Uridine(5')diphospho(1)-alpha-D-glucose. A binding study to glycogen phosphorylase b in the crystal.

Journal article

UDP-glucose is an R-state inhibitor of glycogen phosphorylase b, competitive with the substrate, glucose 1-phosphate and noncompetitive with the allosteric activator, AMP. Diffusion of 100 mM UDP-glucose into crystals of phosphorylase b resulted in a difference Fourier synthesis at 0.3-nm resolution that showed two peaks: (a) binding at the allosteric site and (b) binding at the catalytic site. At the allosteric site the whole of the UDP-glucose molecule can be located. It is in a well define...

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Authors: Oikonomakos, N; Acharya, K; Stuart, D; Melpidou, A; McLaughlin, P

• Publication status: Published
• Journal: European journal of biochemistry / FEBS
• Volume: 173
• Issue: 3
• Pages: 569-578
• Publication date: 1988-05-01
• DOI: 10.1111/j.1432-1033.1988.tb14037.x
• EISSN: 1432-1033
• ISSN: 0014-2956
• Language: English
• Keywords: Allosteric Site; Inosine Monophosphate; Structure-Activity Relationship; Catalysis; Protein Conformation; Uridine Diphosphate Glucose; Hydrogen Bonding; Uridine Diphosphate Sugars; Chemistry; X-Ray Diffraction; Phosphorylases; Chemical Phenomena; Models, Molecular; Enzyme Activation; Binding, Competitive