5MEM

A potent fluorescent inhibitor of glycogen phosphorylase as a catalytic site probe.

5MEM の概要

• エントリーDOI: 10.2210/pdb5mem/pdb
• 分子名称: Glycogen phosphorylase, muscle form, PYRIDOXAL-5'-PHOSPHATE, 2-[[1-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]-2-oxidanylidene-pyrimidin-4-yl]amino]-10~{H}-acridin-9-one, ... (4 entities in total)
• 機能のキーワード: gp inhibitors, glucopyranosyl cytosine acridine derivatives, electronic absorption spectra, fluorescence spectra, fluorescent protein
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 98135.98

構造登録者

Mamais, M.,Chrysina, E.D. (登録日: 2016-11-15, 公開日: 2017-11-29, 最終更新日: 2025-04-09)

主引用文献

Mamais, M.,Degli Esposti, A.,Kouloumoundra, V.,Gustavsson, T.,Monti, F.,Venturini, A.,Chrysina, E.D.,Markovitsi, D.,Gimisis, T.
A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site.
Chemistry, 23:8800-8805, 2017

PubMed 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.

PubMed: 28493496
DOI: 10.1002/chem.201701591

実験手法

X-RAY DIFFRACTION (1.78 Å)