Abstract
Enzyme systems that catalyze a lipoic acid-mediated oxidative decarboxylation of pyruvate and α-ketoglutarate have been isolated from microbial and eukaryotic cells as functional units with molecular weights in the millions. Each complex consists of three catalytic components: pyruvate dehydrogenase or α -ketoglutarate dehydrogenase (E1); dihydrolipoyl transacetylase or dihydrolipoyl trans-succinylase (E2); and dihydrolipoyl dehydrogenase (E3), a flavopro-tein that is a common component of the two complexes. These three enzymes, acting in sequence, catalyze1 the reactions shown in Fig. 1, E1 catalyzes both the decarboxylation of the α -keto acid (reaction 1) and the subsequent reductive acylation of the lipoyl moiety (reaction 2) that is covalently bound2 to E2. E2 catalyzes the tran-sacylation step (reaction 3), and E3 catalyzes reoxidation of the dihydrolipoyl moiety with NAD+ as the ultimate electron acceptor (reactions 4 and 5). The pyruvate dehydrogenase complexes from eukaryotic cells also contain small amounts of two regulatory enzymes, a kinase and a phosphatase, that modulate the activity of E1 by phosphorylation and dephosphorylation, respectively.3
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References
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Reed, L.J., Oliver, R.M. (1982). Structure-Function Relationships in Pyruvate and α-Ketoglutarate Dehydrogenase Complexes. In: Bossa, F., Chiancone, E., Finazzi-Agrò, A., Strom, R. (eds) Structure and Function Relationships in Biochemical Systems. Advances in Experimental Medicine and Bioligy, vol 148. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9281-5_19
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DOI: https://doi.org/10.1007/978-1-4615-9281-5_19
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