The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and carbon dioxide, and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 beta subunit. Mutations in this gene are associated with pyruvate dehydrogenase E1-beta deficiency. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Mar 2012].
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Grimm, Calgéer, Teriete, Biegner, Munz, Reinert: "Targeting thiamine-dependent enzymes for metabolic therapies in oral squamous cell carcinoma?" in: Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico, Vol. 18, Issue 2, pp. 196-205, (2016) (PubMed).
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: "Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells." in: Nature methods, Vol. 10, Issue 4, pp. 315-23, (2013) (PubMed).