CATH Classification

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 2PHK
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.
Lowe, E.D., Noble, M.E., Skamnaki, V.T., Oikonomakos, N.G., Owen, D.J., Johnson, L.N.
EMBO J.
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