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Enzyme Catalysis And Enzyme Inhibition Essay

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Enzyme catalysis and enzyme inhibition are two essential biological mechanisms of organisms. In this experiment, WT-AP and MBP-AP enzyme are reacted with different concentrations of PNPP substrate in SpectrovVis time based assays. From the change in absorbance over time data, and the rates of the reactions are calculated, followed by the determination of the kinetic constants. Then, the MBP-AP assays are repeated with two different concentrations of phosphate inhibitor and the kinetic constants of the uninhibited enzymes are compared to those of the inhibited enzymes. Results of the experiment show that the uninhibited WT-AP and MBP-AP enzymes yielded expected kinetic constants according to a reference. However, the inhibited enzymes produced kinetics constants that did not resemble a competitive inhibition, which was expected. Instead, the inhibitor is observed to be a mixed inhibitor.

Introduction Enzymes are biological catalysts. Without them, biological reactions will not proceed in a reasonable rate. For example, without a series of digestive enzymes, it can take 20 years to digest a hamburger. Enzyme-catalyzed reactions proceed through an ES complex, in which the substrate binds to the enzyme, gets transformed into the product, and releases into the environment. For a specific enzyme, only one or a few different substrate molecules can bind in the proper manner and produce a functional ES complex. The substrate must have a size, shape, and polarity compatible with

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