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x * 56000, SDS-PAGE
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x * 56000, calculated from amino acid sequence
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x * 56000, SDS-PAGE
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x * 56000, calculated from amino acid sequence
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x * 15000, recombinant His-tagged enzyme, SDS-PAGE, x * 14740, about, sequence calculation
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x * 35860, recombinant His6-tagged truncated enzyme, SDS-PAGE
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x * 63000, recombinant full-length enzyme, SDS-PAGE, x * 34000, recombinant catalytic module CtGH43 , SDS-PAGE
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x * 35860, calculated from amino acid sequence
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x * 63000, recombinant full-length enzyme, SDS-PAGE, x * 34000, recombinant catalytic module CtGH43 , SDS-PAGE
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x * 35860, recombinant His6-tagged truncated enzyme, SDS-PAGE
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x * 36000, SDS-PAGE
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x * 35860, calculated from amino acid sequence
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x * 34700, isoform AbfI, calculated from amino acid sequence
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x * 41300, isoform AbfII, calculated from amino acid sequence
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x * 59000, mutant N83Q/N202Q, SDS-PAGE
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x * 60700, mutant N83Q, SDS-PAGE
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x * 62000, mutant N202Q, SDS-PAGE
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x * 64500, wild-type enzyme, SDS-PAGE
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x * 35500, SDS-PAGE
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x * 65334, calculated from amino acid sequence
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x * 66000, the purified recombinant abfA before and after treatment with PNGase F migrated by SDS-PAGE has relative molecular masses of about 83000 and 66000 Da, respectively
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x * 83000, the purified recombinant abfA before and after treatment with PNGase F migrated by SDS-PAGE has relative molecular masses of about 83000 and 66000 Da, respectively
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x * 65334, calculated from amino acid sequence
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x * 66000, the purified recombinant abfA before and after treatment with PNGase F migrated by SDS-PAGE has relative molecular masses of about 83000 and 66000 Da, respectively
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x * 83000, the purified recombinant abfA before and after treatment with PNGase F migrated by SDS-PAGE has relative molecular masses of about 83000 and 66000 Da, respectively
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x * 51384, calculated, x * 55000, SDS-PAGE
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x * 51384, calculated, x * 55000, SDS-PAGE
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x * 60000, recombinant isoform AXH-d3, SDS-PAGE
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x * 63000, recombinant isoform AbfA, SDS-PAGE
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x * 87000, recombinant isoform AbfB, SDS-PAGE
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x * 59300, calculated from amino acid sequence
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x * 59300, calculated from amino acid sequence
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x * 133000, recombinant His-tagged enzyme without signal peptide, SDS-PAGE, x * 132981, His-tagged enzyme without signal peptide, sequence calculation
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x * 95000, SDS-PAGE
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x * 41400, mature protein, calculated from amino acid sequence
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x * 48300, estimated from SDS-PAGE
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x * 60000, SDS-PAGE
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x * 67000, SDS-PAGE, x * 79200, about, amino acid sequence calculation
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x * 62000, GH43 alpha-L-arabinofuranosidase, SDS-PAGE
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x * 94000, GH51 alpha-L-arabinofuranosidase, SDS-PAGE
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x * 69000, GH51 alpha-L-arabinofuranosidase, SDS-PAGE
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x * 53400, calculated, x * 56000, SDS-PAGE
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x * 53400, calculated, x * 56000, SDS-PAGE
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x * 39000, SDS-PAGE
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x * 52852, calculated from amino acid sequence
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x * 53000-54000, estimated from SDS-PAGE
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x * 52852, calculated from amino acid sequence
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x * 53000-54000, estimated from SDS-PAGE
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x * 52852, calculated from amino acid sequence
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x * 53000-54000, estimated from SDS-PAGE
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x * 79000, type B enzyme AFQ1, x * 52000, type B enzyme AFS1
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x * 32827, calculated from amino acid sequence
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x * 71000, recombinant tagged enzyme, SDS-PAGE, x * 52000 untagged enzyme, SDS-PAGE, x * 49576, enzyme residues 27-506, sequence calculation
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x * 85000, recombinant tagged enzyme, SDS-PAGE, x * 79000, untagged enzyme, SDS-PAGE, x * 67496, enzyme residues 18-635, sequence calculation
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x * 79000, type B enzyme AFQ1, x * 52000, type B enzyme AFS1
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x * 85000, recombinant tagged enzyme, SDS-PAGE, x * 79000, untagged enzyme, SDS-PAGE, x * 67496, enzyme residues 18-635, sequence calculation
