CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.200 | Phosphorylase Kinase; domain 1 |
|
3.30.200.20 | Phosphorylase Kinase; domain 1 |
Domain Context
CATH Clusters
| Superfamily | Phosphorylase Kinase; domain 1 |
| Functional Family | Phosphorylase b kinase gamma catalytic chain, liver/testis |
Enzyme Information
| 2.7.11.1 |
Non-specific serine/threonine protein kinase.
based on mapping to UniProt P00518
ATP + a protein = ADP + a phosphoprotein.
-!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70.
|
| 2.7.11.26 |
[Tau protein] kinase.
based on mapping to UniProt P00518
ATP + [tau protein] = ADP + [tau protein] phosphate.
-!- Activated by tubulin. -!- Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease. -!- Formerly EC 2.7.1.135.
|
| 2.7.11.19 |
Phosphorylase kinase.
based on mapping to UniProt P00518
2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
-!- Requires calmodulin for activity. -!- The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. -!- For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. -!- The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b. -!- The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit. -!- Formerly EC 2.7.1.38.
|
UniProtKB Entries (1)
| P00518 |
PHKG1_RABIT
Oryctolagus cuniculus
Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
|
PDB Structure
| PDB | 1QL6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Catalytic Mechanism of Phosphorylase Kinase Probed by Mutational Studies.
Biochemistry
|