ArticleActa crystallographica. Section D, Biological crystallography2014
A novel member of glycoside hydrolase family 30 subfamily 8 with altered substrate specificity.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026Article
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Enzymatic Production of Prebiotic Xylooligosaccharides Using aJournal of agricultural and food chemistry · 2026Article
- Characterization of a novel GH30 non-specific endoxylanase AcXyn30B from Acetivibrio clariflavus.Applied microbiology and biotechnology · 2024Article
- Comprehensive Genome Analysis of Cellulose and Xylan-Active CAZymes from the GenusMicrobiology spectrum · 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
- Recent advances in the enzymatic production and applications of xylooligosaccharides.World journal of microbiology & biotechnology · 2021Review
- Catalytic Diversity of GH30 Xylanases.Molecules (Basel, Switzerland) · 2021Article
- Friend or Foe? Impacts of Dietary Xylans, Xylooligosaccharides, and Xylanases on Intestinal Health and Growth Performance of Monogastric Animals.Animals : an open access journal from MDPI · 2021Review
- A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum.Applied microbiology and biotechnology · 2021Article
- A New Subfamily of Glycoside Hydrolase Family 30 with Strict Xylobiohydrolase Function.Frontiers in molecular biosciences · 2021Article
- Crystal structure of GH30-7 endoxylanase C from the filamentous fungus Talaromyces cellulolyticus.Acta crystallographica. Section F, Structural biology communications · 2020Article
- CaXyn30B from the solventogenic bacterium Clostridium acetobutylicum is a glucuronic acid-dependent endoxylanase.BMC research notes · 2020Article
- 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
- Endo-xylanases as tools for production of substituted xylooligosaccharides with prebiotic properties.Applied microbiology and biotechnology · 2018Review
- A plasmid borne, functionally novel glycoside hydrolase family 30 subfamily 8 endoxylanase from solventogenicThe Biochemical journal · 2018Article
- Structural Considerations on the Use of Endo-Xylanases for the Production of prebiotic Xylooligosaccharides from Biomass.Current protein & peptide science · 2018Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Endoxylanases classified into glycoside hydrolase family 30 subfamily 8 (GH30-8) are known to hydrolyze the hemicellulosic polysaccharide glucuronoxylan (GX) but not arabinoxylan or neutral xylooligosaccharides. This is owing to the specificity of these enzymes for the α-1,2-linked glucuronate (GA) appendage of GX. Limit hydrolysis of this substrate produces a series of aldouronates each containing a single GA substituted on the xylose penultimate to the reducing terminus. In this work, the structural and biochemical characterization of xylanase 30A from Clostridium papyrosolvens (CpXyn30A) is presented. This xylanase possesses a high degree of amino-acid identity to the canonical GH30-8 enzymes, but lacks the hallmark β8-α8 loop region which in part defines the function of this GH30 subfamily and its role in GA recognition. CpXyn30A is shown to have a similarly low activity on all xylan substrates, while hydrolysis of xylohexaose revealed a competing transglycosylation reaction. These findings are directly compared with the model GH30-8 enzyme from Bacillus subtilis, XynC. Despite its high sequence identity to the GH30-8 enzymes, CpXyn30A does not have any apparent specificity for the GA appendage. These findings confirm that the typically conserved β8-α8 loop region of these enzymes influences xylan substrate specificity but not necessarily β-1,4-xylanase function.
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