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?
x * 45000, calcuated
?
-
x * 60000, SDS-PAGE, x * 61200, calculated
?
-
x * 60000, recombinant enzyme, SDS-PAGE, x * 61200, about, sequence calculation
?
-
x * 45000, calcuated
-
?
-
x * 69000, SDS-PAGE
-
?
-
x * 69000, SDS-PAGE
-
?
-
x * 22630-22165, SDS-PAGE and mass spectrometry
?
-
x * 22630-22165, SDS-PAGE and mass spectrometry
-
?
x * 42500, about, sequence calculation
?
x * 131500, calculated, x * 130000, SDS-PAGE
?
-
x * 131500, calculated, x * 130000, SDS-PAGE
-
?
x * 21000, SDS-PAGE, x * 24000, claculated
?
x * 20200, extracellular enzyme, SDS-PAGE
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 32200, SDS-PAGE
-
?
-
x * 20200, extracellular enzyme, SDS-PAGE
-
?
-
x * 24500, mass spectrometry, x* 25000, SDS-PAGE
?
-
x * 24500, mass spectrometry, x* 25000, SDS-PAGE
-
?
-
x * 21000, xylanase I, x * 24000, xylanase II, SDS-PAGE
?
-
x * 25100, native enzyme, SDS-PAGE
?
-
x * 25100, native enzyme, SDS-PAGE
-
?
x * 23000, SDS-PAGE, x * 23300, calculated
?
-
x * 23000, SDS-PAGE, x * 23300, calculated
-
?
-
x * 34000, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 33000, SDS-PAGE
-
?
-
x * 38000, native extracellular enzyme, SDS-PAGE
?
-
x * 38000, native extracellular enzyme, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 45000, recombinant enzyme, SDS-PAGE
?
-
x * 44700, recombinat enzyme, calculation from nucleotide sequence
?
-
x * 21500, enzyme component I from strain W1, SDS-PAGE
?
-
x * 22500, enzyme component II from strain W1, SDS-PAGE
?
-
x * 19000, native enzyme, SDS-PAGE
?
-
x * 23475, calculated
-
?
-
x * 20000, SDS-PAGE
-
?
-
x * 45000, recombinant enzyme, SDS-PAGE
-
?
-
x * 44700, recombinat enzyme, calculation from nucleotide sequence
-
?
-
x * 24000, SDS-PAGE
-
?
-
x * 99000, SDS-PAGE
-
?
-
x * 23000, SDS-PAGE
-
?
-
x * 19000, native enzyme, SDS-PAGE
-
?
-
x * 23253, sequence calculation, x * 23000, SDS-PAGE
?
-
x * 21400, SDS-PAGE
-
?
-
x * 23253, sequence calculation, x * 23000, SDS-PAGE
-
?
-
x * 35000, SDS-PAGE
-
?
-
x * 32000, SDS-PAGE
-
?
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
?
x * 49800, about, sequence calculation, mature enzyme protein
?
x * 32500, purified mature enzyme, SDS-PAGE, x * 64960, unprocessed enzyme, amino acid sequence calculation
?
-
x * 56000, wild-type and mutant strain enzyme, SDS-PAGE
?
-
x * 49000, SDS-PAGE
-
?
-
x * 56000, wild-type and mutant strain enzyme, SDS-PAGE
-
?
-
x * 38000, SDS-PAGE
-
?
-
x * 29000, SDS-PAGE
-
?
x * 39000, SDS-PAGE, x * 42925, calculated
?
-
x * 39000, SDS-PAGE, x * 42925, calculated
-
?
x * 34441, sequence calculation, x * 37000, recombinant extracellular His- and c-myc-tagged enzyme, SDS-PAGE
?
x * 49000, about, sequence calculation
?
-
x * 21200, SDS-PAGE
-
?
Halalkalibacterium halodurans
x * 45000, SDS-PAGE
?
Halalkalibacterium halodurans
-
x * 24000, SDS-PAGE
?
Halalkalibacterium halodurans PPKS-2
-
x * 24000, SDS-PAGE
-
?
Halalkalibacterium halodurans TSEV1
-
x * 45000, SDS-PAGE
-
?
-
x * 21000, xylanase 2, SDS-PAGE
?
-
x * 6000, xylanase 1, SDS-PAGE
?
-
x * 24000, Xyl16-3, SDS-PAGE, x * 53000, Xylam, SDS-PAGE, x * 65000, Xyl1-3, SDS-PAGE, x * 90000, Xyl6-6, SDS-PAGE
?
x * 49000, SDS-PAGE, recombinant protein, x * 50480, calculated
?
-
x * 30000, xylanase B, SDS-PAGE
?
