Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species
作者:Julia M. Gauglitz、Alison Butler
DOI:10.1007/s00775-013-0995-3
日期:2013.6
In response to iron-depleted aerobic conditions, bacteria often secrete low molecular weight, high-affinity iron(III)-complexing ligands, siderophores, to solubilize and sequester iron(III). Many marine siderophores are amphiphilic and are produced in suites, wherein each member within a particular suite has the same iron(III)-binding polar head group which is appended by one or two fatty acids of
为了响应缺铁的需氧条件,细菌通常会分泌低分子量、高亲和力的铁 (III) 络合配体、铁载体,以溶解和螯合铁 (III)。许多海洋铁载体是两亲性的,并且是成组产生的,其中特定组内的每个成员都具有相同的结合铁 (III) 的极性头基,该头基附加有一个或两个不同长度、不饱和度和不饱和度的脂肪酸羟基化,建立套件组成。我们报告了一组来自海洋细菌分离菌弧菌的铁载体的分离和结构表征。Nt1。根据结构分析,这套铁载体,moanachelins,是两亲性的,由两个 N-乙酰基-N-羟基-D-鸟氨酸、一个 N-乙酰基-N-羟基-L-鸟氨酸、以及甘氨酸或 L-丙氨酸,附加有各种饱和和不饱和脂肪酸尾部。小侧链氨基酸的变异是单个细菌产生的一组铁载体的肽头基结构中第一次发生变异。