In: Biology
Pyruvate dehydrogenase (PDH) kinase 1 (PDK1) phosphorylates and inhibits PDH and thusly increases citrate production for lipid synthesis
True/false?
Answer :
False.
Pyruvate dehydrogenase kinase phosphorylates and inhibit pyruvate dehydrogenase.
This phosphorylation occurs by ATP to ADP conversion. Inhibition occurs when there is excess ATP, NADH and acetyl CoA.
When pyruvate dehydrogenase is inhibited, the excess acetyl CoA with ATP and NADH enters lipid synthesis.
As there is inhibition of PDH, Pyruvate wont enter citric acid cycle and so no citrate will be formed.
Lipid synthesis consists of 2 phases fattyacid synthesis and triglyceride synthesis. Acetyl CoA is a substrate. Lipids are manufactured in endoplasmic reticulum. Citrate from mitochondria is transported to cytoplasm. There its acted upon by ATPcitrate lyase and cleaved into oxaloacetate and acetyl CoA. This cytosolic acetyl CoA is used for fatty acid synthesis.
So increase in citrate increase fattyacid production. But when pdh is inhibited there will be less citrate formed.