Functions Of Alkaline Phosphatase

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In this series of experiments the productivity and function of the enzyme Alkaline Phosphatase will be examined. Alkaline Phosphatase is an enzyme commonly produced and found throughout the entire human body. Its main function is the cleaving of phosphate groups from mostly organic molecules, including proteins, nucleotides and even alkaloids, which makes it a hydrolase enzyme (Ellis, 2016). In biochemistry, a hydrolase enzyme is an enzyme that speeds up the hydrolysis of complex biomolecules like proteins, starch and fats (Horak, 2014).
The addition and elimination of phosphate groups is an important process in biochemistry, as many enzymes are catalysed or have their activity controlled by this process. Even more important than this process,
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One of these parameters is Temperature. Normally an increase in temperature will lead to an increase in the rate of a chemical reaction, but the reaction rate will decline after it passes the optimum temperature, meaning the temperature at which the activity of the enzyme and the rate of the reaction is the highest. Any temperature higher than optimal will chance denaturing (loss of biological function) the enzyme and lowering the reaction rate. Alkaline Phosphatase is an enzyme found in the human body and as such is expected to function best at a normal human body temperature of 37⁰C.
Another parameter to take into consideration is pH. The optimum pH of an enzyme is the value at which the reaction rate and the activity of the enzyme is highest. Again, an increase in one parameter will increase the reaction rate. Increasing the pH increases the rate of the reaction, right up until the optimum pH, after this point, the enzyme will be denatured and the reaction rate will decline. Alkaline Phosphatase has an optimum alkaline pH, as the name suggests. An alkaline pH is defined as a pH greater than
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According to the Michaelis-Menten model, an enzyme-substrate complex (ES) is formed when an enzyme (E) binds to a substrate (S). After the ES has formed it can then be utilized to form the required product. When the degree of an enzymatic reaction is measured it is done so at different substrate concentrations (the degree of an enzymatic reaction is also known as the velocity). This is an indication that the rate of the reaction largely hinges on the concentration of the substrate. When the substrate level is low, the reaction is in the first order, meaning that the substrate concentration can influence the velocity. When the level of the substrate in the reaction is higher, the order of the reaction will be zero, meaning that the velocity is not influenced by the concentration of the substrate. This happens because all the active sites on the enzyme are saturated with substrate

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