Fig. 4: Changes caused by F208G mutation.

a Relative activity of ItuAL_WT or ItuAL_F208G using each substrate. The activity of each enzyme using C10 as a substrate was defined as 100%. Values and error bars represent the mean and standard deviation, respectively, of three independent experiments. b Relative activity of ItuAL_F208G using each substrate. The activity of ItuAL_WT using the same substrate as that for ItuAL_F208G was defined as 100%. Values and error bars represent the mean and standard deviation, respectively, of three independent experiments. c, d Amino acid residues around the substrate-binding pocket in the predicted structures of ItuAL_WT (c) and ItuAL_F208G (d). The substrate-binding pocket detected using MOLEonline⁵¹ is shown by connected grey-coloured spheres. The modelled fatty acid in the substrate-binding pocket is cyan-coloured. Amino acid residues are coloured as follows: amino acid residues indicated by green carbons are those whose side chains are involved in pocket formation. Amino acid residues indicated by pink carbons are those whose main chains are involved in pocket formation. Amino acid residues labelled in red are those that have been added to pocket formation by the F208G mutation.