes. The statistics for the finalized dataset (mean, standard deviation and number of replicates) are available in Supplementary Table 5. d Positions in the parent sequence alignment that contain non-conserved charged residues within 10 Å of the putative ACP binding site (positively charged residues are shown as blue text, negatively charged residues are shown as red text). e Locations of key charged residues in the structural model of MA-ACR docked with palmitoyl-ACP. Optimal combinations of blocks could produce more favorable interactions with the ACP. Source data underlying Fig. 4c are provided as a Source Data file.
