Biosynthesis of the thioquinolobactin siderophore: An interesting variation on sulfur transfer
Biosynthesis of the thioquinolobactin siderophore: An interesting variation on sulfur transfer
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DOI：
10.1128/jb.01200-06
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发表时间：
2007-04-01
影响因子：
3.2
通讯作者：
Begley, Tadhg P.
中科院分区：
文献类型：
--
作者：
Godert, Amy M.;Jin, Mi;Begley, Tadhg P.
荧光假单胞菌ATCC 17400的硫代喹啉铁载体利用硫胺素和除草剂生物合成中硫转移化学的变化。JAMM基序蛋白在一个小的硫载体蛋白上切割二甘氨酸部分之后的C-末端氨基酸残基，修饰的C末端被激活和硫化，形成硫代羧酸盐。
The thioquinolobactin siderophore from Pseudomonas fluorescens ATCC 17400 utilizes a variation of the sulfur transfer chemistry found in thiamine and molydobterin biosynthesis. A JAMM motif protein cleaves the C-terminal amino acid residues following a diglycine moiety on a small sulfur carrier protein, and the modified C terminus is activated and sulfurylated, forming a thiocarboxylate.