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To determine kinetics, we analyze an enzyme’s activity – the number of reactions it manages over time.
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ACE inhibitors) are specific enzyme inhibitors. Inhibitors reduce activity by either blocking the interaction between the enzyme and substrate or altering the substrate’s transformation rate. The exceptions to this are enzymes found within thermophilic bacteria, which operate maximally at a higher temperature.Īn enzyme’s kinetics can also be controlled by inhibitors. Enzymes also have optimal temperatures, and their rates accelerate as temperatures increase to 50☌, but decrease abruptly as the enzyme denatures around 55-60☌. Enzymes function at an optimal pH when the environmental pH is different, the enzyme loses structural stability and its reaction rate decreases. The reaction rate also depends on the environment. These cofactors can be metals, like zinc or iron, or organic coenzymes (e.g. Furthermore, many enzymes need small molecule cofactors to do part of their reactions. In the first place, most enzymes are tightly regulated: they won’t be active or synthesized until needed. Now it gets complicated… What Affects an Enzyme’s Kinetics?
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By understanding how an enzyme’s behavior is affected, you can figure out how it functions in physiology or fails to function in disease. Enzyme kinetics is the rate of that transformation. As biological catalysts, enzymes transform target substrates into products.
![Enzyme software kinetics](https://kumkoniak.com/43.jpg)