Abstract
Pyruvate oxidase is one of several flavoprotein dehydrogenases that feed electrons into the E. coli respiratory chain. The enzyme catalyzes the oxidative decarboxylation of pyruvate to acetic acid and CO2 (Hager, 1957). Although usually a minor component in E. coli, it can be induced to higher levels in mutant strains and provides a pathway for pyruvate catabolism alternative to that of the pyruvate dehydrogenase complex. Pyruvate oxidase is a tetramer with identical subunits of 60,000 daltons (Williams and Hager, 1960; O’Brien et al., 1976). Each subunit has a tightly bound flav in adenine dinucleotide (FAD), and the addition of a second cofactor, thiamin pyrophosphate, is necessary to elicit catalytic activity. Enzymatic activity is easily monitored spectrophotometrically using ferricyanide as an artificial oxidant.
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© 1982 Plenum Press, New York
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Koland, J.G., Mather, M.W., Gennis, R.B., White, J.S., Hager, L.P. (1982). Activation of Pyruvate Oxidase and Interaction with Membrane Components. In: Martonosi, A.N. (eds) Membranes and Transport. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4082-9_10
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DOI: https://doi.org/10.1007/978-1-4684-4082-9_10
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