ArticleJournal of bacteriology2006
Characterization of XynC from Bacillus subtilis subsp. subtilis strain 168 and analysis of its role in depolymerization of glucuronoxylan.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
50 citing papers in PubMed.
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Advances in Enzymatic Production of Prebiotic Oligosaccharides from Agro-Industrial Waste: A Critical Review and Industrial Framework.Foods (Basel, Switzerland) · 2026Review
- Enzymatic Production of Prebiotic Xylooligosaccharides Using aJournal of agricultural and food chemistry · 2026Article
- GT61 β-1,2-xylosyltransferases define a conserved xylan modification in gymnosperm and Arabidopsis primary cell walls.The Plant journal : for cell and molecular biology · 2025Article
- Xylan Degradation in the Halotolerant BacteriumJournal of agricultural and food chemistry · 2025Article
- Article
- Harnessing the power of Bacillus subtilis MR42: direct production of defined xylooligosaccharides (XOS) from corn stalks with enhanced prebiotic properties.Microbial cell factories · 2025Article
- Large scale identification of pellicle and cell-free liquid phase associated proteins inCurrent research in microbial sciences · 2025Article
- Use of xylosidase 3C from Segatella baroniae to discriminate xylan non-reducing terminus substitution characteristics.BMC research notes · 2024Article
- Characterization of a novel GH30 non-specific endoxylanase AcXyn30B from Acetivibrio clariflavus.Applied microbiology and biotechnology · 2024Article
- Impact of xylan on field productivity and wood saccharification properties in aspen.Frontiers in plant science · 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
- Metabolism in the Niche: a Large-Scale Genome-Based Survey Reveals Inositol Utilization To Be Widespread among Soil, Commensal, and Pathogenic Bacteria.Microbiology spectrum · 2022Review
- Bacterial xylan utilization regulons: systems for coupling depolymerization of methylglucuronoxylans with assimilation and metabolism.Journal of industrial microbiology & biotechnology · 2022Article
- Yeast GH30 Xylanase fromMolecules (Basel, Switzerland) · 2022Article
- Chemical and nutritional characteristics, and microbial degradation of rapeseed meal recalcitrant carbohydrates: A review.Frontiers in nutrition · 2022Review
- 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
- Xylanolytic Bacillus species for xylooligosaccharides production: a critical review.Bioresources and bioprocessing · 2021Review
- A New Subfamily of Glycoside Hydrolase Family 30 with Strict Xylobiohydrolase Function.Frontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretion of xylanase activities by Bacillus subtilis 168 supports the development of this well-defined genetic system for conversion of methylglucuronoxylan (MeGAXn [where n represents the number of xylose residues]) in the hemicellulose component of lignocellulosics to biobased products. In addition to the characterized glycosyl hydrolase family 11 (GH 11) endoxylanase designated XynA, B. subtilis 168 secretes a second endoxylanase as the translated product of the ynfF gene. This sequence shows remarkable homology to the GH 5 endoxylanase secreted by strains of Erwinia chrysanthemi. To determine its properties and potential role in the depolymerization of MeGAXn, the ynfF gene was cloned and overexpressed to provide an endoxylanase, designated XynC, which was characterized with respect to substrate preference, kinetic properties, and product formation. With different sources of MeGAXn as the substrate, the specific activity increased with increasing methylglucuronosyl substitutions on the beta-1,4-xylan chain. With MeGAXn from sweetgum as a preferred substrate, XynC exhibited a Vmax of 59.9 units/mg XynC, a Km of 1.63 mg MeGAXn/ml, and a k(cat) of 2,635/minute at pH 6.0 and 37 degrees C. Matrix-assisted laser desorption ionization-time of flight mass spectrometry and 1H nuclear magnetic resonance data revealed that each hydrolysis product has a single glucuronosyl substitution penultimate to the reducing terminal xylose. This detailed analysis of XynC from B. subtilis 168 defines the unique depolymerization process catalyzed by the GH 5 endoxylanases. Based upon product analysis, B. subtilis 168 secretes both XynA and XynC. Expression of xynA was subject to MeGAXn induction; xynC expression was constitutive with growth on different substrates. Translation and secretion of both GH 11 and GH 5 endoxylanases by the fully sequenced and genetically malleable B. subtilis 168 recommends this bacterium for the introduction of genes required for the complete utilization of products of the enzyme-catalyzed depolymerization of MeGAXn. B. subtilis may serve as a model platform for development of gram-positive biocatalysts for conversion of lignocellulosic materials to renewable fuels and chemicals.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.