In E. coli, phoA gene is responsible in coding for AP, a homodimeric enzyme. The molecular weight of E.coli AP is approximately 94kDa; monomer subunits have an identical weight of 47kDa (3). In addition, each monomer has a polypeptide chain of 449 amino acids and a leader sequence of 21 amino acids (4). Upon arrival in the periplasm, leader sequence is cleaved and transformed the enzyme into its functional form.
AP is a homodimer as mentioned above, but it is also known as a metalloenzyme (5). Thus, it contains two active sites and has metal ions that play a key role in regulating catalytic activities and stabilizing enzyme-substrate complex. The active sites are 30Å apart from each other (7). As proposed by Gettins and Coleman using NMR studies (6), each active site of AP comprises of three metal binding sites, which acknowledged as M1, M2, and M3. Two zinc ions bind to M1 and M2 sites while a magnesium ion occupies M3. In ...
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... of alkaline phosphatase in bloodstream can be a valuable indicator to diagnose liver and bone diseases. Also, mutation in structural gene of human AP will result in hypophosphatasia, a metabolic disease that interfere with uptake of phosphorus and calcium. Thus, understanding the functions of metal ions and reaction mechanism of E. coli AP will provide a general insight of how other enzymes work and discover future potential use of AP in different areas of research or clinical medicine.
This mini-review will provide an in-depth discussion of reaction mechanism performs by E. coli alkaline phosphatase, but specifically examine the role played by magnesium ion in catalysis and structural stabilization of enzyme-substrate complex. This review will also analyze and compare numerous studies in determining which has the best estimation of the function of magnesium ion.
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