-
x * 21000, xylanase A, SDS-PAGE
?
x * 45000, SDS-PAGE, x * 43170, calculated
?
-
x * 24000, SDS-PAGE, isoform xylanase IIIA
?
-
x * 38000, SDS-PAGE, isoform xylanase IA
?
-
x * 68000, SDS-PAGE
-
?
-
x * 42000, SDS-PAGE
-
?
-
x * 86000, SDS-PAGE
-
?
-
x * 41584, calculated
-
?
-
x * 21000, SDS-PAGE
-
?
-
x * 48000, SDS-PAGE
-
?
x * 25827, mutant N38Y/F52W/G56Y/G201L, calculated, x * 25800, SDS-PAGE
?
x * 26000, recombinantenzyme, SDS-PAGE
?
-
x * 26000, recombinantenzyme, SDS-PAGE
-
?
-
x * 33000, xylanase I, SDS-PAGE
?
-
x * 30000, xylanase II, SDS-PAGE
?
-
x * 33000, xylanase I, SDS-PAGE
-
?
-
x * 30000, xylanase II, SDS-PAGE
-
?
x * 26132, XynA, sequence calculation, x * 28000, XynA, SDS-PAGE
?
-
x * 26132, XynA, sequence calculation, x * 28000, XynA, SDS-PAGE
-
?
-
x * 41000, SDS-PAGE
-
?
-
x * 53400, calculated, x * 56000, SDS-PAGE
?
-
x * 53400, calculated, x * 56000, SDS-PAGE
-
?
-
x * 39000, SDS-PAGE
-
?
-
x * 20200, SDS-PAGE
-
?
-
x * 156700, calculated
-
?
x * 20000, SDS-PAGE, x * 20674, calculated
?
x * 20000, recombinant extracellular deglycosylated enzyme, SDS-PAGE, x * 60000, above, recombinant extracellular glycosylated enzyme, SDS-PAGE
?
-
x * 20000, SDS-PAGE, x * 20674, calculated
-
?
-
x * 20000, recombinant extracellular deglycosylated enzyme, SDS-PAGE, x * 60000, above, recombinant extracellular glycosylated enzyme, SDS-PAGE
-
?
-
x * 21300, recombinant XynB, SDS-PAGE and sequence calculation
?
-
x * 21300, SDS-PAGE
-
?
-
x * 22000, Xyn3, SDS-PAGE, x * 21730, Xyn3, sequence calculation
?
-
x * 22000, Xyn3, SDS-PAGE, x * 21730, Xyn3, sequence calculation
-
?
x * 21500, about, sequence calculation
?
-
x * 41600, isoform xynA, x * 28600, isoform xynB, x * 40300, isoform xynC, calculated, x * 52000, isoform xynA, x * 50000, isoform xynB, x * 32000, isoform xynC, SDS-PAGE
?
x * 55000, recombinant enzyme, SDS-PAGE, x * 40000, about, sequence calculation
?
x * 42200, calculated from sequence
?
-
x * 43000, SDS-PAGE
-
?
-
x * 42200, calculated from sequence
-
?
Pomacea insularus
-
x * 47000, SDS-PAGE
?
x * 45982, mass spectrometry
?
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 43000, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 40531, calculated, x * 40000, SDS-PAGE
?
-
x * 40531, calculated, x * 40000, SDS-PAGE
-
?
-
x * 33500, about, PhX33, mass spectrometry, x * 20100, about, PhX20, mass spectrometry
?
-
x * 33500, about, PhX33, mass spectrometry, x * 20100, about, PhX20, mass spectrometry
-
?
x * 38800, calculated, x * 47000, SDS-PAGE, His-tagged protein
?
-
x * 76000, xylanase X-a, SDS-PAGE
?
-
x * 54000, xylanase X-b-I, SDS-PAGE
?
-
x * 45000, xylanase X-b-II, SDS-PAGE
?
-
x * 76000, xylanase X-a, SDS-PAGE
-
?
-
x * 54000, xylanase X-b-I, SDS-PAGE
-
?
-
x * 45000, xylanase X-b-II, SDS-PAGE
-
?
-
x * 27000, SDS-PAGE
-
?
-
x * 85000, SDS-PAGE
-
?
x * 37300, calculated from sequence
?
-
x * 57000, SDS-PAGE
-
?
-
x * 37300, calculated from sequence
-
?
-
x * 36000, SDS-PAGE
-
?
-
x * 30500, isoform XynB, x * 30000, XynC, SDS-PAGE
?
1 * 42800, SDS-PAGE, 1 * 35000, SDS-PAGE. Heavier protein band (42.8 kDa) is observed after 12 h of culture, while the lighter band (35 kDa) appears 12 h later
?
