Magnesium ions phosphate ester hydrolysis

Reactions involving the formation and hydrolysis of phosphate and polyphosphate esters are of vital importance in biological systems in which it is found that magnesium ions are almost invariably implicated. The formation and decomposition of adenosine triphosphate are the fundamental reactions involved in energy storage in living systems. In this context, it is perhaps relevant to note that the hydrolysis of ATP is enhanced, albeit in a very modest manner, by some cobalt(m) complexes. 

Metalloenzyme-catalyzed phosphoric ester hydrolysis can be illustrated by alkaline phosphatase, by far the most-investigated enzyme of this class. The protein is a dimer of 94 kDa containing two zinc(II) and one magnesium(II) ions per monomer, and catalyzes, rather unspecifically, the hydrolysis of a variety of phosphate monoesters as well as transphosphorylation reactions. The x-ray structure at 2.8 A resolution obtained on a derivative in which all the native metal ions were replaced by cadmium(II) reveals three metals in each subunit. 

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