Sikora Alison L, Cahill Sean M, Blanchard John S
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Biochemistry. 2009 Nov 24;48(46):10827-9. doi: 10.1021/bi901680m.
The EntE enzyme, involved in the synthesis of the iron siderophore enterobactin, catalyzes the adenylation of 2,3-dihydroxybenzoic acid, followed by its transfer to the phosphopantetheine arm of holo-EntB, an aryl carrier protein. In the absence of EntB, EntE catalyzes the formation of Ap(4)A, a molecule that is implicated in regulating cell division during oxidative stress. We propose that the expression of EntE during iron starvation produces Ap(4)A to slow growth until intracellular iron stores can be restored.
参与铁载体肠杆菌素合成的EntE酶催化2,3 - 二羟基苯甲酸的腺苷化反应，随后将其转移至全酶EntB（一种芳基载体蛋白）的磷酸泛酰巯基乙胺臂上。在没有EntB的情况下，EntE催化形成Ap(4)A，该分子与氧化应激期间的细胞分裂调节有关。我们推测，在铁饥饿期间EntE的表达会产生Ap(4)A以减缓生长，直到细胞内铁储备得以恢复。
