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homotetramer
x-ray crystallography
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x * 65000, SDS-PAGE
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x * 83000, SDS-PAGE
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x * 72000, isozyme 1, SDS-PAGE
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x * 64000, SDS-PAGE
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x * 60400, calculated from amino acid sequence
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x * 62000, isozyme ZmChlMe1, x * 72000, isozyme ZmChlMe2
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x * 62000-66000, recombinant chimeric enzymes, SDS-PAGE
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x * 62000-66000, SDS-PAGE
dimer

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2 * 42000, SDS-PAGE
dimer
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the dimeric form of c-NADP-ME is as active as tetramers, analytical ultracentrifugation
dimer
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2 * 70000, SDS-PAGE
dimer
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2 * 49000, SDS-PAGE
dimer
2 * 42500, SDS-PAGE
dimer
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2 * 42500, SDS-PAGE
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dimer
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2 * 72000, SDS-PAGE
dimer
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2 * 61300, about, DNA sequence calculation
monomer

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1 * 70000, SDS-PAGE
monomer
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1 * 72000, SDS-PAGE
monomer
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1 * 61300, about, DNA sequence calculation
oligomer

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the cytosolic PtNADP-ME2 aggregates as octamers and hexadecamers while the plastidic PtNADP-ME4 resembles hexamers and octamers. Different PtNADP-ME family members present different oligomeric states in vitro
oligomer
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x * 62000, detagged recombinant wild-type enzyme
tetramer

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4 * 64000, SDS-PAGE
tetramer
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subunit structure and organisation, crystal structure
tetramer
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structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview
tetramer
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4 * 64000, SDS-PAGE
tetramer
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4 * 63000, SDS-PAGE
tetramer
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4 * 65000, SDS-PAGE
tetramer
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c-NADP-ME exists mainly as a tetramer, analytical ultracentrifugation
tetramer
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c-NADP-ME has a dimer-dimer quaternary structure in which the dimer interface associates more tightly than the tetramer interface
tetramer
a dimer of dimers. The c-NADP-ME monomer is composed of four domains. Domain A (residues 23-130) is predominantly helical and confers the ability to bind fumarate. Domain B (residues 131-277 and 464-535) contains a central five-stranded parallel beta-sheet surrounded by helices on both sides. Domain C (residues 278-463) exhibits a dinucleotide-binding Rossmann fold with a modification: strand beta3 is replaced by a short antiparallel beta-strand. Domain D (residues 536-579) contains one helix followed by a long extended random coil structure protruding away from the ordered portion of the ME monomer. The active site of ME is located at the interface of domains B and C, whereas residues in domains A and D primarily participate in the formation of dimers and tetramers
tetramer
4 * 64000, about, isozyme Hvme3, sequence calculation; 4 * 68000, about, isozyme Hvme2, sequence calculation; 4 * 72000, about, isozyme Hvme1, sequence calculation
tetramer
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4 * 64900, SDS-PAGE
tetramer
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4 * 72000, isozyme 2, SDS-PAGE
tetramer
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4 * 62000, tissue specific isozymes, SDS-PAGE, 4 * 70000, tissue specific isozymes, SDS-PAGE
tetramer
4 * 63000, plastidic isozyme, SDS-PAGE; 4 * 65000, cytosolic isozyme, SDS-PAGE
tetramer
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4 * 72000, SDS-PAGE
tetramer
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4 * 63000, approximately, SDS-PAGE
tetramer
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4 * 64000-65000, SDS-PAGE
tetramer
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4 * 72000, SDS-PAGE
tetramer
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4 * 62000, SDS-PAGE
tetramer
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4 * 61300, about, DNA sequence calculation
tetramer
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4 * 62000, recombinant mature isozyme NADP-ME2, SDS-PAGE
tetramer
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recombinant ZmC4-NADP-ME wild-type and mutants
additional information

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circular dichroism structure analysis of wild-type and mutant enzymes, overview
additional information
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at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, aggregation of the enzyme is attributable to the Trp572 side chain, overview
additional information
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MaeB possesses a multimodular structure, it is composed of two distinct domains, MWs of the different isozymes, overview
additional information
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the enzyme is first dissociated from a tetramer to dimers before the 2 M urea treatment, and the dimers then dissociated into monomers before the 2.5 M urea treatment
additional information
structure comparisons, overview
additional information
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the enzyme exists in several different oligomeric states depending on the metabolite concentrations, light status, ionic strength as well as pH, conformational changes of guanidine hydrochloride-denatured NADP-malic enzyme studied by quenching of protein native fluorescence with KI and acrylamide, overview
additional information
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extent of oligomerization is pH-dependent, 3D-structure analysis
additional information
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the enzyme exists in several different oligomeric states depending on the metabolite concentrations, light status, ionic strength as well as pH, conformational changes of guanidine hydrochloride-denatured NADP-malic enzyme studied by quenching of protein native fluorescence with KI and acrylamide, overview