Search results for PYGL

Showing 8 results out of 8

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Protein (5 results from a total of 5)

Identifier: R-HSA-6801509
Species: Homo sapiens
Compartment: secretory granule lumen
Primary external reference: UniProt: PYGL: P06737
Identifier: R-HSA-6801505
Species: Homo sapiens
Compartment: ficolin-1-rich granule lumen
Primary external reference: UniProt: PYGL: P06737
Identifier: R-HSA-71585
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PYGL: P06737
Identifier: R-HSA-71580
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P06737
Identifier: R-HSA-6801551
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P06737

Reaction (3 results from a total of 3)

Identifier: R-HSA-71588
Species: Homo sapiens
Compartment: cytosol
The cytosolic phosphorylase kinase complex catalyzes the phosphorylation of glycogen phosphorylase (PYGL). Two forms of phosphorylase kinase complex have been described (Brushia and Walsh 1999). The one annotated here, consisting of four copies each of PHKA2 (alpha regulatory) (van den Berg et al. 1995), PHKB (beta regulatory) (Burwinkel et al. 2003a), PHKG2 (gamma catalytic) (Burwinkel et al. 2003b; Maichele et al. 2006) and CALM (calmodulin) subunits is abundant in liver and its action on the form of phosphorylase (PYGL) abundant in liver is described.

While initial studies of glycogen phosphorylase PGYM from rabbit muscle suggested that it is a homotetramer (Keller and Cori 1953), more recent work indicates that under physiological conditions the enzyme occurs as a homodimer (Huang and Graves 1970) and a dimeric structure for human PYGL enzyme is inferred here.

Identifier: R-HSA-71590
Species: Homo sapiens
Compartment: cytosol
The phosphorylated PYGL dimer (a form) of glycogen phosphorylase catalyzes the reaction of orthophosphate and glycogen-glycogenin 1 to form D-glucose 1-phosphate and limit dextrin-glycogenin 1. This reaction occurs on the surfaces of cytosolic glycogen granules. Non-phosphorylated PYGL dimers (b form) are catalytically inactive even in the presence of AMP. In the body, this reaction takes place in the liver where its dependence on hormonally stimulated PYGL phosphorylation (and lack of sensitivity to AMP) allow glucose mobilization in response to a demand for glucose from the rest of the body (Newgard et al. 1989; Rath et al. 2000).
Identifier: R-HSA-453339
Species: Homo sapiens
Compartment: cytosol
The phosphorylated PYGL dimer (a form) of glycogen phosphorylase catalyzes the reaction of orthophosphate and poly((1,4)-alpha-glucosyl) glycogenin-2 to form D-glucose 1-phosphate and glycogenin-2. This reaction occurs on the surfaces of cytosolic glycogen granules. Non-phosphorylated PYGL dimers (b form) are catalytically inactive even in the presence of AMP. In the body, this reaction takes place in the liver where its dependence on hormonally stimulated PYGL phosphorylation (and lack of sensitivity to AMP) allow glucose mobilization in response to a demand for glucose from the rest of the body (Newgard et al. 1989; Rath et al. 2000).
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