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Literature summary for 2.4.1.1 extracted from
- Properties and functions of the storage sites of glycogen phosphorylase (2015), J. Biochem., 157, 451-458.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| AMP | - |
Oryctolagus cuniculus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | when maltohexaose is used as the substrate, typical Michaelis-Menten curves ar obtained | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| [(1->4)-alpha-D-glucosyl]n + phosphate | Oryctolagus cuniculus | - |
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | P00489 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the assay of enzyme activity at micromolar concentration of maltooligosyl-substrate is about 100 times lower than that in conventional enzyme assays using glycogen | Oryctolagus cuniculus | ? | - |
? | |
| pyridylamino-maltohexaose + alpha-D-glucose 1-phosphate | - |
Oryctolagus cuniculus | pyridylamino-maltoheptaose + phosphate | - |
r | |
| [(1->4)-alpha-D-glucosyl]n + phosphate | - |
Oryctolagus cuniculus | [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
| [(1->4)-alpha-D-glucosyl]n + phosphate | bovine liver glycogen, effects of the C-terminal domain on enzyme binding to glycogen, overview | Oryctolagus cuniculus | [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | biologically active form, each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site | Oryctolagus cuniculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| glycogen phosphorylase b | - |
Oryctolagus cuniculus |
| GPb | - |
Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at, glycogen synthesis | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.8 | - |
assay at, glycogen synthesis | Oryctolagus cuniculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme activity consists of two activities: (i) binding to the glycogen molecule and (ii) phosphorolysis of the non-reducing-end glucose residues. Activity (i) is mainly due to the activities of the two storage sites, which depend on the ionic strength of the medium and are directly inhibited by cyclodextrins. Activity (ii), the total activity of the two catalytic sites, exhibit relatively little ionic strength dependence. Because the combined activity of (i) and (ii) is deduced using glycogen as an assay substrate, the sole activity of (ii) must be measured using small maltooligosyl-substrates | Oryctolagus cuniculus |
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