Abstract
Pyruvate dehydrogenase systems have been isolated from Escherichia coli, avian and mammalian tissues, and Neurospora crassa as functional units with molecular weights in the millions (1). The bacterial, avian, and mammalian pyruvate dehydrogenase complexes have been separated into three enzymes — pyruvate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase (a flavoprotein), and functional units resembling the native complexes have been reassembled from the individual enzymes. These three enzymes act in a coordinated manner as indicated in Fig. 1 (1,2). The discussion will be limited to the structure, function, and regulation of the mammalian pyruvate dehydrogenase complex.
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Reed, L.J. et al. (1972). Molecular Aspects of the Regulation of the Mammalian Pyruvate Dehydrogenase Complex. In: Wieland, O., Helmreich, E., Holzer, H. (eds) Metabolic Interconversion of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-37966-0_29
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DOI: https://doi.org/10.1007/978-3-662-37966-0_29
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