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. T
he alpha anomer is identical with natural UDP-N-acetylmuramic acid. Bo
th anomers are substrates for the L-alanine-adding enzyme from Escheri
chia coli with K-m values of 0.13mM (alpha) and 2 mM (beta).