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 | ||||||||
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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
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
External links
- Pyruvate dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH)
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