Fig. 2.

Individual preferences in the S1 pocket of LTA4H toward unnatural amino acid substrates compared to the best natural amino acid conjugate, l-Arg. Enzyme activity was monitored using an fmax multi-well fluorescence plate reader (molecular devices) at excitation wavelength of 355 nm and an emission wavelength of 460 nm. The x-axis represents the abbreviated amino acid names. The y-axis represents the average relative activity expressed as a percent of the best amino acid. All structures and information about fluorogenic substrates are in Online Resource 1