The pyruvate dehydrogenase complex is subject to allosteric control, especially inhibition by reaction products. From the list b
elow, select the main regulatory processes controlling pyruvate dehydrogenase's activity in eukaryotes. a. AMP binding to and activating the enzyme.
b. Phosphorylation by a kinase using ATP (which turns the complex off) and dephosphorylation by a phosphatase (which turns the complex on).
c. Exchange of ADP and ATP on the pyruvate dehydrogenase complex.
d. Phosphorylation by a kinase using ATP (which turns the complex on) and dephosphorylation by a phosphatase (which tums the complex off).
b. Phosphorylation by a kinase using ATP (which turns the complex off) and dephosphorylation by a phosphatase (which turns the complex on).
Explanation:
The pyruvate dehydrogenase complex is described as a complex having many enzymes that catalyse decarboxylation of pyruvate by oxidation to yield NADH and acetyl‐CoA, which makes the influx of acetyl-coA from glycolysis to increase into the Krebs cycle.
It can be found in the mitochondrial matrix and pyruvate which is conveyed through enzyme Pyruvate Translocase to PDH complex.
Regulation of pyruvate dehydrogenase complex occured through allosteric effectors as well as phosphorylation.the main regulatory processes controlling pyruvate dehydrogenase's activity in eukaryotes such as plants and animals Phosphorylation is by a kinase using ATP which first turns the complex off and the later dephosphorylation by a phosphatase which turns the complex on
