Extended Data Fig. 1: MBOAT-catalysed reactions and chemical structures of MBOAT substrates.

a, General reaction catalysed by MBOATs. b, Structure of CoA and acyl-CoA. The red rectangle highlights the Ppant prosthetic group within the CoA structure. For known acyl-group donors of MBOATs, the acyl groups are covalently linked with a sulfhydryl group (for example, that of Ppant in acyl-CoA or DltC-Ppant). c, Comparison of acyl-group donors and acceptors of PORCN, GOAT, DGAT1, ACAT and DltB. In the acyl-group donor column, the red dashed lines indicate the bonds that are broken during acyl-transfer reactions. In the acyl-group acceptor column, the hydroxyl groups that accept acyl groups are highlighted in red. ACAT1, ACAT2 and DGAT1 use saturated and unsaturated long-chain acyl-CoA. d, The reaction catalysed by DltB. DltB catalyses d-alanylation of both wall teichoic acid and LTA. Because the d-alanylation of wall teichoic acid is at least partially dependent on LTA d-alanylation, here we discuss only the d-alanylation of LTA. DltB transfers d-alanyl groups onto hydroxyl groups of the polyglycerolphosphate chain of the LTA molecule. For simplicity, only the type I LTA structure is shown here. The fatty-acid chains are responsible for the anchoring of LTA to the membrane of Gram-positive bacteria.