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dimer or tetramer
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a tight dimer, known as the functional dimer, is the minimal catalytically active unit, two of these functional dimers assemble into a loose tetramer in the quaternary structure
heterotetramer
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native, catalytically active form, dimer of dimers
homodimer
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2 * 60000, smallest enzymatically active unit, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
oligomer
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the enzyme forms filamentous structures at pH 6.0-6.5 of octamers and dodecamers, NcPDC tetramers display the lowest catalytic efficiency among all functional oligomeric forms of this enzyme, analysis by analytical gel filtration, analytical ultracentrifugation and small-angle X-ray solution scattering
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x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
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x * 58873, anhydrous molecular mass, calculated from the amino acid sequence
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x * 62590, calculated from amino acid sequence
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x * 59200, calculated, x * 60000, SDS-PAGE
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x * 59200, calaculated from amino acid sequence
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x * 60000, SDS-PAGE
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x * 59200, calaculated from amino acid sequence
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x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
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x * 60800, about, sequence calculation, x * 59000, recombinant His-tagged enzyme, SDS-PAGEs
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x * 103400, maltose binding protein-bound isoform Pdc1p, calculated from amino acid sequence
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x * 104900, maltose binding protein-bound isoform Pdc5p, calculated from amino acid sequence
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x * 103400, maltose binding protein-bound isoform Pdc1p, calculated from amino acid sequence
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x * 104900, maltose binding protein-bound isoform Pdc5p, calculated from amino acid sequence
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x * 64000, alpha-subunit + x * 62000, beta-subunit
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x * 60800, calculated from amino acid sequence
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x * 60000, SDS-PAGE
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x * 60800, calculated from amino acid sequence
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2 protein bands detected in SDS-PAGE: 65000 and 68000, the enzyme exists as a mixture of tetramers, octamers and higher oligomers
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x * 60000, about, SDS-PAGE, x * 61486, calculated from the amino acid sequence
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x * 60000, SDS-PAGE, x * 61320, mass spectrometry, x * 61468, calculated from the nucleotide sequence
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x * 62000, recombinant enzyme, SDS-PAGE
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x * 66000, SDS-PAGE
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x * 58000, recombinant enzyme, SDS-PAGE
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2 types of subunits, MW 61000 and MW 62000, SDS-PAGE
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x * 60930, calculated from amino acid sequence
dimer
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
dimer
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catalytically active form
dimer
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1 * 39800 + 1 * 41700, the dimeric pyruvate decarboxylase is a component of the multienzyme complex pyruvate dehydrogenase, SDS-PAGE
dimer
2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
dimer
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2 * 58700, SDS-PAGE, 2 * 62000, calculated, both isoform PDC I and PDC II
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homotetramer
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homotetramer
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4 * 60000, native, active enzyme state, dimer of dimers, PDC consists of dimers and tetramers under physiological conditions, subunit interactions, SDS-PAGE
homotetramer
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dimer of dimers, minimal catalytic unit is a functional dimer
homotetramer
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dimer of dimers, minimal catalytic unit is a functional dimer, two active sites in the functional dimer act in an antiphase manner during the reaction, with each active site eventually completing the full catalytic cycle, study of subunit dissociation into two types of dimers depending on the experimental conditions and their reassociation
homotetramer
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dimer of dimers, the minimal catalytic unit is the dimer with its active sites are not acting independently of one another, alternating sites model
homotetramer
4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
homotetramer
Sarcina ventriculi Goodsir / ATCC 55887
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4 * 58000, recombinant PDC, pH 6.5, SDS-PAGE
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homotetramer
alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
homotetramer
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alpha4, 4 * 61000, SDS-PAGE, 4 * 61600, amino acid sequence
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homotetramer
2 * 59400, calculated from amino acid sequence
homotetramer
4 * 60800, wild-type PDC, SDS-PAGE
monomer
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1 * 60000, alpha subunit, catalytically inactive form
monomer
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1 * 60000, catalytically inactive enzyme state, SDS-PAGE
octamer
2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
octamer
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2 * 12000 + 2 * 26000 + 2 * 35000 + 2 * 46000, SDS-PAGE
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tetramer
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4 * 57000, SDS-PAGE
tetramer
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4 * 60000, SDS-PAGE
tetramer
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4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme shows a half-side closed tetramer in presence or absence of any activator, the half-side closed form is predominant for Kluyveromyces lactis pyruvate decarboxylase, the structuring of the flexible loop region 105-113 seems to be the crucial step during the substrate activation process, overview
tetramer
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4 * 61500, mass spectrometry, SDS-PAGE, 4 * 61821, calculated from the amino acid sequence
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tetramer
4 * 61000, calculated, 4 * 66000, SDS-PAGE
tetramer
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4 * 62000-64000, SDS-PAGE
tetramer
1 * 45000 plus 1 * 35000 plus 1 * 22000 plus 1 * 14000, SDS-PAGE
tetramer
2 * 61000, SDS-PAGE, the isozyme is found in two different native forms, dimer and tetramer, with the dimer being the predominant form
tetramer
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4 * 60000, SDS-PAGE
tetramer
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enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
tetramer
subunit crystal structure analysis, the subunits are each composed of three domains, the R domain, the PYR domain, and the PP domain, all three domains exhibit typical alpha/beta-topology, the enzyme contains flexible loops comprising residues 106-113 and 292-301 involved in catalysis via four active sites, open and closed conformation of the activate and nonactivated enzyme, respectively, the completely open enzyme state is favoured for Saccharomyces cerevisiae pyruvate decarboxylase, overview
tetramer
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enzyme structure, differences in the tetramer assembly of form A and B PDC, form A is the native PDC
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tetramer
1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
tetramer
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1 * 46000 plus 1 * 35000 plus 1 * 23000 plus 1 * 13000, SDS-PAGE
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tetramer
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4 * 60000, SDS-PAGE
tetramer
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4 * 60000, SDS-PAGE
tetramer
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4 * 59000, SDS-PAGE
tetramer
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4 * 56500, SDS-PAGE
tetramer
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4 * 60746, SDS-PAGE
tetramer
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two of the dimers form a tightly packed tetramer with pseudo 222 symmetry
tetramer
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4 * 60000, wild-type PDC and mutants D27E, D27N, E473D and E473Q, SDS-PAGE
additional information
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additional information
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additional information
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4 * 62000, SDS-PAGE
additional information
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one isoenzyme has the subunit structure alpha4 and the other has the subunit structure alpha2'beta2
additional information
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thiamine diphosphate is required for complete association of subunits to form active oligomer
additional information
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different oligomeric states, tetramers, dimers and monomers, of enzyme occur under defined conditions, unfolding kinetics, tetramers dissociate via a stable dimeric state into monomers
additional information
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treatment with 0.5 M urea results in dimeric, with 2 M urea in monomeric enzyme state
additional information
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conformational equilibrium between the open and closed conformations of the enzyme identified in the pyruvamide-activated structure
additional information
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additional information
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hydroxyl-ion-induced subunit dissociation
additional information
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additional information
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two types of protein chains detected by SDS-PAGE: MW 63000-65000 and MW 61000-62000
additional information
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additional information
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2 protein bands, MW 61000 and MW 60000, detected by SDS-PAGE of enzyme from kernels. 3 protein bands: MW 59000, 58000 and 44000, detected by SDS-PAGE of the enzyme from roots
additional information
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phosphate stabilizes the tetramer by shifting the dimer-tetramer equilibrium to higher pH values, without altering the conformation of the tetramer