draw 3 allosteric enzyme curves for alpha ketoglutarate dehydrogenase in the presence of high AMP, high succinylCoA, and no regulators on 1 graphdraw 3 allosteric enzyme curves for alpha ketoglutarate dehydrogenase in the presence of high AMP, high succinylCoA, and no regulators on 1 graph

Regulations and the Role of Regulators in Allosteric Enzyme Curves for Alpha-ketoglutarate Dehydrogenase

Alpha-ketoglutarate hydrogenase, also known as?-KGDH (or?-KGDH), is an enzyme which is part of the citric acid cycle. This enzyme is regulated by various means. The allosteric enzyme curves for?-KGDH may be affected by high levels of succinyl coenzyme (SuccinylCoA) and high adenosine monophosphate. Research has shown that if there is no external regulator, the activity of?–KGDH’s allosteric enzymes will increase as substrate concentrations rise (Kubota et al. 2018, 2018). This phenomenon is called the positive cooperativity and is due to the formation of an enzyme-substrate combination and an increased enzyme affinity for the substrate. (Klussmann and al., 2017). The allosteric enzyme curves may be altered if regulators are present. In the presence of AMP, for example, the activity of?-KGDH can decrease as substrate concentrations increase (Kubota et al. 2020).