L
Lester J. Reed
Researcher at University of Texas at Austin
Publications - 143
Citations - 9459
Lester J. Reed is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Pyruvate dehydrogenase complex & Pyruvate dehydrogenase phosphatase. The author has an hindex of 52, co-authored 143 publications receiving 9249 citations. Previous affiliations of Lester J. Reed include Virginia Tech & National Institutes of Health.
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Function of phosphorylation sites on pyruvate dehydrogenase.
TL;DR: Evidence is presented that dephosphorylation of the three phosphorylation sites on bovine kidney pyruvate dehydrogenase by pyruVate dehydrogensase phosphatase is random, and the presence of phosphoryl groups at sites 2 and 3 did not significantly affect the rate of deph phosphatelation at site 1 or the rates of reactivation of the enzyme by the phosphat enzyme.
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Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae.
TL;DR: Comparison of the deduced amino acid sequences of yeast protein X and dihydrolipoamide acetyltransferase indicates that the two proteins evolved from a common ancestor.
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alpha-Keto acid dehydrogenation complexes. III. Purification and properties of dihydrolipoic dehydrogenase of Escherichia coli.
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On the Unique Structural Organization of the Saccharomyces cerevisiae Pyruvate Dehydrogenase Complex
James K. Stoops,R. Holland Cheng,Mohammed A. Yazdi,Cheol Young Maeng,John P. Schroeter,Uwe Klueppelberg,Uwe Klueppelberg,Steven J. Kolodziej,Timothy S. Baker,Lester J. Reed +9 more
TL;DR: Investigation of the structures of the truncated 60-mer core dihydrolipoamide acetyltransferase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex shows that the 12 large openings in the tE2 core permit the entrance of tBP, BP, and BP·;E3 into a large central cavity where the BP component apparently binds near the tip of the t E2 trimer.
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Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics.
Z. Hong Zhou,Wangcai Liao,R. Holland Cheng,Janet E. Lawson,Diane McCarthy,Lester J. Reed,James K. Stoops +6 more
TL;DR: It is proposed that this springlike feature is involved in a thermally driven expansion and contraction of the core and, since it appears to be a common feature in the phylogeny of pyruvate dehydrogenase complexes, protein dynamics is an integral component of the function of these multienzyme complexes.