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Literature summary for 2.7.11.19 extracted from
- Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (alphabetagammadelt)4 phosphorylase kinase complex (2012), Mol. Cell. Proteomics, 11, 1768-1776.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 16696 | - |
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation | Oryctolagus cuniculus |
| 16784 | - |
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 16787 | - |
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 44643 | - |
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation | Oryctolagus cuniculus |
| 44667 | - |
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 44669 | - |
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 125084 | - |
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation | Oryctolagus cuniculus |
| 125602 | - |
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 125660 | - |
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 138325 | - |
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation | Oryctolagus cuniculus |
| 138792 | - |
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 139358 | - |
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| 1299000 | - |
calculated from sequence, hexadecameric complex | Oryctolagus cuniculus |
| 1305000 | - |
mass spectrometry, hexadecameric complex | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | autophosphorylation results in a 40fold activation of phosphorylase conversion at pH 6.8 | Oryctolagus cuniculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| psoas | - |
Oryctolagus cuniculus | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -80°C in 50 mM HEPES buffer (pH 6.8, 10% w/v sucrose, and 0.2 mM EDTA) | Oryctolagus cuniculus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexadecamer | 4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation | Oryctolagus cuniculus |
| hexadecamer | 4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
| hexadecamer | 4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry | Oryctolagus cuniculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the phosphorylase kinase enzyme complex regulates glycogenolysis | Oryctolagus cuniculus |
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