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<i>Escherichia coli</i> strains have been modified in a variety of ways to enhance the production of different recombinant proteins, targeting membrane protein expression, proteins with disulphide bonds, and more recently, proteins which require <i>N</i>-linked glycosylation. The addition of glycans to proteins remains a relatively inefficient process and here we aimed to combine genetic modifications within central carbon metabolic pathways in order to increase glycan precursor pools, prior to transfer onto polypeptide backbones. Using a lectin screen that detects cell surface representation of glycans, together with Western blot analyses using an <i>O</i>-antigen ligase mutant strain, the enhanced uptake and phosphorylation of sugars (<i>ptsA</i>) from the media combined with conservation of carbon through the glyoxylate shunt (<i>icl</i>) improved glycosylation efficiency of a bacterial protein AcrA by 69% and over 100% in an engineered human protein IFN-&#945;2b. Unexpectedly, overexpression of a gene involved in the production of DXP from pyruvate (<i>dxs</i>), which was previously seen to have a positive impact on glycosylation, was detrimental to process efficiency and the possible reasons for this are discussed.