-
1 * 42800, SDS-PAGE, 1 * 35000, SDS-PAGE. Heavier protein band (42.8 kDa) is observed after 12 h of culture, while the lighter band (35 kDa) appears 12 h later
-
?
x * 45000, SDS-PAGE, x * 47000, calculated
?
-
x * 45000, SDS-PAGE, x * 47000, calculated
-
?
MK331807
x * 44000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
-
?
-
x * 24500, Xyl1, SDS-PAGE, x * 37500, Xyl2, SDS-PAGE, x * 38000, Xyl3, SDS-PAGE
?
x * 47000, SDS-PAGE, XynAS27. x * 33000, SDS-PAGE, XynAS27cd. x * 34000, SDS-PAGE, XynAS27cdl
?
-
x * 24500, Xyl1, SDS-PAGE, x * 37500, Xyl2, SDS-PAGE, x * 38000, Xyl3, SDS-PAGE
-
?
x * 38000, recombinant enzyme, SDS-PAGE
?
x * 43962, sequence calculation
?
-
x * 43962, sequence calculation
-
?
x * 43000, SDS-PAGE, x * 25902, calculated, x * 29949-34912, ESI-MS
?
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
?
-
x * 30000, isozyme I, SDS-PAGE, x * 25500, isozyme II, SDS-PAGE, x * 33500, isozyme III, SDS-PAGE
?
x * 51000, SDS-PAGE of N-deglycosylated protein, x * 42000, calculated
?
x * 40997, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
?
-
x * 40997, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
-
?
-
x * 27000, SDS-PAGE
-
?
Thermochaetoides thermophila
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
?
Thermochaetoides thermophila CBS 144.50
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila DSM 1495
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila IMI 039719
-
x * 47000, about, sequence calculation, x * 48000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
-
x * 44377, calculation from nucleotide sequence
?
-
x * 54000, recombinant xylanase A produced in Escherichia coli, SDS-PAGE
?
-
x * 54000, recombinant xylanase A produced in Escherichia coli, SDS-PAGE
-
?
Thermomonospora sp.
-
x * 38000
?
x * 21900-22300, recombinant enzyme, SDS-PAGE
?
x * 21900 or x * 22100 or x * 22300, mass spectrometry of recombinant protein with variability in the amino terminus, x * 26900, SDS-PAGE
?
-
x * 21900-22300, recombinant enzyme, SDS-PAGE
-
?
-
x * 21300, SDS-PAGE
-
?
-
x * 24700, SDS-PAGE
-
?
-
x * 23600, SDS-PAGE
-
?
-
x * 82000, SDS-PAGE
-
?
-
x * 119642, calculated
?
-
x * 26000, mutant hybrid enzyme, SDS-PAGE
?
-
x * 29000, the enzyme also exists as a 20000 Da enzyme form, SDS-PAGE
?
-
x * 20000, the enzyme also exists as a 29000 Da enzyme form, SDS-PAGE
?
-
x * 18600, SDS-PAGE
-
?
-
x * 32000, xylanase I, SDS-PAGE
?
-
x * 23000, xylanase II, SDS-PAGE
?
-
x * 21000-22000, native wild-type enzyme, SDS-PAGE, x * 25000, recombinant wild-type enzyme, SDS-PAGE
?
B2CNY5
x * 21000, recombinant enzyme, SDS-PAGE
?
-
x * 20000-21000, recombinant wild-type enzyme, SDS-PAGE, x * 26000, mutant hybrid enzyme, SDS-PAGE
?
B2CNY5
x * 21000, recombinant His-tagged mature enzyme without N-terminal signal sequence, SDS-PAGE
?
-
x * 21000, Xyn2, SDS-PAGE
?
-
x * 20000-21000, recombinant wild-type enzyme, SDS-PAGE, x * 26000, mutant hybrid enzyme, SDS-PAGE
-
?
-
x * 21000, recombinant enzyme, SDS-PAGE
-
?
-
x * 30100, isozyme EX1, SDS-PAGE, x * 20100, isozyme EX2, SDS-PAGE
?
-
x * 30100, isozyme EX1, SDS-PAGE, x * 20100, isozyme EX2, SDS-PAGE
-
?
