Journal Article PUBDB-2017-13502

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A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site

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2017
Wiley-VCH Weinheim

Chemistry - a European journal 23(37), 8800 - 8805 () [10.1002/chem.201701591]
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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.

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

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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Medline ; Current Contents - Physical, Chemical and Earth Sciences ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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 Record created 2017-12-14, last modified 2025-07-30


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