Zobrazeno 1 - 10
of 144
pro vyhledávání: '"LESTER J. REED"'
Autor:
D. W. Carroll, Janet E. Lawson, Lester J. Reed, Marvin L. Hackert, Stephen R. Ernst, James E. Knapp
Publikováno v:
Protein Science. 9:37-48
The dihydrolipoamide succinyltransferase (E2o) component of the alpha-ketoglutarate dehydrogenase complex catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A. E2o is normally a 24-mer, but is found as a tr
Autor:
Lester J. Reed, R. Holland Cheng, Janet E. Lawson, James K. Stoops, Wangcai Liao, Z. Hong Zhou, Diane McCarthy
Publikováno v:
Journal of Biological Chemistry. 276:21704-21713
Structural studies by three-dimensional electron microscopy of the Saccharomyces cerevisiae truncated dihydrolipoamide acetyltransferase (tE2) component of the pyruvate dehydrogenase complex reveal an extraordinary example of protein dynamics. The tE
Publikováno v:
Protein Expression and Purification. 20:128-131
A facile one-step affinity chromatographic purification of the recombinant catalytic subunit (PDPc) of bovine pyruvate dehydrogenase phosphatase (PDP) to near homogeneity is described. PDPc binds in the presence of Ca(2+) to the inner lipoyl domain (
Autor:
Lester J. Reed, James E. Knapp, Mohammad A. Yazdi, David T. Mitchell, Stephen R. Ernst, Marvin L. Hackert
Publikováno v:
Journal of Molecular Biology. 280:655-668
The dihydrolipoamide succinyltransferase (E2o) component of the 2-oxoglutarate dehydrogenase multienzyme complex is composed of 24 subunits arranged with 432 point group symmetry. The catalytic domain (CD) of the E2o component catalyzes the transfer
Autor:
Lester J. Reed
Publikováno v:
Protein Science. 7:220-224
Publikováno v:
Journal of Biological Chemistry. 272:31625-31629
cDNA encoding the regulatory subunit of bovine mitochondrial pyruvate dehydrogenase phosphatase (PDPr) has been cloned. Overlapping cDNA fragments were generated by the polymerase chain reaction from bovine genomic DNA and from cDNA synthesized from
Publikováno v:
Biochemistry. 35:5879-5882
The dihydrolipoamide dehydrogenase-binding protein (E3BP), a component of the Saccharomyces cerevisiae and mammalian pyruvate dehydrogenase (PDH) complexes, anchors an E3 homodimer inside each of the 12 pentagonal faces of the 60-mer dihydrolipoamide
Autor:
Xiao-Da Niu, John P. Schroeter, Steven J. Kolodziej, Timothy S. Baker, Lester J. Reed, James K. Stoops
Publikováno v:
The Journal of biological chemistry, vol 267, iss 34
Dihydrolipoamide acyltransferase (E2), a catalytic and structural component of the three functional classes of multienzyme complexes that catalyze the oxidative decarboxylation of alpha-keto acids, forms the central core to which the other components
Publikováno v:
Biochemistry. 30:11249-11254
The LAT1 gene encoding the dihydrolipoamide acetyltransferase component (E2) of the pyruvate dehydrogenase (PDH) complex from Saccharomyces cerevisiae was disrupted, and the lat1 null mutant was used to analyze the structure and function of the domai
Publikováno v:
Biochemistry. 30:2834-2839
Disruption of the PDX1 gene encoding the protein X component of the mitochondrial pyruvate dehydrogenase (PDH) complex in Saccharomyces cerevisiae did not affect viability of the cells. However, extracts of mitochondria from the mutant, in contrast t