The function of β‐N‐acetyl‐D‐glucosaminyl monophosphorylundecaprenol in biosynthesis of lipoteichoic acids in a group of Bacillus strains

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Abstract
Membrane preparations, obtained from Bacillus strains which have N‐acetylglucosamine‐linked lipoteichoic acids in their membranes, were shown to catalyze the transfer of N‐[14C]acetylglucosamine (GlcNAc) from β‐[14C]GlcNAc‐P‐undecaprenol to endogenous polymer. In this reaction, α‐GlcNAc‐P‐undecaprenol or α‐GlcNAc‐PP‐undecaprenol could not substitute for β‐GlcNAc‐P‐undecaprenol as the N‐acetylglucosamine donor. This enzyme was most active at pH 6.0 and in the presence of 40 mM MgCl2. The apparent Km for β‐GlcNAc‐P‐undecaprenol was 2 μM. The radioactive polymer products, solubilized by hot phenol treatment, coincided with lipoteichoic acids in chromatographic behavior. Hydrogen fluoride treatment of the polymer products gave a major fragment identical with GlcNAc(α→2)glycerol, which corresponded to the dephosphorylated repeating units of the lipoteichoic acids in the examined strains. Thus it is concluded that β‐GlcNAc‐P‐undecaprenol serves as the donor of N‐acetylglucosamine in the biosynthesis of lipoteichoic acids in a group of Bacillus strains.