Pyruvate dehydrogenase kinase: Difference between revisions
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== Function == | == Function == | ||
'''Pyruvate dehydrogenase kinase''' (PDK) is part of the pyruvate dehydrogenase complex. This complex is located in the mitochondria and converts pyruvate to acetyl-CoA as part of the citric acid cycle. PDK phosphphorylates serine residues on pyruvate dehydrogenase using ATP. There are 4 isozymes of PDK. The isozymes differ in length, activity and phosphorylation sites<ref>PMID:11486000</ref>. | '''Pyruvate dehydrogenase kinase''' (PDK) is part of the pyruvate dehydrogenase complex. This complex is located in the mitochondria and converts pyruvate to acetyl-CoA as part of the citric acid cycle. PDK phosphphorylates serine residues on pyruvate dehydrogenase using ATP. There are 4 isozymes of PDK. The isozymes differ in length, activity and phosphorylation sites<ref>PMID:11486000</ref>. | ||
*'''PDK1''' is abundant in heart cells. | *'''PDK1''' is abundant in heart cells. PDK1 expression was found to predict future major adverse cardiovascular events<ref>PMID:36866436</ref>. | ||
*'''PDK2''' is abundant in mitochondria. | *'''PDK2''' is abundant in mitochondria. | ||
*'''PDK3''' is abundant in testis. | *'''PDK3''' is abundant in testis. | ||
*'''PDK4''' is abundant in muscle and heart. It is important during starvation for regulation of pyruvate dehydrogenate complex activity and glucose homoeostasis<ref>PMID:16606348</ref> | *'''PDK4''' is abundant in muscle and heart. It is important during starvation for regulation of pyruvate dehydrogenate complex activity and glucose homoeostasis<ref>PMID:16606348</ref>. | ||
== Relevance == | == Relevance == | ||
