Pyruvate dehydrogenase (quinone)

Pyruvate dehydrogenase (quinone)
Identifiers
EC number 1.2.5.1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Pyruvate dehydrogenase (quinone) (EC 1.2.5.1, pyruvate dehydrogenase, pyruvic dehydrogenase, pyruvic (cytochrome b1) dehydrogenase, pyruvate:ubiquinone-8-oxidoreductase, pyruvate oxidase (ambiguous)) is an enzyme with systematic name pyruvate:ubiquinone oxidoreductase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction

pyruvate + ubiquinone + H2O acetate + CO2 + ubiquinol

This bacterial enzyme is located on the inner surface of the cytoplasmic membrane.

References

  1. ↑ Recny, M.A.; Hager, L.P. (1982). "Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD". J. Biol. Chem. 257 (21): 12878–12886. PMID 6752142.
  2. ↑ Cunningham, C.C.; Hager, L.P. (1975). "Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids". J. Biol. Chem. 250 (18): 7139–7146. PMID 1100621.
  3. ↑ Koland, J.G.; Miller, M.J.; Gennis, R.B. (1984). "Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase". Biochemistry. 23 (3): 445–453. doi:10.1021/bi00298a008. PMID 6367818.
  4. ↑ Grabau, C.; Cronan, J.E. Jr. (1986). "In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site". Biochemistry. 25 (13): 3748–3751. doi:10.1021/bi00361a003. PMID 3527254.
  5. ↑ Wang, A.Y.; Chang, Y.Y.; Cronan, J.E. Jr. (1991). "Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding". J. Biol. Chem. 266 (17): 10959–10966. PMID 2040613.
  6. ↑ Chang, Y.Y.; Cronan, J.E. Jr. (1997). "Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase". Biochemistry. 36 (39): 11564–11573. doi:10.1021/bi9709102. PMID 9305946.
  7. ↑ O'Brien, T.A.; Schrock, H.L.; Russell, P.; Blake, R. 2nd; Gennis, R.B. (1976). "Preparation of Escherichia coli pyruvate oxidase utilizing a thiamine pyrophosphate affinity column". Biochim. Biophys. Acta. 452 (1): 13–29. doi:10.1016/0005-2744(76)90054-1. PMID 791368.
  8. ↑ Bertagnolli, B.L.; Hager, L.P. (1993). "Role of flavin in acetoin production by two bacterial pyruvate oxidases". Arch. Biochem. Biophys. 300 (1): 364–371. doi:10.1006/abbi.1993.1049. PMID 8424670.
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