Feedback inhibition, is a correct answer. Feedback inhibition is a regulation where the product in excess will bind to the allosteric site of the enzyme. This regulation will prevent the depletion of the substrate by inhibiting the enzyme from breaking down too many substrates into products. If our body is lacked of the product involves in feedback inhibition, the product bind to the allosteric site will fall off from the enzyme and be used for our body. The enzyme can now be used to catalyze the reaction (Citovsky, Lecture 7). This regulation is an allosteric regulation since the allosteric site will be occupied with …show more content…
Kinases are enzymes that transfer the gamma phosphate of ATP on hydroxyl group of substrates. The addition of phosphate to hydroxyl group is known as phosphorylation. Phosphorylation is a common reaction for a lot of cellular processes. However, atypical phosphorylation will lead to several severe disorder such as cancer and inflammatory diseases. (Fabbro et al., pg. 172). Therefore, small molecule kinase inhibitors(SMKIs) are being studied and developed in drug discovery especially for the treatment of cancers. A total 28 SMKIs that are approved by FDA available on the market on October 2015. Among the other kinases, serine/threonine kinases MEK and Akt have been researched and investigated the most (Wu et al., pg. 60). Mitogen-activated protein kinase kinase(MAPKK) composed of a lot the members. MEK is one of the members. It is a major component in the Raf-Ras-MEK signaling pathway which plays an important role in gene expression regulation (Wu et al., pg. 60; McCubrey et al., pg. 1264). Currently, the clinical trials of treatment of lung cancer are using allosteric MEK inhibitors. (Wu et al., pg. 60). The serine/threonine kinase Akt involves in numerous biological activities such as cell proliferation, survival and migration. However, development of Akt inhibitor is not as advanced as MEK inhibitors due to different challenges (Wu et al., pg. 62). Based on