Recent advances in the allosteric inhibition of glycogen phosphorylase
Author(s)
Loughlin, WA
Griffith University Author(s)
Year published
2010
Metadata
Show full item recordAbstract
Glycogen Phosphorylase (GP) is an important target for the development of anti-hyperglycaemic drugs. GP is an enzyme which is moderated allosterically with multiple ligand binding sites where inhibitors can potentially modulate enzyme activity. The search for potent and isoform selective inhibitors of GP is ongoing with an increasing focus on allosteric inhibition. In this review, the structural diversity, and enzyme interactions of the most recent inhibitors, and in particular allosteric inhibitors, of GP at the different key binding sites is explored. A range of inhibitors of GP, with known as well as unknown binding site ...
View more >Glycogen Phosphorylase (GP) is an important target for the development of anti-hyperglycaemic drugs. GP is an enzyme which is moderated allosterically with multiple ligand binding sites where inhibitors can potentially modulate enzyme activity. The search for potent and isoform selective inhibitors of GP is ongoing with an increasing focus on allosteric inhibition. In this review, the structural diversity, and enzyme interactions of the most recent inhibitors, and in particular allosteric inhibitors, of GP at the different key binding sites is explored. A range of inhibitors of GP, with known as well as unknown binding site or mechanism is presented.
View less >
View more >Glycogen Phosphorylase (GP) is an important target for the development of anti-hyperglycaemic drugs. GP is an enzyme which is moderated allosterically with multiple ligand binding sites where inhibitors can potentially modulate enzyme activity. The search for potent and isoform selective inhibitors of GP is ongoing with an increasing focus on allosteric inhibition. In this review, the structural diversity, and enzyme interactions of the most recent inhibitors, and in particular allosteric inhibitors, of GP at the different key binding sites is explored. A range of inhibitors of GP, with known as well as unknown binding site or mechanism is presented.
View less >
Journal Title
Mini-Reviews in Medicinal Chemistry
Volume
10
Issue
12
Publisher URI
Subject
Medicinal and biomolecular chemistry
Biologically active molecules
Pharmacology and pharmaceutical sciences