engleski

Comparative susceptibility of a peptidoglycan monomer from Brevibacterium divaricatum and its anhydromuramyl analogue to hydrolysis with N-acetylmuramyl-L-alanine amidase

Peptidoglycan monomer GlcNAc-MurNAc-L-Ala-D-isoGln-mesoDpm-D-Ala-D-Ala from Brevibacterium divaricatum is composed of the disaccharide pepntapeptide containing muramic acid with a reducing end (ca. 90-95%) and of the anhydromuramyl analogue (anhydromuramyl-PGM ; ca. 5-10%) according to the analysis by HPLC and FAB-MS. The two peptidoglycan analogues can not be separated by simple physico-chemical procedures. The enzyme N-acetylmuramyl-L-alanine amidase cleaves the bond between N-acetylmuramic acid and L-alanine in the PGM molecule. It is shown that anhydromuramyl-PGM is also the substrate for this amidase. In a preparation containing both analogues the amidase hydrolyses preferantially PGM rather than anhydromuramyl-PGM.

peptidoglycan monomer ; anhydromuramyl analogue ; N-acetylmuramyl-L-alanine amidase ; FAB-MS ; HPLC

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