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x * 71000, recombinant tagged enzyme, SDS-PAGE, x * 52000 untagged enzyme, SDS-PAGE, x * 49576, enzyme residues 27-506, sequence calculation
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x * 32827, calculated from amino acid sequence
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x * 35900, calculated from amino acid sequence
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x * 35900, calculated from amino acid sequence
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x * 83000, SDS-PAGE, x * 65600, calculated
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x * 99350, His-tagged enzyme, sequence calculation
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x * 55000, SDS-PAGE
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x * 81302, calculated from amino acid sequence
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x * 85000, SDS-PAGE
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x * 80000, SDS-PAGE
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x * 81302, calculated from amino acid sequence
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x * 45248, sequence calculation, x * 31000, SDS-PAGE
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x * 45248, sequence calculation, x * 31000, SDS-PAGE
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x * 46232, calculated from amino acid sequence
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x * 35900, calculated from amino acid sequence
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x * 33148 , isozyme PcABF43A, sequence calcualtion
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x * 37100, about isozyme PfABF62a, sequence calculation, x * 35400, about isozyme PfABF62b, sequence calculation, x * 41300, about isozyme PfABF62c, sequence calculation, x * 37400, about isozyme mutant pfabf62cDELTACBM, sequence calculation
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x * 55400, calculated for mature protein, x * 68000, SDS-PAGE
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x * 56102, sequence calculation
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x * 50000, SDS-PAGE
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x * 67840, His-tagged enzyme, sequence calculation
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x * 67840, His-tagged enzyme, sequence calculation
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x * 28400, isoform Abf5, x * 24500, isoform Abf6, calculated
dimer
2 * 58000, SDS-PAGE
dimer
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2 * 58000, SDS-PAGE
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dimer
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1 * 52500 + 1 * 57500, SDS-PAGE
dimer
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1 * 52500 + 1 * 57500, SDS-PAGE
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dimer
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2 * 46000, SDS-PAGE
hexamer
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anion exchange chromatography
hexamer
6 * 59500, recombinant enzyme, SDS-PAGE
hexamer
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6 * 59500, recombinant enzyme, SDS-PAGE
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hexamer
6 * 57218, calculated from sequence
hexamer
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6 * 57218, calculated from sequence
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hexamer
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6 * 61000, SDS-PAGE
hexamer
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6 * 69000, SDS-PAGE
hexamer
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6 * 69000, SDS-PAGE
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hexamer
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small angle X-ray scattering
hexamer
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small angle X-ray scattering
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homodimer
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2 * 37000, SDS-PAGE
homodimer
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2 * 37000, SDS-PAGE
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homodimer
2 * 40000, SDS-PAGE
homodimer
2 * 39768, calculated from amino acid sequence
homooctamer
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8 * 58000, SDS-PAGE
homooctamer
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8 * 57882, calculated from amino acid sequence
homotetramer
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4 * 40000, SDS-PAGE
homotetramer
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4 * 39784, calculated from amino acid sequence
homotetramer
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4 * 40000, SDS-PAGE
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homotetramer
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4 * 39784, calculated from amino acid sequence
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monomer
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1 * 80000, SDS-PAGE
monomer
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1 * 33000, strain 3M43, SDS-PAGE
monomer
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1 * 33000, strain 3M43, SDS-PAGE
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monomer
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1 * 34300, SDS-PAGE
monomer
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1* 41000-43000 SDS-PAGE, gel filtration
monomer
1 * 49000, SDS-PAGE
monomer
1 * 49900, calculated from sequence
monomer
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1 * 49000, SDS-PAGE
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monomer
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1 * 49900, calculated from sequence
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monomer
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1 * 60000, SDS-PAGE
monomer
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1 * 60000, SDS-PAGE
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monomer
1 * 52900, SDS-PAGE
monomer
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1 * 52900, SDS-PAGE
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monomer
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1 * 90000, SDS-PAGE
monomer
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Arb93A has a six-bladed beta-propeller fold
monomer
1 * 81500, SDS-PAGE
monomer
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1 * 58000, SDS-PAGE
monomer
1 * 70000, SDS-PAGE
monomer
1 * 47305, mature protein, calculated from amino acid sequence
monomer