-
x * 71300, calculated, x * 80000, SDS-PAGE
?
x * 55000, wild-type, x * 28000, mutant XylA, x * 40000, mutant XylB, x * 26000, mutant XylC, SDS-PAGE
?
multimodular enzyme consisting of a catalytic domain and two tandem carbohydrate-binding modules (CBM36)
?
x * 60600, about, sequence calculation
dimer
-
2 * 27500, SDS-PAGE
dimer
-
2 * 27500, SDS-PAGE
-
dimer
-
2 * 49800, xylanase II
monomer
Acacia verek
-
1 * 60000, SDS-PAGE
monomer
1 * 63000, SDS-PAGE, recombinant EGXA
monomer
-
1 * 27000, isoform xyl I, 1 * 17700, isoform xylII, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
-
monomer
-
1 * 48000, SDS-PAGE
monomer
-
x * 32000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
-
monomer
-
1 * 56000, SDS-PAGE
monomer
-
1 * 50000, enzyme component II from strain W2, SDS-PAGE
monomer
-
1 * 49500, enzyme component II from strain W1, SDS-PAGE
monomer
-
1 * 56000, SDS-PAGE
-
monomer
1 * 20000, SDS-PAGE and HPLC
monomer
-
1 * 20000, SDS-PAGE and HPLC
-
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
-
monomer
1 * 49000, SDS-PAGE
monomer
-
1 * 49000, SDS-PAGE
-
monomer
-
1 * 65000, xylanase A, SDS-PAGE
monomer
-
1 * 29900, xylanase B, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 23000, SDS-PAGE
-
monomer
-
1 * 22400, SDS-PAGE
monomer
-
1 * 22400, SDS-PAGE
-
monomer
-
1 * 43000, SDS-PAGE
monomer
-
1 * 43000, SDS-PAGE
-
monomer
-
1 * 70000, SDS-PAGE, 1 * 69300, LabChip microfluidic system
monomer
1 * 43500, SDS-PAGE
monomer
-
1 * 43500, SDS-PAGE
-
monomer
-
1 * 22900, isozyme Ia, SDS-PAGE, 1 * 20700, isozyme Ib, SDS-PAGE, 1 * 18600, isozyme Ic, SDS-PAGE, 1 * 31300, isozyme IIa, SDS-PAGE, 1 * 25400, isozyme IIb, SDS-PAGE, 1 * 38500, isozyme IIc, SDS-PAGE, 1 * 34300, isozyme IId, SDS-PAGE
monomer
-
1 * 22900, isozyme Ia, SDS-PAGE, 1 * 20700, isozyme Ib, SDS-PAGE, 1 * 18600, isozyme Ic, SDS-PAGE, 1 * 31300, isozyme IIa, SDS-PAGE, 1 * 25400, isozyme IIb, SDS-PAGE, 1 * 38500, isozyme IIc, SDS-PAGE, 1 * 34300, isozyme IId, SDS-PAGE
-
monomer
-
1 * 38000, SDS-PAGE
monomer
-
1 * 38000, SDS-PAGE
-
monomer
1 * 31600, SDS-PAGE
monomer
-
1 * 31600, SDS-PAGE
-
monomer
-
1 * 23900, xylanase I, SDS-PAGE, 1 * 33100, xylanase II, SDS-PAGE
monomer
-
1 * 54200, xylanase III
monomer
-
1 * 58800, gel filtration
monomer
-
1 * 58800, gel filtration
-
monomer
-
1 * 21000, SDS-PAGE
monomer
1 * 47000, SDS-PAGE
monomer
-
1 * 45500, SDS-PAGE
monomer
-
1 * 45500, SDS-PAGE
-
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 50000, xylanase X-I, SDS-PAGE
monomer
-
1 * 25000, xylanase X-II-A and X-II-B, SDS-PAGE
monomer
-
1 * 26400, SDS-PAGE
monomer
-
1 * 26400, SDS-PAGE
-
monomer
-
1 * 44000, SDS-PAGE
-
monomer
-
1 * 50000, xylanase X-I, SDS-PAGE
-
monomer
-
1 * 25000, xylanase X-II-A and X-II-B, SDS-PAGE
-
monomer
1 * 46000, SDS-PAGE
monomer
-
1 x * 12000, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
-
monomer
Thermochaetoides thermophila
1 * 29300, sequence analysis, 1 * 30000, SDS-PAGE
monomer
Thermochaetoides thermophila NIBGE 1
-
1 * 29300, sequence analysis, 1 * 30000, SDS-PAGE
-
monomer
-
1 * 44000, xylanase A, SDS-PAGE
monomer
-
1 * 44000, xylanase C, SDS-PAGE
monomer
-
1* 72000, xylanase B, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
monomer
-
1 * 24000, SDS-PAGE
monomer
-
1 * 27500, SDS-PAGE
monomer
-
1 * 21500, SDS-PAGE
monomer
-
1 * 22000, wild-type enzyme, SDS-PAGE, 1 * 24000, mutant enzyme, SDS-PAGE
monomer
-
1 * 27500, SDS-PAGE
-
monomer
1 * 41100, SDS-PAGE
additional information
homology modeling, enzyme XYL1p has the overall fold typical to family 11 xylanases, comparison of XYL1 structure with other homologous acidophilic, neutrophilic and alkalophilic xylanases, overview
additional information
secondary structure comparisons, overview
additional information
-
secondary structure comparisons, overview
-
additional information
-
secondary structure comparisons, overview
-
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
-
additional information
-
two protein bands are detected by SDS-PAGE: 18400 Da and 19600 Da
additional information
structure homology modelling of wild-type and mutant enzymes, overview
additional information
-
bi-modular enzyme comprising a GH10 catalytic module and a family 15 carbohydrate-binding module, crystallization data
additional information
Mxyn10 contains a catalytic domain from positions 36 to 339 and a carbohydrate-binding module at the C-terminus. Glu163 and Glu271 are the most likely residues located in the catalytic site of Mxyn10
additional information
-
secondary structure analysis, enzyme contains 10-15% alpha-helices at pH 6.0 and 35°C, portion of alpha-helix is pH-dependent
additional information
Halalkalibacterium halodurans
the enzyme has the common eightfold TIM-barrel structure of family 10 xylanases, however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft, structure comparisons, overview
additional information
Halalkalibacterium halodurans S7
-
the enzyme has the common eightfold TIM-barrel structure of family 10 xylanases, however, unlike non-alkaline active xylanases, it has a highly negatively charged surface and a deeper active site cleft, structure comparisons, overview
