ArticleThe Journal of biological chemistry2008
The Cellvibrio japonicus mannanase CjMan26C displays a unique exo-mode of action that is conferred by subtle changes to the distal region of the active site.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 84 citations in OpenAlex.
- The development of activity-based mannanase probes.Chemical science · 2026Article
- Involvement of two putative gene clusters for exopolysaccharide biosynthesis and modification in sporangium formation inApplied and environmental microbiology · 2026Article
- Late Stage Mannan Metabolism in Cellvibrio japonicus Requires the Combined Action of a Mannosyl-Glucose Phosphorylase and a Mannobiose Epimerase.Molecular microbiology · 2026Article
- Isolation of a Novel Low-Temperature-Active and Organic-Solvent-Stable Mannanase from the Intestinal Metagenome ofInternational journal of molecular sciences · 2024Article
- Towards an understanding of the enzymatic degradation of complex plant mannan structures.World journal of microbiology & biotechnology · 2023Review
- Marine bacteroidetes use a conserved enzymatic cascade to digest diatom β-mannan.The ISME journal · 2023Article
- Enzymatic Conversion of Mannan-Rich Plant Waste Biomass into Prebiotic Mannooligosaccharides.Foods (Basel, Switzerland) · 2021Review
- Spatially remote motifs cooperatively affect substrate preference of a ruminal GH26-type endo-β-1,4-mannanase.The Journal of biological chemistry · 2020Article
- Molecular Cloning, Expression and Biochemical Characterization of a Family 5 Glycoside Hydrolase First Endo-Mannanase (RfGH5_7) from Ruminococcus flavefaciens FD-1 v3.Molecular biotechnology · 2019Article
- A surface-exposed GH26 β-mannanase fromThe Journal of biological chemistry · 2019Article
- Structural and functional analyses of glycoside hydrolase 138 enzymes targeting chain A galacturonic acid in the complex pectin rhamnogalacturonan II.The Journal of biological chemistry · 2019Article
- Structural and functional characterization of a bifunctional GH30-7 xylanase B from the filamentous fungusThe Journal of biological chemistry · 2019Article
- Crystal structure and substrate interactions of an unusual fungal non-CBM carrying GH26 endo-β-mannanase from Yunnania penicillata.Scientific reports · 2019Article
- Structural basis of exo-β-mannanase activity in the GH2 family.The Journal of biological chemistry · 2018Article
- SACCHARIS: an automated pipeline to streamline discovery of carbohydrate active enzyme activities within polyspecific families and de novo sequence datasets.Biotechnology for biofuels · 2018Article
- Galactomannan Catabolism Conferred by a Polysaccharide Utilization Locus of Bacteroides ovatus: ENZYME SYNERGY AND CRYSTAL STRUCTURE OF A β-MANNANASE.The Journal of biological chemistry · 2017Article
- Genome-Centric Analysis of a Thermophilic and Cellulolytic Bacterial Consortium Derived from Composting.Frontiers in microbiology · 2017Article
- Polysaccharide degradation systems of the saprophytic bacterium Cellvibrio japonicus.World journal of microbiology & biotechnology · 2016Review
- A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family.Applied and environmental microbiology · 2016Article
- The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans.The Journal of biological chemistry · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The microbial degradation of the plant cell wall is a pivotal biological process that is of increasing industrial significance. One of the major plant structural polysaccharides is mannan, a beta-1,4-linked d-mannose polymer, which is hydrolyzed by endo- and exo-acting mannanases. The mechanisms by which the exo-acting enzymes target the chain ends of mannan and how galactose decorations influence activity are poorly understood. Here we report the crystal structure and biochemical properties of CjMan26C, a Cellvibrio japonicus GH26 mannanase. The exo-acting enzyme releases the disaccharide mannobiose from the nonreducing end of mannan and mannooligosaccharides, harnessing four mannose-binding subsites extending from -2 to +2. The structure of CjMan26C is very similar to that of the endo-acting C. japonicus mannanase CjMan26A. The exo-activity displayed by CjMan26C, however, reflects a subtle change in surface topography in which a four-residue extension of surface loop creates a steric block at the distal glycone -2 subsite. endo-Activity can be introduced into enzyme variants through truncation of an aspartate side chain, a component of a surface loop, or by removing both the aspartate and its flanking residues. The structure of catalytically competent CjMan26C, in complex with a decorated manno-oligosaccharide, reveals a predominantly unhydrolyzed substrate in an approximate (1)S(5) conformation. The complex structure helps to explain how the substrate "side chain" decorations greatly reduce the activity of the enzyme; the galactose side chain at the -1 subsite makes polar interactions with the aglycone mannose, possibly leading to suboptimal binding and impaired leaving group departure. This report reveals how subtle differences in the loops surrounding the active site of a glycoside hydrolase can lead to a change in the mode of action of the enzyme.
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