1 * 50700, deduced from SDS-PAGE
monomer
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1 * 47305, mature protein, calculated from amino acid sequence
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monomer
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1 * 50700, deduced from SDS-PAGE
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monomer
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1 * 35000, SDS-PAGE
octamer
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octamer
8 * 57882, sequence calculation, 8 * 58000, recombinant enzyme, SDS-PAGE
oligomer
higher than the tetramer, subunit mass 58000
oligomer
two oligomeric forms are observed, the dimer (116 kDa) and an oligomer with a higher-order structure than the tetramer, subunit mass 58000
oligomer
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two oligomeric forms are observed, the dimer (116 kDa) and an oligomer with a higher-order structure than the tetramer, subunit mass 58000
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tetramer
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4 * 56000-60000, SDS-PAGE
tetramer
4 * 64000, SDS-PAGE
tetramer
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4 * 64000, SDS-PAGE
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tetramer
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4 * 64000, SDS-PAGE
tetramer
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4 * 64000, SDS-PAGE
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tetramer
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4 * 64000, SDS-PAGE
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tetramer
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4 * 72000, SDS-PAGE
tetramer
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4 * 72000, SDS-PAGE
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tetramer
4 * 56520, sequence calculation, 4 * 57000, recombinant His-tagged enzyme, SDS-PAGE
tetramer
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4 * 56520, sequence calculation, 4 * 57000, recombinant His-tagged enzyme, SDS-PAGE
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tetramer
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4 * 59000, SDS-PAGE
tetramer
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4 * 59000, SDS-PAGE
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tetramer
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4 * 75000, SDS-PAGE
tetramer
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4 * 75000, SDS-PAGE
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tetramer
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4 * 82000, SDS-PAGE
tetramer
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4 * 82000, SDS-PAGE
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tetramer
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4 * 52000, SDS-PAGE
additional information
the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus. Circular dichroism analysis of catalytic domain CtGH43 shows 48% beta-sheets, 49% random coils but only 3% alpha-helices
additional information
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the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus. Circular dichroism analysis of catalytic domain CtGH43 shows 48% beta-sheets, 49% random coils but only 3% alpha-helices
additional information
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the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus. Circular dichroism analysis of catalytic domain CtGH43 shows 48% beta-sheets, 49% random coils but only 3% alpha-helices
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additional information
the enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, mechanisms associated with the unfolding process by molecular dynamics simulations, important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
additional information
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the enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, mechanisms associated with the unfolding process by molecular dynamics simulations, important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
additional information
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the enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, mechanisms associated with the unfolding process by molecular dynamics simulations, important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
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additional information
each subunit is composed of 2 domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with jelly-roll topology
additional information
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each subunit is composed of 2 domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with jelly-roll topology
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additional information
three-dimensional structure, overview
additional information
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three-dimensional structure, overview
additional information
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molecular weight 404000, subunit mass about 79000 Da, SDS-PAGE
additional information
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enzyme domain structure: genes PfabfB1, PfabfB2, PfabfB3, and PfabfB4 all encode for a AbfB catalytic domain, genes PfabfB1, PfabfB2, and PfabfB3 also code for an ABD arabinose-binding domain, while PfabfB4 lacks this domain but harbors a CBD fungal cellulose-binding domain and a LCR low-complexity region instead, overview
additional information
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three-dimensional structure of the enzyme, overview
additional information
the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview
additional information
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the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview
additional information
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the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview
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additional information
three-dimensional structure, overview
additional information
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three-dimensional structure, overview
additional information
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three-dimensional structure, overview
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3.2.1.55 non-reducing end alpha-L-arabinofuranosidase
results (
results (
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