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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ acetate + CO₂ + ubiquinol

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

References

1. Recny, M.A. and 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. and 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. and 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. and 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. and 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. and 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 and 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. and 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.

External links

• Pyruvate dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH)