Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformational shift which favors the more active glycogen phosphorylase “a” form over the less active glycogen phosphorylase b.
PHK, Native (Rabbit)
Phosphorylase kinase from rabbit muscle has been used in a study to assess features of glycogen phosphorylase. It has also been used in a study to investigate the activation of different forms of muscle phosphorylase kinase by actin.
Phosphorylase kinase contains four subunits each containing an α, β, γ, and Creative Enzymes component. The Creative Enzymes component binds 4 calcium molecules and is termed calmodulin while the γ unit acts as the catalytic subunit.
Lyophilized powder containing (NH4)2SO4, sucrose, β-glycerophosphate and dithioerythritol
Enzyme Commission Number
> 60 units/mg protein
One unit will form 1.0 μmolar unit of phosphorylase a from phosphorylase b per min at pH 7.7 at 30°C in the presence of ATP.
Phosphorylase Kinase; dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17; EC 22.214.171.124; EC 126.96.36.199; 9001-88-1