The influence of metal ions on the orthophosphatase and inorganic pyrophosphatase activities of human alkaline phosphatase.
1. The differential effects of adding Zn(2+) and Mg(2+) on the orthophosphatase and inorganic pyrophosphatase activities of human intestinal alkaline phosphatase were studied. 2. In the presence of excess of Zn(2+), inorganic pyrophosphatase activity is inhibited. At higher concentrations of pyrophosphate, hydrolysis of this substrate takes place, but is inhibited competitively by the Zn(2+)-pyrophosphate complex. This complex also acts as a competitive inhibitor of orthophosphate hydrolysis. 3. Excess of Mg(2+) also inhibits pyrophosphatase action by removal of substrate; at low concentrations, this ion activates pyrophosphatase, as is the case with orthophosphatase. 4. It is concluded that, when interactions between metal ions and pyrophosphate are taken into account, the effects of these ions are consistent with the view that alkaline phosphatases possess both orthophosphatase and inorganic pyrophosphatase activities.
D000469:Alkaline Phosphatase; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D011756:Diphosphates; D006801:Humans; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors; D011755:Pyrophosphatases / Q000037:antagonists & inhibitors; D015032:Zinc
D011756:Diphosphates; D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; D011755:Pyrophosphatases; D008274:Magnesium; D015032:Zinc