0524686 - ÚFCH JH 2021 RIV US eng J - Journal Article
Alonso-Gil, Santiago
Mimicking the transition state of reactions of glycoside hydrolases: Updating the conformational space of the oxocarbenium cation.
Journal of Carbohydrate Chemistry. Roč. 39, č. 4 (2020), s. 175-188. ISSN 0732-8303. E-ISSN 1532-2327
Institutional support: RVO:61388955
Keywords : carbohydrate * glycoside hydrolase * conformation
OECD category: Physical chemistry
Impact factor: 1.667, year: 2020
Method of publishing: Limited access

One strategy for developing glycoside hydrolase (GH) inhibitors is to mimic the conformation of the transition state (TS) along the hydrolysis reaction coordinate. We present a DFT-based model to understand the conformational space of the oxocarbenium cation as a TS in carbohydrate chemistry. Using Bolzano’s theorem, we have demonstrated the existence of a function that divides the puckering coordinate space. These results are compared with the available experimental crystal structures of GH-inhibitor complexes, and a contradictory case (GH92) was computationally studied. Our mathematical model opens a door to design more specific inhibitors and to decipher the catalytic pathways of controversial cases.
Permanent Link: http://hdl.handle.net/11104/0309006