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Literature summary for 2.4.1.1 extracted from
- Studies on phosphorylase isozymes in lower vertebrates. Purification and properties of lamprey phosphorylase (1977), Arch. Biochem. Biophys., 181, 447-453.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 5'-AMP | activation | Lethenteron camtschaticum |  |
| Na2SO4 | 500 mM, 40% activation of phosphorylase b in the presence of AMP | Lethenteron camtschaticum | |
| phosphate | activation | Lethenteron camtschaticum | |
| phosphate | in the presence of ATP-Mg | Lethenteron camtschaticum | |
| phosphate | converts phosphorylase b into phosphorylase a | Lethenteron camtschaticum | |
| Phosphorylase kinase | activation | Lethenteron camtschaticum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data | Lethenteron camtschaticum | |
| additional information | - |
additional information | comparison of muscle phosphorylases of various animals | Lethenteron camtschaticum | |
| 0.1 | - |
AMP | phosphorylase b | Lethenteron camtschaticum | |
| 3.5 | - |
alpha-D-glucose 1-phosphate | phosphorylase a | Lethenteron camtschaticum | |
| 15 | - |
alpha-D-glucose 1-phosphate | phosphorylase b, pH 6.3 | Lethenteron camtschaticum | |
| 22 | - |
alpha-D-glucose 1-phosphate | phosphorylase b, pH 6.8 | Lethenteron camtschaticum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 94000 | - |
2 * 94000, SDS-PAGE | Lethenteron camtschaticum |
| 170000 | - |
native PAGE | Lethenteron camtschaticum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lethenteron camtschaticum | - |
lamprey | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| side-chain modification | activation by rabbit muscle calcium-activated phosphorylase kinase in the presence of ATP and Mg2+ | Lethenteron camtschaticum |
| side-chain modification | phosphorylation converts inactive phosphorylase b into active phosphorylase a | Lethenteron camtschaticum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| pH 5.4, ammonium sulfate, DEAE-cellulose, 5'-AMP-Sepharose | Lethenteron camtschaticum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | tissue distribution | Lethenteron camtschaticum | - |
| muscle | skeletal muscle | Lethenteron camtschaticum | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 60 | - |
phosphorylase a, in the absence of AMP | Lethenteron camtschaticum |
| 75 | - |
phosphorylase a, in the presence of 1 mM AMP | Lethenteron camtschaticum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| [(1->4)-alpha-D-glucosyl]n + phosphate | - |
Lethenteron camtschaticum | [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 94000, SDS-PAGE | Lethenteron camtschaticum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.3 | - |
- |
Lethenteron camtschaticum |
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