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PYGL
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. Belongs to the glycogen phosphorylase family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: Carbohydrate Metabolism - starch and sucrose; EC 2.4.1.1; Transferase |
| Chromosomal Location of mouse Ortholog: 12 C2|12 29.01 cM |
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Cellular Component:
cytoplasm
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Molecular Function:
1,4-alpha-oligoglucan phosphorylase activity; AMP binding; ATP binding; bile acid binding; carbohydrate binding; catalytic activity; glucose binding; glycogen phosphorylase activity; glycosyltransferase activity; identical protein binding; linear malto-oligosaccharide phosphorylase activity; nucleotide binding; protein binding; purine nucleobase binding; pyridoxal phosphate binding; SHG alpha-glucan phosphorylase activity; transferase activity; vitamin binding
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Biological Process:
5-phosphoribose 1-diphosphate biosynthetic process; carbohydrate metabolic process; glucose homeostasis; glycogen catabolic process; glycogen metabolic process; metabolic process; necroptotic process; response to bacterium
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Reference #:
Q9ET01
(UniProtKB)
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Alt. Names/Synonyms: Glycogen phosphorylase, liver form; liver glycogen phosphorylase; OTTMUSP00000031636; Pygl
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Gene Symbols: Pygl
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Molecular weight:
97,463 Da
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Basal Isoelectric point:
6.63
Predict pI for various phosphorylation states
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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