Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 53, Issue -, Pages 183-191Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2019.09.007
Keywords
Glycosidases; Enzyme mechanisms; Sugar conformation; Quantum mechanics/molecular mechanics; Molecular dynamics; Metadynamics
Categories
Funding
- Spanish Minister of Science, Innovation and Universities (MICINN) [CTQ2017-85496-P]
- Spanish Minister of Science, Innovation and Universities (MICINN) (FEDER)
- Agency for Management of University and Research Grants of Generalitat de Catalunya (AGAUR) [2017SGR-1189]
- Spanish Structures of Excellence Maria de Maeztu [MDM-2017-0767]
- MICINN [FPI-BES-2015-072055]
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Modeling catalysis in carbohydrate-active enzymes is a daunting challenge because of the high flexibility and diversity of both enzymes and carbohydrates. Glycoside hydrolases (GHs) are an illustrative example, where conformational changes and subtle interactions have been shown to be critical for catalysis. GHs have pivotal roles in industry (e.g. biofuel or detergent production) and biomedicine (e.g. targets for cancer and diabetes), and thus, a huge effort is devoted to unveil their molecular mechanisms. Besides experimental techniques, computational methods have served to provide an in-depth understanding of GH mechanisms, capturing complex reaction coordinates and the conformational itineraries that substrates follow during the whole catalytic pathway, providing a framework that ultimately may assist the engineering of these enzymes and the design of new inhibitors.
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