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x * 35600, calculated from amino acid sequence
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x * 62000, recombinant GST-tagged enzyme, SDS-PAGE
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x * 32638, calculated from sequence
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x * 32638, calculated from sequence
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x * 37000, FLAG-tagged enzyme, SDS-PAGE
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x * 32000-34000, SDS-PAGE
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x * 32000-34000, SDS-PAGE
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x * 50000, GST-tagged enzyme, SDS-PAGE
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x * 35000, SDS-PAGE, x * 34689, sequence calculation
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x * 35000, SDS-PAGE, x * 34689, sequence calculation
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x * 36517, cMDH, sequence calculation, x * 37340, C-terminally His-tagged cMDH, sequence calculation, x * 36000, His-tagged cMDH, SDS-PAGE
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x * 36517, calculated, x * 36000, SDS-PAGE, recombinant protein
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x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
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x * 35000, recombinant enzyme, SDS-PAGE, x * 35560, plasma membrane-associated enzyme, sequence calculation
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dimer
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dimer
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2 * 39500, pH 7.0, SDS-PAGE
dimer
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crystal structure shows a compact homodimer with one coenzyme bound per subunit. The crystal structure reveals that the association of the dimers to form tetramers is prevented by several deletions, taking place at the level of two loops that are known to be essential for the tetramerization process within the LDH and malDH enzymes
dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
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dimer
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2 * 34000, SDS-PAGE
dimer
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2 * 34000, SDS-PAGE
dimer
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2 * 36000, SDS-PAGE
dimer
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2 * 34000, m-MDH, SDS-PAGE
dimer
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2 * 36000, s-MDH, SDS-PAGE
dimer
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2 * 34600, SDS-PAGE
dimer
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1 * 39000 + 1 * 37000, SDS-PAGE
dimer
in the wild type the dimeric enzyme form is very unstable under low-salt conditions. The R207S/R292S mutation stabilizes the dimer sufficiently so that it can be observed and studied. The R207S/R292S mutant enzyme dissociates into dimers at 2 M NaCl, or at very low protein concentrations in 4 M NaCl above pH 7. This dimer is as active as the wild type tetramer at pH 8 but loses its activity at pH 7, without large changes in structure or association state
dimer
wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein
dimer
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in the wild type the dimeric enzyme form is very unstable under low-salt conditions. The R207S/R292S mutation stabilizes the dimer sufficiently so that it can be observed and studied. The R207S/R292S mutant enzyme dissociates into dimers at 2 M NaCl, or at very low protein concentrations in 4 M NaCl above pH 7. This dimer is as active as the wild type tetramer at pH 8 but loses its activity at pH 7, without large changes in structure or association state
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dimer
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wild-type enzyme and R207S/R292S mutant enzyme can both exist as dimeric species depending on solvent conditions. F- and SO42-, as well as the NADH cofactor, stabilize the dimeric form of the wild-type protein
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dimer
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2 * 39000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 45000, SDS-PAGE
dimer
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2 * 45000, SDS-PAGE
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dimer
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2 * 39400, SDS-PAGE
dimer
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2 * 31350, SDS-PAGE
dimer
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2 * 31350, SDS-PAGE
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dimer
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2 * 35600, cytoplasmic form, SDS-PAGE
dimer
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2 * 37000, mitochondrial form, SDS-PAGE
dimer
2 * 35000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 27500, SDS-PAGE
dimer
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2 * 27500, SDS-PAGE
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dimer
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2 * 47000, or tetramer, SDS-PAGE
dimer
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2 * 47000, or tetramer, SDS-PAGE
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dimer
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2 * 90000-95000, fusion protein of MDH with mitochondrial citrate synthase, SDS-PAGE
dimer
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2 * 40000, SDS-PAGE
dimer
2 * 36675, MALDI-TOF mass spectrometry
dimer
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2 * 36675, MALDI-TOF mass spectrometry
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dimer
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286630, 286632, 286633, 286636, 286638, 286640, 286641, 286645, 286658, 286661, 286672, 286673, 286675
dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
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dimer
