Glycogen Phosphorylase

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Yeast glycogen phosphorylase dimer with pyridoxal-5-phosphate and phosphate (PDB entry 1ygp)

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Additional Resources

For additional information, see: Carbohydrate Metabolism

References

  1. 1.0 1.1 1.2 Kristiansen M, Andersen B, Iversen LF, Westergaard N. Identification, synthesis, and characterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site. J Med Chem. 2004 Jul 1;47(14):3537-45. PMID:15214781 doi:10.1021/jm031121n
  2. 2.0 2.1 Roach PJ. Glycogen and its metabolism. Curr Mol Med. 2002 Mar;2(2):101-20. PMID:11949930
  3. 3.0 3.1 3.2 3.3 Palm D, Klein HW, Schinzel R, Buehner M, Helmreich EJM. The role of pyridoxal 5’-phosphate in glycogen phosphorylase catalysis. Biochemistry. 1990 Feb 6; 29(5):1099-1107.
  4. Biorn AC, Graves DJ. The amino-terminal tail of glycogen phosphorylase is a switch for controlling phosphorylase conformation, activation, and response to ligands. Biochemistry. 2001 May 1;40(17):5181-9. PMID:11318640 doi:10.1021/bi0020372
  5. 5.0 5.1 5.2 5.3 5.4 Barford D, Hu SH, Johnson LN. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J Mol Biol. 1991 Mar 5;218(1):233-60. PMID:1900534
  6. 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 Fletterick RJ, Sprang SR. Glycogen phosphorylase Structures and function. Accounts of Chemical Research. 1982 Nov; 15(11):361-369.
  7. 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 Johnson LH. Glycogen Phosphorylase: Control by phosphorylation and allosteric effectors. The FASEB Journal. 1992 March;6:2274-2282.
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