PDHK1 or Pyruvate Dehydrogenase Kinase 1 is a member of the PDHK family that phosphorylate and inactivate the Pyruvate Dehydrogenase (PDH). PDH is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. PDHK1 is an important regulator of PDH in clonal beta-cells and the activity of PDHK1 and PDH are important for efficient metabolic coupling. Maintaining low PDHK1 expression/activity and keeping PDH in a dephosphorylated and active state, is important for beta-cells to achieve the metabolic flux rates necessary for maximal glucose-stimulated insulin secretion.
The Biochemical journal, 429(1), 205-213 (2010-04-27)
Tight coupling between cytosolic and mitochondrial metabolism is key for GSIS (glucose-stimulated insulin secretion). In the present study we examined the regulatory contribution of PDH (pyruvate dehydrogenase) kinase 1, a negative regulator of PDH, to metabolic coupling in 832/13 clonal
The Journal of biological chemistry, 270(48), 28989-28994 (1995-12-01)
Recent evidence from this laboratory indicates that at least two isoenzymic forms of pyruvate dehydrogenase kinase (PDK1 and PDK2) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation (Popov, K.M., Kedishvili, N.Y., Zhao
Warburg effect enhances glucose to lactate conversion in tumor cells, regardless of oxygen levels; impacting cancer metabolism since 1924.
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