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heterotetramer
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x-ray crystallography
monomer
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1 * 100000, SDS-PAGE
?
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x * 40000-41000 + x * 37000
dimer
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2 * 94000, SDS-PAGE
dimer
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2 * 99474, calculation from nucleotide sequence
dimer
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2 * 95000-96500, SDS-PAGE with and without urea
dimer
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2 * 100000, SDS-PAGE
dimer
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alpha2,beta2, 2 * 43000 + 2 * 40000, SDS-PAGE, immunoblotting
dimer
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alpha2,beta2, 2 * 38000 + 2 * 56000, SDS-PAGE, N-terminal amino acid sequencing
multimer
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x * 68000, lipoate acetyltransferase, x * 54800, lipoamide dehydrogenase, x *41900, alpha-pyruvate dehydrogenase, x * 45000, beta-pyruvate dehydrogenase subunit, plus x * 45000, component X, SDS-PAGE
multimer
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x *42000 and x * 37000, alpha- and beta-subunits of pyruvate dehydrogenase, respectively, x * 76000, lipoate acetyltransferase, and x * 56000, lipoamide dehydrogenase. Two unknown polypeptides of 46000 and 41000 are additionally detected
multimer
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x * 57000, x * 54000, x * 42000 and x * 36000, respectively, SDS-PAGE. The empirical unit must be repeated at least 50 times to make up the assembled complex
multimer
x * 70000, E2 subunit, x * 55000, E3 subunit, SDS-PAGE
multimer
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x * 160000, x * 57600, x * 55600, x * 52500, x * 37100, SDS-PAGE
multimer
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x * 100000, pyruvate dehydrogenase, x * 87000, dihydrolipoamide transacetylase (acetyl-CoA:dihydrolipoamide S-acetyltransferase, EC 2.3.1.12), and x * 56000, dihydrolipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.6.4.3) components, respectively, SDS-PAGE
multimer
x * 78000, i.e. dihydrolipoamide transacetylase (E2) subunit, x * 60000, x * 58000, i.e. dihydrolipoamide dehydrogenase (E3) subunit, x * 55000, x * 43000 and x * 41000, i.e. alpha-subunits of pyruvate dehydrogenase, and x * 37000, i.e. beta-subunit of pyruvate dehydrogenase (E1), respectively, SDS-PAGE
multimer
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x * 39800, x * 41700, 53700, and 57500, i.e. pyruvate decarboxylase subunits (E1), lipoate acetyltransferase (E2), and lipoamide dehydrogenase (E3), respectively, SDS-PAGE
oligomer
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x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE
oligomer
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x * 58000-59000, i.e. transacetylase, x * 53 000, i.e. lipoamide dehydrogenase, x * 40000-41000, x * 37000, SDS-PAGE
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oligomer
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60 * 41000 (E1 alpha) + 60 * 36000 (E1 beta) + 60 * 52000 (E2, EC 2.3.1.12) + 12 * 55000 (E3, EC 1.8.1.4) + 8-12 * 50000 (component X) + kinase and phosphatase components, heart pyruvate dehydrogenase complex
oligomer
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quaternary structure of pyruvate dehydrogenase complex
tetramer
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alpha2,beta2, 2 * 42000 + 2 * 38000, SDS-PAGE
tetramer
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alpha2,beta2, 2 * 41000 + 2 * 36000
tetramer
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alpha2,beta2, 2 * 42000 + 2 * 36000, SDS-PAGE, calculated from gene sequence
tetramer
Pigeon
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alpha2,beta2, 2 * 42000 + 2 * 37000, SDS-PAGE
tetramer
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alpha2,beta2, 2 * 41000 + 2 * 35000, SDS-PAGE
tetramer
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alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
tetramer
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alpha2,beta2, 2 * 45000 + 2 * 35000, SDS-PAGE
tetramer
alpha2,beta2, 1 * 43000 + 1 * 41000 + 2 * 37000, SDS-PAGE
additional information
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lipoamide dehydrogenase and two unknown polypeptides bind tightly to complex
additional information
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enzyme component organization and binding structures in the pyruvate dehydrogenase multienzyme complex, core is formed by compoenents E2 and E3, regulatory role
additional information
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identification of key amino acid residues responsible for enzyme component assembly to the multienzyme complex, overview
additional information
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analysis of pyruvate dehydrogenase core complex consisting of dihydrolipoyl acetyltransferase and dihydrolipoyl dehydrogenase enzymes and comparison with structure of enzyme complex with dihydrolipoyl acetyltransferase
additional information
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analysis of architecture of enzyme subunits in pyruvate dehydrogenase complex. Complex contains 30 enzyme heterotetramers plus dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase multimers
additional information
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the affinity of PDH2 for the PDH-binding domain of E2 of pyruvate dehydrogenase complex differs only modestly from that of PDH1, surface plasma resonance studies
additional information
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
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the complex consists of four subunits, i.e. E1alpha (44 kDa), E1beta (35 kDa), E2 (73 kDa), and E3 (60 kDa), SDS-PAGE
additional information
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PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
additional information
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the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
additional information
the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
additional information
-
PDC displays size versatility in an ionic strength-dependent manner. PDC is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Each oligomeric component of PDC displays a larger size than expected. The activity of PDC is reduced in higher ionic strength
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additional information
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the pyruvate dehydrogenase complex PDC displays size versatility in an ionic strength-dependent manner. Yeast PDC is a salt-labile complex that dissociates into submegadalton individual components even under physiological ionic strength. The ionic strength can modulate its catalytic activity. E1 elutes at fractions for about 440 kDa proteins that mainly contain E1alpha, E1beta, and a nominal amount of E2. E3 elutes at fractions for about 230 kDa, which contain mostly E3
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