Journal Article

PUBDB-2017-13502

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site

Mamais, M. ; DegliEsposti, A. ; Kouloumoundra, V. ; Gustavsson, T. ; Monti, F. ; Venturini, A. (Corresponding author) ; Chrysina, E. D. ; Markovitsi, D. ; Gimisis, T.

2017
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/chem.201701591

Abstract: 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.

Note: © Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim ; Post referee fulltext in progress; Embargo 12 months from publication

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)
2. BIOSTRUCT-X - Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities (283570) (283570)
3. LASERLAB-EUROPE - The Integrated Initiative of European Laser Research Infrastructures III (284464) (284464)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2017

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Database coverage:
; Current Contents - Physical, Chemical and Earth Sciences ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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