3.2.1.156: oligosaccharide reducing-end xylanase
This is an abbreviated version!
For detailed information about oligosaccharide reducing-end xylanase, go to the full flat file.
Word Map on EC 3.2.1.156
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3.2.1.156
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glycoside
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xylooligosaccharides
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xylanases
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halodurans
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subsite
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adolescentis
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xylotriose
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bifidobacterium
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pseudoalteromonas
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glycosynthase
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haloplanktis
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glucuronoxylan
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prebiotic
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endo-xylanase
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xylopentaose
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hemicelluloses
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xylohexaose
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xylosidase
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arabinoxylan
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deconstruction
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beechwood
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xylotetraose
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heteroxylans
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paenibacillus
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biotechnology
- 3.2.1.156
- glycoside
- xylooligosaccharides
- xylanases
- halodurans
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subsite
- adolescentis
- xylotriose
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bifidobacterium
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pseudoalteromonas
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glycosynthase
- haloplanktis
- glucuronoxylan
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prebiotic
- endo-xylanase
- xylopentaose
- hemicelluloses
- xylohexaose
- xylosidase
- arabinoxylan
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deconstruction
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beechwood
- xylotetraose
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heteroxylans
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paenibacillus
- biotechnology
Reaction
+ = 2 beta-D-xylopyranosyl-(1-4)-alpha-D-xylopyranose
Synonyms
BaRex8A, BhRex8A, DFQ00_11062, GH8 xylanase, More, oligosaccharide reducing-end xylanase, PhXyl, reducing end xylose-releasing exo-oligoxylanase, reducing-end xylose-releasing exo-oligoxylanase, reducing-end xylose-releasing exooligoxylanase, Rex, Rex8A, RexA, rXyn8, XYLA
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General Information
General Information on EC 3.2.1.156 - oligosaccharide reducing-end xylanase
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evolution
physiological function
additional information
the enzyme belongs to the glycoside hydrolase family 8, GH8
evolution
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the enzyme belongs to the glycoside hydrolase family 8, GH8
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evolution
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the enzyme belongs to the glycoside hydrolase family 8, GH8
-
evolution
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the enzyme belongs to the glycoside hydrolase family 8, GH8
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Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
physiological function
Halalkalibacterium halodurans
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
physiological function
the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts
physiological function
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Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
Halalkalibacterium halodurans DSM 181973
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Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
-
the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
-
physiological function
-
the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts
-
physiological function
-
the enzyme is involved in depolymerization of glucuronoxylan, a major component of the lignocellulosic substrates. Rex8A is a reducing-end xylose-releasing exo-oligoxylanase that efficiently hydrolyzes xylose from neutral and acidic xylooligosaccharides generated by the action of other xylanases also secreted by the strain. The hydrolytic ability of Rex8A on branched oligomers can be crucial for the complete depolymerization of highly substituted xylans, which is indispensable to accomplish biomass deconstruction and to generate efficient catalysts
-
physiological function
-
Rex8As are key enzymes in the efficient saccharification of heteroxylan into xylose, a major component of lignocellulosic substrates
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three conserved catalytic residues are Glu90, Asp148, and Asp286
additional information
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A
additional information
-
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A
additional information
-
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A
-
additional information
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three conserved catalytic residues are Glu90, Asp148, and Asp286
-
additional information
-
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A
-
additional information
-
modeling of the three-dimensional structure of Rex8A shows an (alpha/alpha)6 barrel fold where the loops connecting the alpha-helices contour the active site. These loops, which show high sequence diversity among GH8 enzymes, shape a catalytic cleft with a -2 subsite that can accommodate methyl-glucuronic acid decorations. Putative proton donor is Glu70 and catalytic base is Asp265. Residues Leu320, His321, and Pro322 form the loop structure. Structural molecular modeling of Rex8A
-