-
additional information
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
-
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
additional information
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
-
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
additional information
-
the enzyme possesses an N-terminal catalytic glycosyl hydrolase family 11 (GH-11) domain and and a C-terminal CBM 2 domain, tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview. The XYN11Ks_480 endo-1,4-beta-xylanase has a compact globular structure with a single alpha-helix and two extended pleated beta-sheets that formed a jelly-roll fold. The main feature is the presence of a long cleft that spanned the entire molecule. This cleft contains a site of activity that included two glutamate residues that directly participate in xylan hydrolysis wherein one acts as an acid/base (position 165) catalyst and the other acts as a nucleophile (position 273)
-
additional information
-
tertiary structural homology modeling and the three-dimensional structure of the xylanase, overview
-
additional information
catalytic residues are Glu78 and Glu172
additional information
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
additional information
-
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
additional information
-
XynBE18 structure-function relationship, homology modeling and molecular dynamic simulation, overview
additional information
-
XynB structure homology molecular modelling, overview
additional information
-
Xyn3 homology modelling
additional information
-
Xyn3 homology modelling
-
additional information
-
PhX33 contains predominant alpha-and, while PhX22 contains predominantly beta-sheets
additional information
-
PhX33 contains predominant alpha-and, while PhX22 contains predominantly beta-sheets
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additional information
XynA19 contains a complete GH10 catalytic domain of GH 10 from Ile38 to Ala381, structure homology modeling of the recombinant enzyme, overview
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(beta/alpha)8 barrel with 2 catalytic functions, the acid/base and the nucleophile, at the C-terminal side
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enzyme N-terminal structure analysis and homology modelling, overview
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structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling
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structure homology modelling, XylG folds to form an (alpha/beta)8-barrel with two catalytic residues of an acid/base Glu181 and a nucleophile Glu289. The formation of a disulfide bond between Cys321 and Cys327 is predicted by homology modeling
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additional information
the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
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the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
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the enzyme XynD consists of 387 amino acid residues with an N-terminal catalytic module, a linker rich in Ser and Thr residues, and a C-terminal family 1 carbohydrate-binding module
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additional information
enzyme three-dimensional structure analysis
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enzyme three-dimensional structure analysis
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enzyme three-dimensional structure analysis
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enzyme three-dimensional structure analysis
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a 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
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a 38000 Da enzyme form and a 48000 Da enzyme form are detected by SDS-PAGE. The 38000 Da enzyme form does not contain the cellulose-binding domain
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additional information
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enzyme N-terminal structure analysis and homology modelling, overview
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Thermomonospora sp.
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the enzyme is composed of 38% alpha-helix and 10% beta-sheet
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modeled structure of full-length XYN10A xylanase, overview
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enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data
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enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data
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additional information
domain composition, the enzyme contains an N-termminal domain D1 which is the xylan-binding domain XBD, it is homologous to noncatalytic thermostabilizing domains of other xylanases, D1 is followed by the catalytic D2 domain, and 2 cellulose-binding domains D3 and D4, the latter linked via a proline-threonine-rich sequence