A three dimensional model of the digestion of peptidoglycan by lysozyme.
The digestion of single peptidoglycan chains of the recently proposed conformation (Formanek et al., 1974) can be described with the same enzymatic mechanism as proposed by Phillips for a hexasaccharide consisting of alternating N-acetylglucosamine, N-acetylmuramic acid residues (Phillips, 1966). It is shown by model building, that in a peptidoglycan lysozyme complex the peptide chains do not exhibit any sterical hindrance. The digestion of the peptidoglycan sacculus by lysozyme may occur at latice defects of its paracrystalline structure. A slit of about 30 A length and 10--15 A width between peptidoglycan micells may be sufficient for the attachment of lysozyme.
D000117:Acetylglucosamine; D002686:Chitin; D006020:Glycopeptides / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D009112:Muramic Acids; D009113:Muramidase / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*; D011487:Protein Conformation
D006020:Glycopeptides; D009112:Muramic Acids; D010457:Peptidoglycan; D002686:Chitin; D009113:Muramidase; D000117:Acetylglucosamine