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2 * 36000, SDS-PAGE
dimer
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2 * 36000, SDS-PAGE
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dimer
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2 * 35000, SDS-PAGE
dimer
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2 * 35000, SDS-PAGE
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dimer
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2 * 34500, SDS-PAGE
dimer
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2 * 58000, SDS-PAGE
dimer
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2 * 31600, SDS-PAGE
homodimer
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2 * 35000, SDS-PAGE
homodimer
2 * 45600, full-length enzyme, SDS-PAGE, 2 * 36500, mature enzyme without transit peptide, SDS-PAGE and glutaraldehyde cross-linking of plNAD-MDH
homodimer
2 * 37500, calculated from amino acid sequence
homodimer
2 * 37000, SDS-PAGE. Thioredoxin-reversible homodimerization of isoform cytMDH1 through Cys330 disulfide formation protects the protein from overoxidation
homodimer
2 * 35000, SDS-PAGE
homodimer
2 * 32200, calculated from amino acid sequence
homodimer
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2 * 36000, SDS-PAGE
homodimer
the dimer form dissociates to monomer at low enzyme concentration, and at low pH, and is active only in dimer form
homodimer
2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35800, about, sequence calculation
homodimer
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2 * 35000, recombinant enzyme, SDS-PAGE, 2 * 35800, about, sequence calculation
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homodimer
the active form of the Mtb MDH is a dimer. The His6-tag at the N-terminus of recombinant MDH does not inhibit the formation of a dimer by MDH
homodimer
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the active form of the Mtb MDH is a dimer. The His6-tag at the N-terminus of recombinant MDH does not inhibit the formation of a dimer by MDH
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homodimer
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2 * 45000, gel filtration
homodimer
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isoform MDH3, 2 * 35000, SDS-PAGE
homodimer
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isoform MDH3, 2 * 35000, SDS-PAGE
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homodimer
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2 * 37200, SDS-PAGE
homodimer
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x-ray crystallography
homodimer
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2 * 32000, native enzyme, gel filtration
homodimer
2 * 36874.5, recombinant enzyme, sequence calculation
homodimer
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2 * 35500, calculated from amino acid sequence
homooctamer
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isoform MDH1, 8 * 35000, SDS-PAGE
homooctamer
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isoform MDH1, 8 * 35000, SDS-PAGE
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homotetramer
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homotetramer
4 * 34700, His8-tagged enzyme, calculated from amino acid sequence
homotetramer
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4 * 35000, recombinant enzyme, SDS-PAGE, 4 * 33200, about, sequence calculation
homotetramer
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4 * 36100, calculated from amino acid sequence
homotetramer
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isoform MDH2, 4 * 35000, SDS-PAGE
homotetramer
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isoform MDH2, 4 * 35000, SDS-PAGE
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monomer
the monomer is in an inactive molten globule-like state, which can be reactivated through a structural change induced by NADH binding that allows it to associate into active dimers
monomer
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the monomer is in an inactive molten globule-like state, which can be reactivated through a structural change induced by NADH binding that allows it to associate into active dimers
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monomer
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1 * 38000, SDS-PAGE under both nonreduced and reduced conditions
tetramer
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4 * 39500, pH 8.0, SDS-PAGE
tetramer
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4 * 35000, SDS-PAGE
tetramer
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4 * 33500, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
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tetramer
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4 * 36000, SDS-PAGE
tetramer
4 * 32000, SDS-PAGE
tetramer
4 * 33000, SDS-PAGE
tetramer
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4 * 32000, SDS-PAGE
tetramer
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4 * 32000, SDS-PAGE
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tetramer
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4 * 35000, SDS-PAGE
tetramer
stabilized by ordered water molecule networks and intersubunit complex salt bridges locked in by bound solvent chloride and sodium ions
tetramer
the active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. In 4 M NaCl (pH 8) and for the protein concentration range above 5 mg/ml, the R207S/R292S mutant enzyme is predominantly a tetramer
tetramer
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stabilized by ordered water molecule networks and intersubunit complex salt bridges locked in by bound solvent chloride and sodium ions
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tetramer
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the active tetrameric mutant enzyme R207S/R292S dissociates under certain conditions to active dimers and under other conditions to inactive dimers. These dimers further dissociate into folded monomers which eventually unfold. In 4 M NaCl (pH 8) and for the protein concentration range above 5 mg/ml, the R207S/R292S mutant enzyme is predominantly a tetramer
