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General structural organization of mitochondrial NAD-dependent multienzyme alpha-ketoacid dehydrogenase complexes with alpha-ketoacid and acyl-CoA as their substrate and product, respectively

Pyruvate and acetyl-CoA are the substrate and product, respectively for pyruvate dehydrogenase complex (PDC). E3 binding protein (E3BP) – the product of PDHX and specific to PDC, is not depicted. E3, dihydrolipoamide dehydrogenase – the product of DLD, is not unique to PDC but shared by other NAD-dependent alpha-ketoacid dehydrogenase complexes, such as the branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) and alpha-ketoglutarate dehydrogenase complex (KGDC), among others. Lipoate modification of E2 component is noted, which is crucial for the acyltransferase reaction. Pyruvate dehydrogenase phosphatase and kinase, such as those encoded by PDP1 and PDK3, respectively, are specific regulators to PDC, with other phosphatases and kinases unique to the other alpha-ketoacid dehydrogenase complexes. (Contributed by Dr. Jirair K Bedoyan.)

Abbreviations: CoA, coenzyme A; FAD, flavin adenine dinucleotide; NAD, nicotinamide adenine dinucleotide; R, methyl group for pyruvate as the PDC substrate; and TPP, thiamine pyrophosphate, aka thiamine diphosphate (TDP).

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Associated Disorders

  • Disorder of pyruvate oxidation
  • Mitochondrial disorder
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