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Glycosidase mechanisms: anatomy of a finely tuned catalyst.
Abstract
In order to accelerate the hydrolysis of glycosidic bonds by factors approaching 10(17)-fold, glycosidases have evolved finely tuned active sites optimally configured for transition-state stabilization. Structural analyses of various enzyme complexes representing stable intermediates along the reaction coordinate, in conjunction with detailed mechanistic studies on wild-type and mutant enzymes, have delineated the contributions of nucleophilic and general acid/base catalysis, as well as the roles of noncovalent interactions, to these impressive rate enhancements.
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Gosling, A., Stevens, G. W., Barber, A. R., Kentish, S. E., & Gras, S. L. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2009.12.063 · Cited by 313
Watts, A. G., Damager, I., Amaya, M. L., Buschiazzo, A., Alzari, P., Frasch, A. C., & Withers, S. G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0344967 · Cited by 211
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Metadata
- Authors
- Zechel, D. L., & Withers, S. G.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society
- Published
- 2000-01-18
- Volume
- 33
- Issue
- 1
- Pages
- 11-18
- ISSN
- 0001-4842 (ISSN-L)
- OpenAlex
- W2076301285
- Cited by
- 698
- References
- 0
- FWCI
- 28.17
- Type
- journal article
- Language
- en
- Open access
- closed
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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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