Fig. 1From: High cell density production of multimethyl-branched long-chain esters in Escherichia coli and determination of their physicochemical propertiesMBE biosynthesis in E. coli RQ1. Overexpression of native PrpE and heterologous PCC complex from S. coelicolor leads to the production of extender unit methylmalonyl-CoA from exogenous propionate. FadD28 allows loading of free FA (FFA) onto KS domain of Mas via its conversion into acyl-AMP derivatives. To be active, Mas must be post-translationally modified by B. subtilis phosphopantetheinyl transferase Sfp. Once modified, Mas is able to elongate the acyl group loaded on its KS domain using methylmalonyl-CoA as extender unit through four iterative catalytic cycles. Finally, PapA5 catalyzes a transesterification reaction between the enzyme-linked multimethyl-branched FA and exogenous n-octanol, giving rise to MBE. Gray ovals indicate protein expression from genome insertions. White ovals indicate protein expression from plasmids. All protein-coding genes referred in this scheme are under the control of T7 promotersBack to article page