The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61: Structure and Function of a Large, Enigmatic Family
Abstract
Currently, the relatively high cost of enzymes such as glycoside hydrolases that catalyze cellulose hydrolysis represents a barrier to commercialization of a biorefinery capable of producing renewable transportable fuels such as ethanol from abundant lignocellulosic biomass. Among the many families of glycoside hydrolases that catalyze cellulose and hemicellulose hydrolysis, few are more enigmatic than family 61 (GH61), originally classified based on measurement of very weak endo-1,4-beta-d-glucanase activity in one family member. Here we show that certain GH61 proteins lack measurable hydrolytic activity by themselves but in the presence of various divalent metal ions can significantly reduce the total protein loading required to hydrolyze lignocellulosic biomass. We also solved the structure of one highly active GH61 protein and find that it is devoid of conserved, closely juxtaposed acidic side chains that could serve as general proton donor and nucleophile/base in a canonical hydrolytic reaction, and we conclude that the GH61 proteins are unlikely to be glycoside hydrolases. Structure-based mutagenesis shows the importance of several conserved residues for GH61 function. By incorporating the gene for one GH61 protein into a commercial Trichoderma reesei strain producing high levels of cellulolytic enzymes, we are able to reduce by 2-fold the total protein loading (and hence the cost) required to hydrolyze lignocellulosic biomass.
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Basic local alignment search tool
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PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
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Process Engineering Economics of Bioethanol Production
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Blair, D. E., Schüttelkopf, A. W., MacRae, J. I., & van Aalten, D. M. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504339102 · Cited by 230
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
Van Dyk, J. S., & Pletschke, B. I. (2012) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.03.002 · Cited by 1,015
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
Riley, R., Salamov, A. A., Brown, D. W., Nagy, L. G., Floudas, D., Held, B. W., Levasseur, A., Lombard, V., Morin, E., Otillar, R., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400592111 · Cited by 745
Recent advances in surface-modified cellulose nanofibrils
Rol, F., Belgacem, M. N., Gandini, A., & Bras, J. (2019) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2018.09.002 · Cited by 698
Metadata
- Authors
- Harris, P. V., Welner, D., McFarland, K. C., Re, E., Navarro Poulsen, J.-C., Brown, K., Salbo, R., Ding, H., Vlasenko, E., Merino, S., Xu, F., Cherry, J., Larsen, S., & Lo Leggio, L.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-03-29
- Volume
- 49
- Issue
- 15
- Pages
- 3305-3316
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2091513159
- Cited by
- 795
- References
- 5
- FWCI
- 32.40
- Type
- journal article
- Language
- en
- Open access
- closed
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