Disease relevance of N-acetylmuramic acid

• In a previous communication (J. Biol. Chem. (1975) 250, 1676-1682), methods were described for the purification of the N-acetylmuramic acid L-alanine amidase from Bacillus subtilis ATCC 6051 and of a modifier protein which combines stoichiometrically with the enzyme and stimulates the activity approximately 3-fold [1].
• Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase" [2].
• We found that two signatures of Gram-negative PG, the presence of diaminopimelic acid in the peptide bridge and a 1,6-anhydro form of N-acetylmuramic acid in the glycan chain, allow discrimination between Gram-negative and Gram-positive bacteria [3].
• Dependence of proliferation of Bacteroides forsythus on exogenous N-acetylmuramic acid [4].
• Neisseria gonorrhoeae acetylates its cell wall peptidoglycan (PG) at the C-6 position on N-acetylmuramic acid [5].

High impact information on N-acetylmuramic acid

• Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers [1].
• Bacillus subtilis N-acetylmuramic acid L-alanine amidase [6].
• The N-acetylmuramoyl-l-alanine amidases of Escherichia coli (AmiA, B and C) are periplasmic enzymes that remove murein cross-links by cleaving the peptide moiety from N-acetylmuramic acid [7].
• Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D [8].
• It has properties similar to those of basic class I chitinases with lysozyme activity, such as cleavage specificity at the C-1 of N-acetylmuramic acid with inversion of configuration, but as it lacks an N-terminal hevein domain, it should be classified as a class II chitinase [9].

Chemical compound and disease context of N-acetylmuramic acid

• Endolysin from the phage Cp-1 (Cpl-1) cleaves the glycosidic beta1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the pneumococcal cell wall [10].

Biological context of N-acetylmuramic acid

• Bacteroides forsythus is the first wild-type or mutant bacterium found to require exogenous N-acetylmuramic acid for proliferation and maintenance of cell shape [4].
• Muropeptides generated by Acd hydrolysis demonstrated that Acd hydrolyses peptidoglycan bonds between N-acetylglucosamine and N-acetylmuramic acid, confirming that Acd is an N-acetylglucosaminidase [11].
• Murein biosynthesis and O-acetylation of N-acetylmuramic acid during the cell-division cycle of Proteus mirabilis [12].

Associations of N-acetylmuramic acid with other chemical compounds

• Also known as murein, the cell wall is a two-dimensional polymer, consisting of a linear, repeating N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) motif, cross-linked via peptides appended to MurNAc [13].
• Lytic transglycosylases cleave the beta-(1-->4)-glycosidic bond in the bacterial cell wall heteropolymer peptidoglycan between the N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues with the concomitant formation of a 1,6-anhydromuramoyl residue [14].
• This enzyme has a different specificity than egg white lysozyme and cleaves the beta 1 leads to 4 glycosidic linkage between N-acetylglucosamine and N-acetylmuramic acid in gonococcal peptidoglycan [15].

Gene context of N-acetylmuramic acid

• Structure of the O-specific polysaccharide of Providencia alcalifaciens O16 containing N-acetylmuramic acid [16].

References