Frontispiece: A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site. Issue 37 (3rd July 2017)

• Record Type: Journal Article
• Authors: Mamais, Michael; Degli Esposti, Alessandra; Kouloumoundra, Virginia; Gustavsson, Thomas; Monti, Filippo; Venturini, Alessandro; Chrysina, Evangelia D.; Markovitsi, Dimitra; Gimisis, Thanasis
• Is Part Of: Chemistry. Volume 23:Issue 37(2017)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-07-03
• Subjects: acridone based inhibitors -- glycogen phosphorylase -- optical spectra -- quantum chemistry -- X-ray crystallography; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201783763
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : Glycogen phosphorylase (GP) plays a key role in glucose regulation. The design and synthesis of a new potent inhibitor of GP is described. By exploiting its optical properties, it is shown that, due to an extended hydrogen bonding network, the local pH in the GP catalytic site is higher than12 . For the full story, see the Communication by A. Venturini, E. D. Chrysina, D. Markovitsi, T. Gimisis et al. onpage 8800 ff.