ArticleApplied and environmental microbiology2012
Modular glucuronoxylan-specific xylanase with a family CBM35 carbohydrate-binding module.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Enzymatic Production of Prebiotic Xylooligosaccharides Using aJournal of agricultural and food chemistry · 2026Article
- Functional identification of two novel carbohydrate-binding modules of glucuronoxylanase CrXyl30 and their contribution to the lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2023Article
- The first crystal structure of a xylobiose-bound xylobiohydrolase with high functional specificity from the bacterial glycoside hydrolase family 30, subfamily 10.FEBS letters · 2022Article
- Catalytic Diversity of GH30 Xylanases.Molecules (Basel, Switzerland) · 2021Article
- Carbohydrate-binding modules targeting branched polysaccharides: overcoming side-chain recalcitrance in a non-catalytic approach.Bioresources and bioprocessing · 2021Review
- A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum.Applied microbiology and biotechnology · 2021Article
- CaXyn30B from the solventogenic bacterium Clostridium acetobutylicum is a glucuronic acid-dependent endoxylanase.BMC research notes · 2020Article
- Substrate recognition by a bifunctional GH30-7 xylanase B from Talaromyces cellulolyticus.FEBS open bio · 2020Article
- A predator-prey interaction between a marine Pseudoalteromonas sp. and Gram-positive bacteria.Nature communications · 2020Article
- GH30-7 Endoxylanase C from the Filamentous FungusApplied and environmental microbiology · 2019Article
- Mode of Action of GH30-7 Reducing-End Xylose-Releasing Exoxylanase A (Xyn30A) from the Filamentous Fungus Talaromyces cellulolyticus.Applied and environmental microbiology · 2019Article
- Structural and functional characterization of a bifunctional GH30-7 xylanase B from the filamentous fungusThe Journal of biological chemistry · 2019Article
- A novel fungal GH30 xylanase with xylobiohydrolase auxiliary activity.Biotechnology for biofuels · 2019Article
- Fiber-associated spirochetes are major agents of hemicellulose degradation in the hindgut of wood-feeding higher termites.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A New Group of Modular Xylanases in Glycoside Hydrolase Family 8 from Marine Bacteria.Applied and environmental microbiology · 2018Article
- A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenicThe Biochemical journal · 2018Article
- GH30 Glucuronoxylan-Specific Xylanase from Streptomyces turgidiscabies C56.Applied and environmental microbiology · 2018Article
- Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.Extremophiles : life under extreme conditions · 2018Review
- Structural Investigation of Cell Wall Xylan Polysaccharides from the Leaves of Algerian Argania spinosa.Molecules (Basel, Switzerland) · 2016Article
- The Glycoside Hydrolase Family 8 Reducing-End Xylose-Releasing Exo-oligoxylanase Rex8A from Paenibacillus barcinonensis BP-23 Is Active on Branched Xylooligosaccharides.Applied and environmental microbiology · 2016Article
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3 authors.
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Abstract
Xyn30D from the xylanolytic strain Paenibacillus barcinonensis has been identified and characterized. The enzyme shows a modular structure comprising a catalytic module family 30 (GH30) and a carbohydrate-binding module family 35 (CBM35). Like GH30 xylanases, recombinant Xyn30D efficiently hydrolyzed glucuronoxylans and methyl-glucuronic acid branched xylooligosaccharides but showed no catalytic activity on arabinose-substituted xylans. Kinetic parameters of Xyn30D were determined on beechwood xylan, showing a K(m) of 14.72 mg/ml and a k(cat) value of 1,510 min(-1). The multidomain structure of Xyn30D clearly distinguishes it from the GH30 xylanases characterized to date, which are single-domain enzymes. The modules of the enzyme were individually expressed in a recombinant host and characterized. The isolated GH30 catalytic module showed specific activity, mode of action on xylan, and kinetic parameters that were similar to those of the full-length enzyme. Computer modeling of the three-dimensional structure of Xyn30D showed that the catalytic module is comprised of a common (β/α)(8) barrel linked to a side-associated β-structure. Several derivatives of the catalytic module with decreasing deletions of this associated structure were constructed. None of them showed catalytic activity, indicating the importance of the side β-structure in the catalysis of Xyn30D. Binding properties of the isolated carbohydrate-binding module were analyzed by affinity gel electrophoresis, which showed that the CBM35 of the enzyme binds to soluble glucuronoxylans and arabinoxylans. Analysis by isothermal titration calorimetry showed that CBM35 binds to glucuronic acid and requires calcium ions for binding. Occurrence of a CBM35 in a glucuronoxylan-specific xylanase is a differential trait of the enzyme characterized.
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