||The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 188.8.131.52, branched-chain α-keto acid dehydrogenase system, EC 184.108.40.206, 2-oxoglutarate dehydrogenase system, EC 220.127.116.11, glycine cleavage system, and EC 18.104.22.168, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 22.214.171.124, pyruvate dehydrogenase (acetyl-transferring) (E1), EC 126.96.36.199, dihydrolipoyllysine-residue acetyltransferase (E2), and EC 188.8.131.52, dihydrolipoyl dehydrogenase (E3). The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
||Reed, L.J., Pettit, F.H., Eley, M.H., Hamilton, L., Collins, J.H. and Oliver, R.M. Reconstitution of the Escherichia coli pyruvate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 72 (1975) 3068–3072. [PMID: 1103138]
||Bates, D.L., Danson, M.J., Hale, G., Hooper, E.A. and Perham, R.N. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Nature 268 (1977) 313–316. [PMID: 329143]
||Stanley, C.J., Packman, L.C., Danson, M.J., Henderson, C.E. and Perham, R.N. Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources. Biochem. J. 195 (1981) 715–721. [PMID: 7032507]
||Yang, H.C., Hainfeld, J.F., Wall, J.S. and Frey, P.A. Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli. J. Biol. Chem. 260 (1985) 16049–16051. [PMID: 3905803]
||Patel, M.S. and Roche, T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4 (1990) 3224–3233. [PMID: 2227213]