The Enzyme Database

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Accepted name: pyruvate dehydrogenase system
Reaction: pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH
Other name(s): pyruvate dehydrogenase complex; PDH
Systematic name: pyruvate:NAD+ 2-oxidoreductase (CoA-acetylating)
Comments: The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC, branched-chain α-keto acid dehydrogenase system, EC, 2-oxoglutarate dehydrogenase system, EC, glycine cleavage system, and EC, 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, pyruvate dehydrogenase (acetyl-transferring) (E1), EC, dihydrolipoyllysine-residue acetyltransferase (E2), and EC, dihydrolipoyl dehydrogenase (E3). The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  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. [DOI] [PMID: 1103138]
2.  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. [DOI] [PMID: 329143]
3.  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. [DOI] [PMID: 7032507]
4.  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]
5.  Patel, M.S. and Roche, T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4 (1990) 3224–3233. [DOI] [PMID: 2227213]
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