The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides
Open accessAbstract
Many enzymes that hydrolyze insoluble crystalline polysaccharides such as cellulose and chitin guide detached single-polymer chains through long and deep active-site clefts, leading to processive (stepwise) degradation of the polysaccharide. We have studied the links between enzyme efficiency and processivity by analyzing the effects of mutating aromatic residues in the substrate-binding groove of a processive chitobiohydrolase, chitinase B from Serratia marcescens . Mutation of two tryptophan residues (Trp-97 and Trp-220) close to the catalytic center (subsites +1 and +2) led to reduced processivity and a reduced ability to degrade crystalline chitin, suggesting that these two properties are linked. Most remarkably, the loss of processivity in the W97A mutant was accompanied by a 29-fold increase in the degradation rate for single-polymer chains as present in the soluble chitin-derivative chitosan. The properties of the W220A mutant showed a similar trend, although mutational effects were less dramatic. Processivity is thought to contribute to the degradation of crystalline polysaccharides because detached single-polymer chains are kept from reassociating with the solid material. The present results show that this processivity comes at a large cost in terms of enzyme speed. Thus, in some cases, it might be better to focus strategies for enzymatic depolymerization of polysaccharide biomass on improving substrate accessibility for nonprocessive enzymes rather than on improving the properties of processive enzymes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Features of promising technologies for pretreatment of lignocellulosic biomass
MOSIER, N. (2005) · Bioresource Technology · doi:10.1016/j.biortech.2004.06.025 · Cited by 6,251
Hydrolysis of lignocellulosic materials for ethanol production: a review
Sun, Y., & Cheng, J. (2002) · Bioresource Technology · doi:10.1016/s0960-8524(01)00212-7 · Cited by 6,070
The Path Forward for Biofuels and Biomaterials
Ragauskas, A. J., Williams, C. K., Davison, B. H., Britovsek, G., Cairney, J., Eckert, C. A., Frederick, W. J., Hallett, J. P., Leak, D. J., Liotta, C. L., et al. (2006) · Science · doi:10.1126/science.1114736 · Cited by 5,741
Host-Microbe Interactions: Shaping the Evolution of the Plant Immune Response
Chisholm, S. T., Coaker, G., Day, B., & Staskawicz, B. J. (2006) · Cell · doi:10.1016/j.cell.2006.02.008 · Cited by 2,957
Ethanol Can Contribute to Energy and Environmental Goals
Farrell, A. E., Plevin, R. J., Turner, B. T., Jones, A. D., O'Hare, M., & Kammen, D. M. (2006) · Science · doi:10.1126/science.1121416 · Cited by 2,823
Carbohydrate-binding modules: fine-tuning polysaccharide recognition
BORASTON, A. B., BOLAM, D. N., GILBERT, H. J., & DAVIES, G. J. (2004) · Biochemical Journal · doi:10.1042/bj20040892 · Cited by 2,030
Structures and mechanisms of glycosyl hydrolases
Davies, G., & Henrissat, B. (1995) · Structure · doi:10.1016/s0969-2126(01)00220-9 · Cited by 2,028
Nomenclature for sugar-binding subsites in glycosyl hydrolases
DAVIES, G. J., WILSON, K. S., & HENRISSAT, B. (1997) · Biochemical Journal · doi:10.1042/bj3210557 · Cited by 1,059
Acidic Mammalian Chitinase in Asthmatic Th2 Inflammation and IL-13 Pathway Activation
Zhu, Z., Zheng, T., Homer, R. J., Kim, Y.-K., Chen, N. Y., Cohn, L., Hamid, Q., & Elias, J. A. (2004) · Science · doi:10.1126/science.1095336 · Cited by 805
Crystalline cellulose degradation: new insight into the function of cellobiohydrolases
Teeri, T. T. (1997) · Trends in Biotechnology · doi:10.1016/s0167-7799(97)01032-9 · Cited by 693
Cited by
Deconstruction of Lignocellulosic Biomass to Fuels and Chemicals
Chundawat, S. P. S., Beckham, G. T., Himmel, M. E., & Dale, B. E. (2011) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-061010-114205 · Cited by 1,017
Payne, C. M., Knott, B. C., Mayes, H. B., Hansson, H., Himmel, M. E., Sandgren, M., Ståhlberg, J., & Beckham, G. T. (2015) · Chemical Reviews · doi:10.1021/cr500351c · Cited by 855
Near-complete depolymerization of polyesters with nano-dispersed enzymes
DelRe, C., Jiang, Y., Kang, P., Kwon, J., Hall, A., Jayapurna, I., Ruan, Z., Ma, L., Zolkin, K., Li, T., et al. (2021) · Nature · doi:10.1038/s41586-021-03408-3 · Cited by 298
Processivity of Cellobiohydrolases Is Limited by the Substrate
Kurašin, M., & Väljamäe, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.161059 · Cited by 274
Metadata
- Authors
- Horn, S. J., Sikorski, P., Cederkvist, J. B., Vaaje-Kolstad, G., Sørlie, M., Synstad, B., Vriend, G., Vårum, K. M., & Eijsink, V. G. H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-11-28
- Volume
- 103
- Issue
- 48
- Pages
- 18089-18094
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2035160545
- Cited by
- 277
- References
- 46
- FWCI
- 2.70
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. https://app.cochat.ai/papers/10.1073/pnas.0608909103
- The paper
- Horn, S. J., Sikorski, P., Cederkvist, J. B., Vaaje-Kolstad, G., Sørlie, M., Synstad, B., Vriend, G., Vårum, K. M., & Eijsink, V. G. H. (2006). Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0608909103
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
