An UDP-activated murein precursor was isolated from Butyribacterium rettgeri after one hour inhibition by D-cycloserine. The compound contains UDP, muramic acid, L-serine, D-glutamic acid and L-ornithine in equimolar amounts. The amino acid sequence of the tripeptide attached to muramic acid is L-Ser-D-Glu-L-Orn as determined by end group analysis and identification of peptides obtained after partial hydrolysis. As shown by the identification of glutamic acid -γ-hydrazid after hydrazinolysis of the compound, ornithine is bound by its α-amino group to the γ-carboxyl group of glutamic acid. The amino acid sequence of the precursor is in agreement with the structure of the corresponding part of the whole murein of Butyribacterium rettgeri, as proposed recently.
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Miller et al. (1968) studied this question.