Phosphatases are enzymes capable of catalysing the hydrolysis of phosphoric esters with liberation 'of inorganic phosphate, they are found widely spread throughout nature. The early work on the discovery and properties of these enzymes has been thoroughly reviewed by Kay (1932). There are probably many different phosphatases present in living organisms and much valuable data is being accumulated on their identity and methods of differential estimation. In the present state of our knowledge, however, and from the aspect of clinical application, we can best think of them in terms of two groups, the so- called' alkaline ' and' acid' phosphatases. These enzymes are distinguished by the fact that the first class are optimally active at an alkaline and the second at an acid pH. The actual pH varies with the particular substrate, but when phenyl phosphate is used, the acid phosphatases have an optimum pH of 4.9 and the alkaline phosphatases are optimally active at pH 9.8. Since these pH values are sufficiently far apart, it is possible to determine one of the two groups of phosphatase in the presence of the other.
I think the major difference is in the pH range at which their activity is optimum. Acid phosphatases are mostly active between pH 4.5 - 6.0 while alkaline phosphatases are active optimally between pH 9 - 11
thank you for your replays. I determined each alkaline and acid phosphatase in soil that inoculated with phosphate solubilizng bacteria. which of these two enzymes can i use in my discussion?
The description given by Valentina applies mostly at animal phosphatases. In other organisms such as plants and fungi, acid phosphatases tend to predominate, and alkaline phosphatases are rare. Nevertheless, even acid phosphatases are a widly diverse group of proteins, as the activity seem to have evolved idependently in a number of proteins families, so you may find purple acid phosphatases (Tran HT , Hurley BA , & Plaxton WC (2010) Feeding hungry plants: The role of purple acid phosphatases in phosphate nutrition. Plant Science 179(1--2):14 - 27), HAD phosphatases (Baldwin JC , Karthikeyan AS , Cao A , & Raghothama KG (2008) Biochemical and molecular analysis of LePS2;1: a phosphate starvation induced protein phosphatase gene from tomato. Planta 228(2):273-80), and specific phosphatases such as glucose-6-phosphatase, fluctose-1,6-biphosphatase, sucrose-P phosphatase, thehalose-P phosphatase, Nucleotide phosphoanhidride hydrolases (NUDIX) and so on.
Bacterial phosphatases are at least as diverse al plant phosphatases, but most likely they are even more diverse.
If you have no idea what kind of protein is being excreted to the soil, and all you know about it is the enzymatica activity, you may have to purify the protein or enrich the sample using fractionation and chromatography, and then with the help of proteomic techniques you may be able to identify the protein in question.
The difference between the two groups of enzymes is also reflected in their substrate specificity. Alkaline phosphatase will hydrolyse Ssubstituted monoesters of phosphorothioic acid (R-SP03H2) and not O-substituted monoesters of phosphorothioic acid (R-OPOjH2 and the reverse applies to acid phosphatase. Another major distinction lies in the activation by Mg2+ and inhibition by metal chelating agents of alkaline phosphatase and not acid phosphatase.
The acid phosphatase is produced in prostate, while alkaline phosphatase is produced in liver/gall ducts, in osteoblasts and placenta. For a couple of decades it was used for the diagnostics and follow up of prostate carcinoma, but that is now the much more reliable PSA