Nomenclature
EC number
1.2.5.1
Systematic name
pyruvate:ubiquinone oxidoreductase
Recommended name
pyruvate dehydrogenase (quinone)
Synonyms
EC 1.2.2.2 <1> (<1> formerly [16]) [16]
ECPOX <4> [3]
POXEC <1> [5]
poxB <1> [8]
pqo <2> (<2> gene name [10]) [10]
pyruvate oxidase <1,3> (<1> enzyme also catalyzes the formation of acetoin
from pyruvate and acetaldehyde [5]) [1,2,4,5,7,9,11,16,18,19]
pyruvate:quinone oxidoreductase <2> [10]
pyruvate:ubiquinone-8-oxidoreductase <1> [16]
ubiquinione-dependent pyruvate oxidase <1> [6]
ubiquinone-dependent pyruvate oxidase <1> [13]
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References
Blake, R.; Hager, L.P.: Activation of pyruvate oxidase by monomeric and micellar amphiphiles. J. Biol. Chem., 253, 1963-1971 (1978)
Cunningham, C.C.; Hager, L.P.: Crystalline pyruvate oxidase from Escherichia coli. II. Activation by phospholipids. J. Biol. Chem., 246, 1575-1582 (1971)
Neumann, P.; Weidner, A.; Pech, A.; Stubbs, M.T.; Tittmann, K.: Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli. Proc. Natl. Acad. Sci. USA, 105, 17390-17395 (2008)
Kiuchi, K.; Hager, L.P.: Reconstitution of the lipid-depleted pyruvate oxidase system of Escherichia coli: the palmitic acid effect. Arch. Biochem. Biophys., 233, 776-784 (1984)
Bertagnolli, B.L.; Hager, L.P.: Role of flavin in acetoin production by two bacterial pyruvate oxidases. Arch. Biochem. Biophys., 300, 364-371 (1993)
Koland, J.G.; Miller, M.J.; Gennis, R.B.: Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase. Biochemistry, 23, 445-453 (1984)
Grabau, C.; Cronan, J.E., Jr.: In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site. Biochemistry, 25, 3748-3751 (1986)
Chang, Y.Y.; Cronan, J.E., Jr.: Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase. Biochemistry, 36, 11564-11573 (1997)
Marchal, D.; Pantigny, J.; Laval, J.M.; Moiroux, J.; Bourdillon, C.: Rate constants in two dimensions of electron transfer between pyruvate oxidase, a membrane enzyme, and ubiquinone (coenzyme Q8), its water-insoluble electron carrier. Biochemistry, 40, 1248-1256 (2001)
Schreiner, M.E.; Riedel, C.; Holatko, J.; Patek, M.; Eikmanns, B.J.: Pyruvate:-quinone oxidoreductase in Corynebacterium glutamicum: molecular analysis of the pqo gene, significance of the enzyme, and phylogenetic aspects. J. Bacteriol., 188, 1341-1350 (2006)
Cunningham, C.C.; Hager, L.P.: Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids. J. Biol. Chem., 250, 7139-7146 (1975)
Recny, M.A.; Hager, L.P.: Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD. J. Biol. Chem., 257, 1287812886 (1982)
Carter, K.; Gennis, R.B.: Reconstitution of the ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex. J. Biol. Chem., 260, 10986-10990 va(1985)
Mather, M.W.; Gennis, R.B.: Kinetic studies of the lipid-activated pyruvate oxidase flavoprotein of Escherichia coli. J. Biol. Chem., 260, 16148-16155 (1985)
Bertagnolli, B.L.; Hager, L.P.: Activation of Escherichia coli pyruvate oxidase enhances the oxidation of hydroxyethylthiamin pyrophosphate. J. Biol. Chem., 266, 10168-10173 (1991)
Wang, A.Y.; Chang, Y.Y.; Cronan, J.E., Jr.: Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding. J. Biol. Chem., 266, 10959-10966 (1991)
Grabau, C.; Cronan, J.E., Jr.: Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein. Nucleic Acids Res., 14, 5449-5460 (1986)
Hamilton, S.E.; Recny, M.; Hager, L.P.: Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase. Biochemistry, 25, 8179-8183 (1986)
Williams, F.; Hager, L.P.: A crystalline flavin pyruvate oxidase. J. Biol. Chem., 236, PC36-37 (1961)
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Schomburg, D., Schomburg, I. (2013). pyruvate dehydrogenase (quinone) 1.2.5.1. In: Schomburg, D., Schomburg, I. (eds) Class 1 Oxidoreductases. Springer Handbook of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36265-1_38
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