| Literature DB >> 597567 |
Abstract
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.Entities:
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Year: 1977 PMID: 597567 DOI: 10.1007/bf00538836
Source DB: PubMed Journal: Biophys Struct Mech ISSN: 0340-1057