A New Potent Inhibitor of Glycogen Phosphorylase Reveals the Basicity of the Catalytic Site.
Chemistry
; 23(37): 8800-8805, 2017 Jul 03.
Article
en En
| MEDLINE
| ID: mdl-28493496
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.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Glucógeno Fosforilasa
/
Inhibidores Enzimáticos
Idioma:
En
Revista:
Chemistry
Asunto de la revista:
QUIMICA
Año:
2017
Tipo del documento:
Article
País de afiliación:
Grecia