Fig. 5: Discovery of GlAT as a bifunctional acetyltransferase on C15 and C22. | Cell Discovery

Fig. 5: Discovery of GlAT as a bifunctional acetyltransferase on C15 and C22.

From: Decoding and reprogramming of the biosynthetic networks of mushroom-derived bioactive type II ganoderic acids in yeast

Fig. 5

a The extracts from the in vitro enzymatic assay of GlAT-containing microsomes with GA-T2 (left), and the enlarged view as highlighted in the black dotted line frame in the middle (right). CK indicates microsomes prepared from the control strain YL-T3-CK-r. b GA-T2 is docked into the T-tunnel of GlAT (shown by surface) at the C22 pose (slate) and C15 pose (cyan), respectively. c The percentage and represented structure at PRSs for the C15 and C22 poses, respectively. H305 and Acyl-CoA are represented by green sticks. GA-T2 in the C15 pose and C22 pose is represented by cyan and slate sticks, respectively. d The concentration (indicated as mg/L or mAU·s) of different substrates (indicated as light blue column) and products after 3 h incubation of strains BJ5464-GlAT-r (WT), BJ5464-A211L-r (A211L), BJ5464-A211F-r (A211F), BJ5464-G208L-r (G208L), BJ5464-R218L-r (R218L), BJ5464-S79L-r (S79L), and BJ5464-H305A-r (H305A) with respective substrates.

Back to article page