background:
Glycolysis is an evolutionarily conserved series of ten chemical reactions that utilizes eleven enzymes to concomitantly generate pyruvate and ATP from glucose. Phospho-fructose kinase-2/fructose 2,6-bisphosphatase (PFK-2) stimulates the synthesis and degradation of fructose 2,6-bisphosphate. Glycogen phosphorylase (also known as GP) is an allosteric enzyme important in carbohydrate metabolism. Its activity is regulated through either noncovalent binding of metabolites or by covalent modification. Glycogen phosphorylase catalyzes the phosphorylation of glycogen to Glc-1-P. There are three genes which encode the brain, liver and muscle forms of glycogen phosphorylase, PYGB, PYGL and PYGM. Because of its fundamental role in the metabolism of glycogen, glycogen phosphorylase has been a target for the design of inhibitory compounds, which could be valuable in the therapeutic treatment of type 2 diabetes mellitus.
Function:
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Subunit:
Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.
Post-translational modifications:
Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.
Similarity:
Belongs to the glycogen phosphorylase family.
Database links:
Entrez Gene: 5834 Human
Entrez Gene: 110078 Mouse
Entrez Gene: 25739 Rat
Omim: 138550 Human
SwissProt: P11216 Human
SwissProt: Q8CI94 Mouse
SwissProt: P53534 Rat
Unigene: 368157 Human
Unigene: 222584 Mouse
Unigene: 1518 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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