TY  - JOUR
AU  - Mamais, Michael
AU  - DegliEsposti, Alessandra
AU  - Kouloumoundra, Virginia
AU  - Gustavsson, Thomas
AU  - Monti, Filippo
AU  - Venturini, Alessandro
AU  - Chrysina, Evangelia D.
AU  - Markovitsi, Dimitra
AU  - Gimisis, Thanasis
TI  - A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site
JO  - Chemistry - a European journal
VL  - 23
IS  - 37
SN  - 0947-6539
CY  - Weinheim
PB  - Wiley-VCH
M1  - PUBDB-2017-13502
SP  - 8800 - 8805
PY  - 2017
N1  - © Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ; Post referee fulltext in progress; Embargo 12 months from publication
AB  - The design and synthesis of a glucose-based acridone derivative (GLAC), a potent inhibitor of glycogen phosphorylase (GP) are described. GLAC is the first inhibitor of glycogen phosphorylase, the electronic absorption properties of which are clearly distinguishable from those of the enzyme. This allows probing subtle interactions in the catalytic site. The GLAC absorption spectra, associated with X-ray crystallography and quantum chemistry calculations, reveal that part of the catalytic site of GP behaves as a highly basic environment in which GLAC exists as a bis-anion. This is explained by water-bridged hydrogen-bonding interactions with specific catalytic site residues.
LB  - PUB:(DE-HGF)16
C6  - pmid:28493496
UR  - <Go to ISI:>//WOS:000404550000003
DO  - DOI:10.1002/chem.201701591
UR  - https://bib-pubdb1.desy.de/record/397870
ER  -