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- W142433246 abstract "The pyruvate dehydrogenase (E1) is the first catalytic component of the multienzyme pyruvate dehydrogenase complex (PDC). El catalyzes the two partial reactions: the thiamin pyrophosphate (TPP)-dependent decarboxylation of pyruvic acid to 2-hydroxyethylidene-TPP (HETPP) [Eq. 1] and reductive acetylation of lipoic acid residues covalently linked to the second catalytic component — dihydrolipoamide acetyltransferase (E2) [Eq. 2] (Reed, 1974): $$C{H_3}COC{O_2} - + E{1_ - }TPP to C{H_3}Cleft( {OH} right) = TPP - E1 + C{O_2}$$([1])$$C{H_3}Cleft( {OH} right) = TPP - E1 + E2 - lipoatesleft( {{S_2}} right) to ETPP + E2 - lipoateleft( {SH} right)SCOC{H_3}$$(2)Mammalian E1 is a heterotetramer (α[2]β2) containing two 41 kDa α subunits and two kDa β subunits. The role of individual subunits is not clear. It was proposed that E1α can catalyze the first partial reaction and E1β the second (Roche and Reed, 1972). E1α is thought to be involved in TPP binding as it contains TPP motif found by sequence comparison of several TPP requiring enzymes (Hawkins et al., 1989). Recent evidence indicates that both subunits are involved in TPP binding (Robinson and Chun, 1993; Ali et al., 1995; Korotchkina et al., 1995)." @default.
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- W142433246 date "1996-01-01" @default.
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- W142433246 title "Probing the active site of mammalian pyruvate dehydrogenase" @default.
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- W142433246 doi "https://doi.org/10.1007/978-3-0348-8981-0_2" @default.
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