Merck, M3003-2.5KU, Myokinase from rabbit muscle

General description
Research area: Cell Signaling
Myokinase, also called Adenylate kinase or ADK, is a phosphotransferase enzyme. It belongs to the family of nucleoside monophosphate kinases. Myokinase is an enzyme that can be found in skeletal muscle and acts as a phosphotransferase agitator.
Application
Myokinase has been used:

in a study to assess its reaction with the mercurials p-hydroxymercuribenzoate and p-mercuribenzenesulfonate
in a study to investigate the ligand-binding properties of its peptide fragments
as one of the components in the ATP generation solution for the quantification of 3’3’-c-di-AMP using an AMP-Luciferase assay

Biochem/physiol Actions
Myokinase or adenylate kinases, play a crucial role in regulating energy metabolism within cells and balancing adenine nucleotide ratios in different cellular compartments.

Myokinase is a key enzyme involved with adenine nucleotide metabolism. The action of myokinase insures that the adenine nucleotides (ATP, ADP, and AMP) are maintained in equilibrium in the cytosol.
Myokinase catalyzes the following reaction:ADP + ADP → ATP + AMP
Rabbit muscle myokinase can be inactivated by treatment with dithiobis-(2-nitrobenzoic) acid which alters methionine residues critical to myokinase activity.
Physical form
Suspension in 3.2 M (NH₄)₂SO₄ solution containing 0.001 M EDTA, pH 6.0
Other Notes
One unit will convert 2.0 μmoles of ADP to ATP+AMP per min at pH 7.6 at 37°C.