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Aconitase

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Aconitase (ACO) is an enzymatic domain that confers the ability to catalyse the equilibrium

citrate = aconitate + H2O = L-isocitrate

This reaction is part of the citrate (TCA-, Krebs-)cycle.

In most organims, there is a cytosolic enzyme with an ACO domain (cAc), and in eukaryotes, a second copy of it was introduced with mitochondria (mAc). Plants developed even more copies in mitochondria.

Catalytic mechanism of mitochondrial ACO

Mitochondrial aconitase from pig, PDB 7acn.

Drag the structure with the mouse to rotate
The bulk of citrate cycle processing happens in mitochondria and so, studies concentrated on . The by three sulfur atoms belonging to the cysteins-385, -448, and -451.


Cytosolic aconitase and its other function

Cytosolic aconitase from rabbit (bound to RNA) and human (with Fe4S4 cluster), from PDB 2ipy and 2b3x.

Drag the structure with the mouse to rotate
A specialty of cAc is that in mammals it has developed a as inhibitor of that carry an . Therefore, the cytosolic cAc is named IREBP for IRE-binding protein when this function is talked about. Only one of the two functions is active, depending on whether is present in the molecule: it's essential for . You can see, by , how much the enzyme structure differs between those two functions.

Weblinks

Retrieved from "http://52.214.119.220/wiki/index.php/Aconitase"
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