Godert Amy M, Jin Mi, McLafferty Fred W, Begley Tadhg P
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
J Bacteriol. 2007 Apr;189(7):2941-4. doi: 10.1128/JB.01200-06. Epub 2007 Jan 5.
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.
来自荧光假单胞菌ATCC 17400的硫喹诺洛菌素铁载体利用了硫胺素和钼蝶呤生物合成中发现的硫转移化学的变体。一种具有JAMM基序的蛋白质切割小硫载体蛋白上双甘氨酸部分后的C末端氨基酸残基,修饰后的C末端被激活并硫酰化,形成硫代羧酸盐。