Pyruvate dehydrogenase kinase
From Proteopedia
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Revision as of 09:20, 13 March 2012
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.
PDK isozyme 1
2q8f – hPDK1 – human
2q8g – hPDK1 + drug
2q8h – hPDK1 + dichloro-acetic acid
PDK isozyme 2
1jm6 – PDK2 + ADP – rat
2btz – hPDK2
2bu2 – hPDK2 + benzonitrile derivative + ATP
2bu5 - hPDK2 + benzonitrile derivative
2bu6 - hPDK2 + propanamide derivative
2bu7 - hPDK2 + acetamide derivative
2bu8 - hPDK2 + dichloro-acetic acid + ADP
3crk, 3crl – hPDK2 + acetyltransferase component of pyruvate dehydrogenase complex
PDK isozyme 3
1y8n, 1y8o, 1y8p, 2pnr – hPDK3 + acetyltransferase component of pyruvate dehydrogenase complex
2q8i – hPDK3 + radicicol
PDK isozyme 4
2e0a – hPDK4 + AMPPNP
2zkj, 3d2r – hPDK4 + ADP
2zdx, 2zdy – hPDK4 (mutant) + inhibitor
