Severin A I, Kokeguchi S, Kato K
Department of Microbiology, Okayama University Dental School, Japan.
Arch Microbiol. 1989;151(4):353-8. doi: 10.1007/BF00406564.
The structure of Eubacterium nodatum cell wall peptidoglycan was investigated. The peptide subunit of E. nodatum peptidoglycan has the following structure: L-Ala-D-Glu (Gly)-L-Orn-D-Ala. The carboxyl group of alanine occupying position 4 is attached to the delta-amino group of ornithine of an other subunit by the cross-linking bridge L-Ala-L-Ala-L-Orn. All glycine molecules are connected with the alpha-carboxyl group of glutamic acid with the ratio being 0.5-1. The hydrolysis of E. nodatum peptidoglycan by the S. albus G enzyme proceeds primarily due to the activity of alanyl-alanine endopeptidase, ornithyl-ornithine endopeptidase, ornithyl-alanine endopeptidase, N-acetyl-muramyl-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase.
对诺氏真杆菌细胞壁肽聚糖的结构进行了研究。诺氏真杆菌肽聚糖的肽亚基具有以下结构:L-丙氨酸-D-谷氨酸(甘氨酸)-L-鸟氨酸-D-丙氨酸。占据第4位的丙氨酸的羧基通过交联桥L-丙氨酸-L-丙氨酸-L-鸟氨酸与另一个亚基的鸟氨酸的δ-氨基相连。所有甘氨酸分子均与谷氨酸的α-羧基相连,比例为0.5-1。白色链霉菌G酶对诺氏真杆菌肽聚糖的水解主要是由于丙氨酰-丙氨酸内肽酶、鸟氨酰-鸟氨酸内肽酶、鸟氨酰-丙氨酸内肽酶、N-乙酰胞壁酰-丙氨酸酰胺酶、N-乙酰胞壁酶和N-乙酰葡糖胺酶的活性。