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. Author manuscript; available in PMC: 2021 Dec 1.
Published in final edited form as: Nat Struct Mol Biol. 2021 Jun 10;28(6):512–520. doi: 10.1038/s41594-021-00605-6

Fig. 5. Proposed ping-pong mechanism and evidence for a covalent acyl-enzyme intermediate.

Fig. 5

a, Schematic outlining proposed ELOVL ping-pong mechanism. b-c, Intact mass analysis of ELOVL7 in presence of b, acyl-CoA substrates demonstrating transacylation to form an acyl-enzyme intermediate and c, acyl-CoA followed by malonyl-CoA. Intact mass analysis of protein only (black), protein + C18:0 acyl-CoA (blue), protein + C18:3 acyl-CoA (cyan) and protein + C18:0 acyl-CoA + malonyl-CoA (red). Peaks are indicated as follows: protein (green icon), acyl enzyme intermediate (green icon + pink/red oblong), background species present in all traces (grey circles). (n=2 biological repeats, see Supplementary Figures 1-2 for replicate traces; Supplementary Table 2 for experimental and theoretical masses and mass errors).