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x * 68000-72000
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x * 44500, SDS-PAGE
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x * 49000, recombinant enzyme expressed in Escherichia coli, SDS-PAGE
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x * 5297, calculated from amino acid sequence
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x * 53000, SDS-PAGE
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x * 5297, calculated from amino acid sequence
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x * 56000, SDS-PAGE
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x * 50000, recombinant enzyme, SDS-PAGE
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x * 50000, SDS-PAGE
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x * 14000, SDS-PAGE
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x * 58000, calculated from amino acid sequence
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x * 58000, calculated from amino acid sequence
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x * 48530, calculated from amino acid sequence
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x * 46520, calculated from amino acid sequence
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x * 46430, calculated from amino acid sequence
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x * 46430, calculated from amino acid sequence
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x * 94930, calculated from nucleotide sequence
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x * 94930, calculated from nucleotide sequence
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x * 47900, calculated from amino acid sequence
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x * 47900, calculated from amino acid sequence
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x * 47300, calculated from amino acid sequence
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x * 45000, SDS-PAGE
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x * 47300, calculated from amino acid sequence
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x * 113400, calculated from amino acid sequence
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x * 108000, truncated enzyme, SDS-PAGE
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x * 112076, calculated from amino acid sequence
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x * 108000, truncated enzyme, SDS-PAGE
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x * 112076, calculated from amino acid sequence
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x * 51400, calculated from amino acid sequence
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x * 51400, calculated from amino acid sequence
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x * 41500, calculated from amino acid sequence
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x * 48000, SDS-PAGE, native form occurs as an aggregate
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x * 47400, calculated from amino acid sequence
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x * 49000, recombinant enzyme, SDS-PAGE
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x * 49000, recombinant enzyme, SDS-PAGE
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x * 47000, SDS-PAGE
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x * 104200, calculated from amino acid sequence
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x * 104200, calculated from amino acid sequence
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x * 46800, calculated from amino acid sequence
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Q60114
x * 46000, SDS-PAGE
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x * 46000, SDS-PAGE
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dimer
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1 * 50000 + 1 * 20000, about, SDS-PAGE
dimer
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1 * 49000 + 1 * 23000, SDS-PAGE
dimer
2 * 47100, calculated from sequence
dimer
2 * 51700, enzyme including a His-tag, SDS-PAGE
dimer
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2 * 47100, calculated from sequence
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dimer
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2 * 51700, enzyme including a His-tag, SDS-PAGE
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dimer
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2 * 64000, SDS-PAGE
dimer
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2 * 64000, SDS-PAGE
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dimer
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2 * 56000, SDS-PAGE
dimer
Q60114
structure depends on ionic strength and pHs, above 7.0, products are short fructo-saccharides (degree of polymerization 3)
monomer
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1 * 52000, extracellular and membrane-associated form, SDS-PAGE
monomer
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1 * 51000, SDS-PAGE
monomer
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1 * 51000, SDS-PAGE
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monomer
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1 * 52000, extracellular and membrane-associated form, SDS-PAGE
monomer
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1 * 52000, extracellular and membrane-associated form, SDS-PAGE
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monomer
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1 * 60000, intracellular enzyme, SDS-PAGE
monomer
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1 * 60000, intracellular enzyme, SDS-PAGE
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additional information
enzyme structure comparisons, overview. The enzyme shows the five-bladed beta-propeller typical of glycoside hydrolase families 32 and 68 members
additional information
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enzyme structure comparisons, overview. The enzyme shows the five-bladed beta-propeller typical of glycoside hydrolase families 32 and 68 members
additional information
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enzyme structure comparisons, overview. The enzyme shows the five-bladed beta-propeller typical of glycoside hydrolase families 32 and 68 members
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additional information
three-dimensional structure comparison, overview
additional information
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three-dimensional structure comparison, overview
additional information
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three-dimensional structure comparison, overview
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additional information
Q60114
microfibrils, structure depends on ionic strength and pHs, below 6.0, well-ordered, precipate out of the solution, synthesis of levan (degree of polymerization greater than 20000). The fibril structure decreases the diffusion of the enzyme away from the bacteria cells, which results in the close association of the cell to the high molecular polymer, levan.
additional information
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microfibrils, structure depends on ionic strength and pHs, below 6.0, well-ordered, precipate out of the solution, synthesis of levan (degree of polymerization greater than 20000). The fibril structure decreases the diffusion of the enzyme away from the bacteria cells, which results in the close association of the cell to the high molecular polymer, levan.