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tetramer
4 * 33500, about, sequence calculation
tetramer
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4 * 33500, about, sequence calculation
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tetramer
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4 * 32000, SDS-PAGE
tetramer
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4 * 32000, SDS-PAGE
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tetramer
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4 * 21550, SDS-PAGE
tetramer
4 * 33292, calculated, 4 * 35086, MALDI-TOF
tetramer
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4 * 33292, calculated, 4 * 35086, MALDI-TOF
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tetramer
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4 * 33000, SDS-PAGE
tetramer
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4 * 35000, native enzyme, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
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tetramer
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4 * 37000, SDS-PAGE
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tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 36000, SDS-PAGE
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tetramer
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or dimer, 4 * 47000, SDS-PAGE
tetramer
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or dimer, 4 * 47000, SDS-PAGE
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tetramer
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4 * 37000, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
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tetramer
4 * 36675, MALDI-TOF mass spectrometry
tetramer
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4 * 36675, MALDI-TOF mass spectrometry
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tetramer
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4 * 34000, SDS-PAGE
tetramer
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4 * 36600, SDS-PAGE
tetramer
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4 * 34000, SDS-PAGE
tetramer
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4 * 31600, SDS-PAGE
tetramer
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4 * 35300, SDS-PAGE
trimer
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additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
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additional information
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increasing the pH from 7.0 to 8.5 causes association of dimers with formation of tetramers, while lowering of pH to 6.0 is accompanied by dissociation of enzyme dimers with formation of MDH monomers
additional information
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increasing the pH from 7.0 to 8.5 causes association of dimers with formation of tetramers, while lowering of pH to 6.0 is accompanied by dissociation of enzyme dimers with formation of MDH monomers
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additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
additional information
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the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
additional information
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the Ignicoccus islandicus MaDH amino-acid sequence predicts two domains: a NAD(P)-binding Rossmann-fold domain (residues 7 to 138) and a LDH C-terminal-like domain (residues 146 to 308), MalDH quaternary structure analysis and comparison, overview
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additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
additional information
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enzyme activity and electrophoretic pattern of MDH and lactate dehydrogenase, EC 1.1.1.27, compared in relation to heat and urea inactivation, overview
additional information
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oligomeric states of MDHs, overview
additional information
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peptide mass fingerprinting, overview
additional information
structure analysis and comparison, MALDI-TOF mass spectrometry, overview
additional information
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oligomeric states of MDHs, overview
additional information
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structure analysis and comparison, MALDI-TOF mass spectrometry, overview
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additional information
structure analysis, overview. Similar to other MDHs, a protomer of TtMDH has the N-terminal NAD binding domain and C-terminal catalytic domain and consists of 12 helices and 11 beta-strands. The N-terminal NAD binding domain (residue 1-156) is an open twisted structure with the classical Rossmann fold composed of a parallel six-stranded beta-sheet (beta1-beta6) and four alpha-helices (alpha1-alpha4). The C-terminal catalytic domain comprises an antiparallel twisted five-stranded sheet (beta7-beta11) surrounded by eight alpha-helices
additional information
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structure analysis, overview. Similar to other MDHs, a protomer of TtMDH has the N-terminal NAD binding domain and C-terminal catalytic domain and consists of 12 helices and 11 beta-strands. The N-terminal NAD binding domain (residue 1-156) is an open twisted structure with the classical Rossmann fold composed of a parallel six-stranded beta-sheet (beta1-beta6) and four alpha-helices (alpha1-alpha4). The C-terminal catalytic domain comprises an antiparallel twisted five-stranded sheet (beta7-beta11) surrounded by eight alpha-helices
additional information
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oligomeric states of MDHs, overview
additional information
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oligomeric states of MDHs, overview
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