ArticleThe Journal of biological chemistry2013
Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 96 citations in OpenAlex.
- A Novel GH26 β-Mannanase from Bacillus subtilis HM7 Producing Manno-Oligosaccharides with Strain-Specific Prebiotic Activity.Applied biochemistry and biotechnology · 2026Article
- Unusual molecular architecture of a human gut microbiota β-mannanase reveals a new CBM family.Cellular and molecular life sciences : CMLS · 2026Article
- Unveiling the Structural and Biochemical Characteristics of an Acidophilic β-Mannanase from Soybean (Journal of agricultural and food chemistry · 2025Article
- Multiomic Analysis Provided Insights into the Responses of Carbon Sources by Wood-Rotting FungiJournal of fungi (Basel, Switzerland) · 2025Article
- Anatomical limitations in adventitious root formation revealed by magnetic resonance imaging, infrared spectroscopy, and histology of rose genotypes with contrasting rooting phenotypes.Journal of experimental botany · 2024Article
- Straw from Different Crop Species Recruits Different Communities of Lignocellulose-Degrading Microorganisms in Black Soil.Microorganisms · 2024Article
- Towards an understanding of the enzymatic degradation of complex plant mannan structures.World journal of microbiology & biotechnology · 2023Review
- Heterologous Expression, Purification and Characterization of an Alkalic Thermophilic β-Mannanase CcMan5C fromJournal of fungi (Basel, Switzerland) · 2023Article
- Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan.The ISME journal · 2023Article
- Biochemical analyses of a novel acidophilic GH5 β-mannanase fromFrontiers in microbiology · 2023Article
- Reshaping the binding channel of a novel GH113 family β-mannanase from Paenibacillus cineris (PcMan113) for enhanced activity.Bioresources and bioprocessing · 2022Article
- Activity-based protein profiling reveals dynamic substrate-specific cellulase secretion by saprotrophic basidiomycetes.Biotechnology for biofuels and bioproducts · 2022Article
- Molecular insight into Aspergillus oryzae β-mannanase interacting with mannotriose revealed by molecular dynamic simulation study.PloS one · 2022Article
- Enzymatic Conversion of Mannan-Rich Plant Waste Biomass into Prebiotic Mannooligosaccharides.Foods (Basel, Switzerland) · 2021Review
- Biochemical properties of a native β-1,4-mannanase fromBiochemistry and biophysics reports · 2021Article
- Novel 3-Applied and environmental microbiology · 2021Article
- Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-β-1,3-galactanase fromThe Journal of biological chemistry · 2020Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Expression, homology modeling and enzymatic characterization of a new β-mannanase belonging to glycoside hydrolase family 1 from Enterobacter aerogenes B19.Microbial cell factories · 2020Article
- Analyzing the Substrate Specificity of a Class of Long-Horned-Beetle-Derived Xylanases by Using Synthetic Arabinoxylan Oligo- and Polysaccharides.Chembiochem : a European journal of chemical biology · 2020Article
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6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-β-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization, and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the -4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4 and 2.85 Å resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the -4 subsite mediated by two aromatic residues Trp-244 and Trp-245. The PaMan26A structure appended to its family 35 carbohydrate binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.
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