The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects
Open accessAbstract
Cell wall degrading enzymes have a complex molecular architecture consisting of catalytic modules and noncatalytic carbohydrate-binding modules (CBMs). The function of CBMs in cell wall degrading processes is poorly understood. Here, we have evaluated the potential enzyme-targeting function of CBMs in the context of intact primary and secondary cell wall deconstruction. The capacity of a pectate lyase to degrade pectic homogalacturonan in primary cell walls was potentiated by cellulose-directed CBMs but not by xylan-directed CBMs. Conversely, the arabinofuranosidase-mediated removal of side chains from arabinoxylan in xylan-rich and cellulose-poor wheat grain endosperm cell walls was enhanced by a xylan-binding CBM but less so by a crystalline cellulose-specific module. The capacity of xylanases to degrade xylan in secondary cell walls was potentiated by both xylan- and cellulose-directed CBMs. These studies demonstrate that CBMs can potentiate the action of a cognate catalytic module toward polysaccharides in intact cell walls through the recognition of nonsubstrate polysaccharides. The targeting actions of CBMs therefore have strong proximity effects within cell wall structures, explaining why cellulose-directed CBMs are appended to many noncellulase cell wall hydrolases.
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Cites
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A classification of glycosyl hydrolases based on amino acid sequence similarities
Henrissat, B. (1991) · Biochemical Journal · doi:10.1042/bj2800309 · Cited by 3,188
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Self-citationCrystalline cellulose degradation: new insight into the function of cellobiohydrolases
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Monoclonal Antibodies to Plant Cell Wall Xylans and Arabinoxylans
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Self-citationCarbohydrate-binding domains: multiplicity of biological roles
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Cited by
Khalifa, A. A. Z., Ichikawa, M., Dai, D., Kubo, S., Black, C. S., Peri, K., McAlear, T. S., Veyron, S., Yang, S. K., Vargas, J., et al. (2020) · eLife · doi:10.7554/elife.52760 · Cited by 1,676
Unusual molecular architecture of a human gut microbiota β-mannanase reveals a new CBM family
Łoś, N., Lelėnaitė, I., Willats, W. G. T., Terrapon, N., Morales-García, A. L., Yau, H. C. L., Lowe, E. C., & Bolam, D. N. (2026) · doi:10.64898/2026.02.11.704390
Metadata
- Authors
- Hervé, C., Rogowski, A., Blake, A. W., Marcus, S. E., Gilbert, H. J., & Knox, J. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-08-09
- Volume
- 107
- Issue
- 34
- Pages
- 15293-15298
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2056457078
- Cited by
- 305
- References
- 29
- FWCI
- 17.46
- Type
- journal article
- Language
- en
- Open access
- green
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- Hervé, C., Rogowski, A., Blake, A. W., Marcus, S. E., Gilbert, H. J., & Knox, J. P. (2010). Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1005732107
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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