The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei: Separation of functional domains
Open accessAbstract
Limited proteolysis of the cellobiohydrolase I (CBH I, 65 kDa) from Trichoderma reesei by papain yields a core protein (56 kDa) which is fully active against small, soluble substrates such as the chromophoric glycosides derived from the cellodextrins and lactose. Activity against an insoluble substrate, such as Avicel, is however completely lost and concomitantly decreased adsorption onto this microcrystalline cellulose is observed. The peptide (10 kDa), initially split off during proteolysis, is identified as the heavily glycosylated carboxy‐terminal of the native CBH I. Depending on the experimental conditions the core protein is further nicked in between disulfide bonds, but its properties and stability do not appreciably differ from those of intact CBH I. These results lead to the proposal of a bifunctional organisation of the CBH I: one domain, corresponding to the carboxyterminal, acts as a binding site for insoluble cellulose and the other, localised in the core protein, contains the active (hydrolytic) site.
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Cites
A colorimetric method for the determination of sugars
DUBOIS, M., GILLES, K., HAMILTON, J. K., REBERS, P. A., & SMITH, F. (1951) · Nature · doi:10.1038/168167a0 · Cited by 2,504
Molecular Cloning of Exo–Cellobiohydrolase I Derived from Trichoderma Reesei Strain L27
Shoemaker, S., Schweickart, V., Ladner, M., Gelfand, D., Kwok, S., Myambo, K., & Innis, M. (1983) · Nature Biotechnology · doi:10.1038/nbt1083-691 · Cited by 351
The purification and properties of the C1 component of Trichoderma koningii cellulase
Wood, T. M., & McCrae, S. I. (1972) · Biochemical Journal · doi:10.1042/bj1281183 · Cited by 220
The Molecular Cloning of the Major Cellulase Gene from Trichoderma Reesei
Teeri, T., Salovuori, I., & Knowles, J. (1983) · Nature Biotechnology · doi:10.1038/nbt1083-696 · Cited by 180
Modification of certain foodstuffs by enzymes
GRAMPP, E. (1982) · Process Biochemistry · Cited by 96
Cited by
Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families
Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C., & Warren, R. A. J. (1991) · Microbiological Reviews · doi:10.1128/mmbr.55.2.303-315.1991 · Cited by 961
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
TOMME, P., VAN TILBEURGH, H., PETTERSSON, G., VAN DAMME, J., VANDEKERCKHOVE, J., KNOWLES, J., TEERI, T., & CLAEYSSENS, M. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13736.x · Cited by 579
Self-citationCarbohydrate Binding Modules: Biochemical Properties and Novel Applications
Shoseyov, O., Shani, Z., & Levy, I. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00028-05 · Cited by 561
Microbial degradation of polyurethane, polyester polyurethanes and polyether polyurethanes
Nakajima-Kambe, T., Shigeno-Akutsu, Y., Nomura, N., Onuma, F., & Nakahara, T. (1999) · Applied Microbiology and Biotechnology · doi:10.1007/s002530051373 · Cited by 284
Metadata
- Authors
- Van Tilbeurgh, H., Tomme, P., Claeyssens, M., Bhikhabhai, R., & Pettersson, G.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1986-08-18
- Volume
- 204
- Issue
- 2
- Pages
- 223-227
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1497315448
- Cited by
- 358
- References
- 5
- FWCI
- 17.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Van Tilbeurgh, H., Tomme, P., Claeyssens, M., Bhikhabhai, R., & Pettersson, G. (1986). Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei: Separation of functional domains. FEBS Letters. https://doi.org/10.1016/0014-5793(86)80816-x
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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).
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