Extended Data Fig. 2: GglsA containing the A domain of E. coli EntF catalyzes the synthesis of the serine-glucolipid.
From: Biosurfactant biosynthesis by Alcanivorax borkumensis and its role in oil biodegradation
a, The GglsA protein carrying the A domain of the E. coli EntF protein (GglsA-EntFA) was expressed in E. coli, and lipids measured by LC-MS/MS. The MS/MS spectrum displays the parental mass at 803.5788 m/z indicative for the aglycone H(O-10:0)4Ser which differs from the aglycone of the glycine-glucolipid H(O-10:0)4Gly (773.5905 m/z) (Fig. 1c) by 29.9883 m/z equivalent to one HC-OH unit (difference between Ser/Gly). The same mass difference was observed between the fragment peak of H(O-10:0)4Ser (106.0436 m/z) and H(O-10:0)4Gly (76.0386 m/z). The structure of the serine-containing aglycone on the right shows the calculated masses. b, The chimeric GglsA-EntFA protein containing the A domain of E. coli EntF catalyzes the synthesis of the aglycone H(O-10:0)4Ser carrying a serine moiety instead of glycine.
