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The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is an oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer.
N-Acetylmuramic acid (NAM or MurNAc) is an organic compound with the chemical formula C 11 H 19 NO 8. It is a monomer of peptidoglycan in most bacterial cell walls, which is built from alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid, cross-linked by oligopeptides at the lactic acid residue of MurNAc.
It is the main component of the radulas of mollusks, the beaks of cephalopods, and a major component of the cell walls of most fungi. Polymerized with glucuronic acid , it forms hyaluronan . GlcNAc has been reported to be an inhibitor of elastase release from human polymorphonuclear leukocytes (range 8–17% inhibition), however this is much ...
Peptidoglycan is made up of a polysaccharide backbone consisting of alternating N-Acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) residues in equal amounts. Peptidoglycan is responsible for the rigidity of the bacterial cell wall, and for the determination of cell shape. It is relatively porous and is not considered to be a permeability ...
N-Acetylglutamic acid is an extracellular metabolite isolated from the prokaryote Rhizobium trifolii that was characterized using many structure determination techniques such as proton nuclear magnetic resonance (1 H NMR) spectroscopy, Fourier-transform infrared spectroscopy, and gas chromatography-mass spectrometry.
A simplified reaction mechanism for N-acetylglutamate synthase (NAGS). Two mechanisms for N-acetyltransferase function have been proposed: a two-step, ping-pong mechanism involving transfer of the relevant acetyl group to an activated cysteine residue [10] and a one-step mechanism through direct attack of the amino nitrogen on the carbonyl group. [11]
PBPs normally catalyze the cross-linking of the bacterial cell wall, but they can be permanently inhibited by penicillin and other β-lactam antibiotics. (NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine) [2] Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin.
The basic components are N-acetylglucosamine and N-acetyltalosaminuronic acid (bacterial peptidoglycan containing N-acetylmuramic acid instead), which are linked by β-1,3-glycosidic bonds. [ 3 ] Lysozyme , a host defense mechanism present in human secretions (e.g. saliva and tears) breaks β-1,4-glycosidic bonds to degrade peptidoglycan.