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dimer or oligomer
the CS4 isoform is not only present as dimer but also as high-molecular-weight oligomer under native conditions
octamer
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8 * 55001, calculated from sequence, 8 * 70000, SDS-PAGE of recombinant protein
?
x * 52200, deduced from amino acid sequence
?
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x * 52200, deduced from amino acid sequence
-
?
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x * 48000, glyoxysomal isozyme, SDS-PAGE
?
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x * 51100, calculated from sequence
?
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x * 42000, SDS-PAGE
-
?
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x * 33200, calculated from amino acid sequence
?
x * 26300, calculated from sequence
?
x * 42679, calculated from sequence
?
-
x * 42679, calculated from sequence
-
?
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x * 49000, SDS-PAGE
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dimer
crystallization data
dimer
2 * 48000, mitochondrial enzyme, SDS-PAGE
dimer
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2 * 48000, mitochondrial enzyme, SDS-PAGE
-
dimer
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2 * 48700, SDS-PAGE
dimer
2 * 44162.7, MALDI-TOF, 2 * 43000, SDS-PAGE
dimer
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2 * 40300, SDS-PAGE, gel filtration in guanidine-HCl, amino acid composition
dimer
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2 * 40300, SDS-PAGE, gel filtration in guanidinium chloride
dimer
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2 * 40300, SDS-PAGE, gel filtration in guanidine-HCl, amino acid composition
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dimer
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2 * 40300, SDS-PAGE, gel filtration in guanidinium chloride
-
dimer
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2 * 36500, CS II, SDS-PAGE
dimer
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isoenzyme CSII 2 * 42000, SDS-PAGE
dimer
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2 * 36500, CS II, SDS-PAGE
-
dimer
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isoenzyme CSII 2 * 42000, SDS-PAGE
-
dimer
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2 * 53000, SDS-PAGE, CS I, reassociation to CS II possible
dimer
-
2 * 42600, SDS-PAGE
dimer
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2 * 42000, dimeric enzyme form, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 50000, CS II, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
-
dimer
-
2 * 43000, SDS-PAGE
hexamer
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6 * 48000, SDS-PAGE
hexamer
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6 * 47000, SDS-PAGE, or homopentamer
hexamer
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6 * 44000, SDS-PAGE, 6 * 49000, guanidine-HCl gel filtration
hexamer
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6 * 46000, SDS-PAGE, amino-terminal amino acid sequence
hexamer
-
6 * 44700, SDS-PAGE
hexamer
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6 * 44700, SDS-PAGE
-
hexamer
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6 * 42000, CS i, SDS-PAGE
hexamer
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isoenzyme CSI 6 * 37500, SDS-PAGE
hexamer
-
6 * 42000, CS i, SDS-PAGE
-
hexamer
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isoenzyme CSI 6 * 37500, SDS-PAGE
-
hexamer
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6 * 53000, SDS-PAGE, CS II
hexamer
-
6 * 45000, hexameric enzyme form
homodimer
2 * 52000, SDS-PAGE
homodimer
2 * 43290, calculated from amino acid sequence
homodimer
2 * 48000, SDS-PAGE
homodimer
2 * 49868, MALDI-TOF mass spectrometry
homodimer
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2 * 48000, SDS-PAGE
-
homodimer
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2 * 49868, MALDI-TOF mass spectrometry
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homodimer
2 * about 50000
homohexamer
6 * 47885, calculated from amino acid sequence
homohexamer
6 * 28000, SDS-PAGE
tetramer
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4 * 69000, sedimentation equilibrium in guanidine-HCl and dithiothreitol
tetramer
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4 * 58500, sedimentation equilibrium in guanidine-HCl and dithiothreitol
tetramer
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4 * 58500, sedimentation equilibrium in guanidine-HCl and dithiothreitol
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tetramer
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4 * 66000, SDS-PAGE
additional information
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recombinant chimeric enzymes, domain functions, subunit organisation
additional information
subunit organization and crystal structure, amino acid residues involved in subunit interaction
additional information
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subunit organization and crystal structure, amino acid residues involved in subunit interaction
additional information
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recombinant chimeric enzymes, domain functions, subunit organisation
additional information
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CS I expressed from different structural gene than CS II
additional information
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CS I expressed from different structural gene than CS II
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additional information
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chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity
additional information
subunit organisation from crystal structure, dimer
additional information
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additional information
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-
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additional information
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additional information
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chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity
additional information
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inter-subunit ionic network, molecular modeling