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棒状杆菌含苏氨酸胞壁质的氨基酸序列。

Amino acid sequence of the threonine-containing mureins of coryneform bacteria.

作者信息

Fiedler F, Schleifer K, Kandler O

出版信息

J Bacteriol. 1973 Jan;113(1):8-17. doi: 10.1128/jb.113.1.8-17.1973.

DOI:10.1128/jb.113.1.8-17.1973
PMID:4683671
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC251595/
Abstract

In a study of the mureins of coryneform bacteria (Arthrobacter, Brevibacterium, Cellulomonas, Corynebacterium, Erysipelothrix), 21 threonine-containing strains were found. In several of the strains the amino acid and amino sugar composition of the murein was muramic acid (Mur), glucosamine (GlcNH(2)), d-Glu, l-Lys, l-Thr, and Ala in a molar ratio of 1:1:1:1:1:4 or 5, and in several other strains it was Mur, GlcNH(2), d-Glu, l-Lys, l-Thr, Ala, and l-Ser in a molar ratio of 1:1:1:1:1:3:1. The amino acid sequence of the mureins was determined by analyzing the oligopeptides derived from partial acid hydrolysates. It was shown that there were five different murein types. The peptide subunits attached to the muramic acid are the same, namely l-Ala-d-GluNH(2)-l-Lys-d-Ala. In one strain, the alpha-carboxyl group of d-Glu is substituted by d-alanine amide. The interpeptide bridges of the different types consist of the peptides l-Ala-l-Thr-l-Ala, l-Ala-l-Thr, l-Ala-l-Ala-l-Thr, l-Ala-l-Ala-l-Ala-l-Thr, or l-Ala-l-Thr-l-Ser which are bound through their C-termini (l-Ala, l-Thr, l-Ser) to the epsilon-amino group of l-Lys of one peptide subunit and by their N-termini (l-Ala) to the C-terminal d-Ala of an adjacent peptide subunit. Determination of the N- and C-terminal groups in the mureins showed that about 15 to 30% of the interpeptide bridges are not cross-linked.

摘要

在一项针对棒状杆菌(节杆菌、短杆菌、纤维单胞菌、棒杆菌、丹毒丝菌)胞壁质的研究中,发现了21株含苏氨酸的菌株。在其中几株菌株中,胞壁质的氨基酸和氨基糖组成为 Mur、GlcNH₂、d - Glu、l - Lys、l - Thr 和 Ala,摩尔比为 1:1:1:1:1:4 或 5;在其他几株菌株中,其组成为 Mur、GlcNH₂、d - Glu、l - Lys、l - Thr、Ala 和 l - Ser,摩尔比为 1:1:1:1:1:3:1。通过分析部分酸水解产物衍生的寡肽来确定胞壁质的氨基酸序列。结果表明存在五种不同类型的胞壁质。连接到 Mur 酸上的肽亚基是相同的,即 l - Ala - d - GluNH₂ - l - Lys - d - Ala。在一个菌株中,d - Glu 的α - 羧基被 d - 丙氨酸酰胺取代。不同类型的肽间桥由肽 l - Ala - l - Thr - l - Ala、l - Ala - l - Thr、l - Ala - l - Ala - l - Thr、l - Ala - l - Ala - l - Ala - l - Thr 或 l - Ala - l - Thr - l - Ser 组成,它们通过其 C 末端(l - Ala、l - Thr、l - Ser)与一个肽亚基的 l - Lys 的ε - 氨基相连,并通过其 N 末端(l - Ala)与相邻肽亚基的 C 末端 d - Ala 相连。对胞壁质中 N 末端和 C 末端基团的测定表明,约15%至30%的肽间桥未交联。

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