Abstract
A convenient synthesis of UDP- N-acetylmuramic acid, a key compound for the study of the cytoplasmic synthetases of bacterial peptidoglycan, is described. Separation of its two anomers was carried out by HPLC. The α anomer is identical with natural UDP- N-acetylmuramic acid. Both anomers are substrates for the l-alanine-adding enzyme from Escherichia coli with K m values of 0.13 mM (α) and 2 mM (β).
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