Fig. 4

Validating the broad applicability of the transmembrane domain truncation (ΔTM) on four additional CYP79 enzymes with distinct substrate specificities and different plant origin. We expressed native and ΔTM variants of SbCYP79A1 (Sorghum bicolor, tyrosine-specific), MeCYP79D2 (Manihot esculenta, valine- and isoleucine-specific), AtCYP79B2 (Arabidopsis thaliana, tryptophan-specific) and BvCYP79F6 (Barbarea vulgaris, homophenylalanine (HPhe)-specific), together with CYP83s, ATR1 and GSTF11. Native and truncated CYP83B1 was paired with SbCYP79A1, MeCYP79D2 and AtCYP79B2, whereas CYP83A1 was co-expressed with BvCYP79F6. We measured the generation of putative glutathione conjugates derived from the respective amino acids by Q-TOF LC-MS/MS. The presented extracted ion chromatograms are representative of 4 biological replicates and the characteristic fragmentation patters for each glutathione conjugate are shown in Fig S6