Formanek H
Biophys Struct Mech. 1977 Dec 27;4(1):1-14. doi: 10.1007/BF00538836.
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.
最近提出的构象(福尔曼内克等人,1974年)的单个肽聚糖链的消化,可以用菲利普斯提出的用于由交替的N - 乙酰葡糖胺、N - 乙酰胞壁酸残基组成的六糖的相同酶促机制来描述(菲利普斯,1966年)。通过模型构建表明,在肽聚糖溶菌酶复合物中,肽链不会表现出任何空间位阻。溶菌酶对肽聚糖囊的消化可能发生在其准晶体结构的晶格缺陷处。肽聚糖微胞之间约30埃长、10 - 15埃宽的缝隙可能足以让溶菌酶附着。