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M3003

Sigma-Aldrich

Myokinase from rabbit muscle

ammonium sulfate suspension, 1,500-3,000 units/mg protein (biuret)

Synonyme(s) :

ATP: AMP phosphotransferase, Adenylate Kinase

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About This Item

Numéro CAS:
9013-02-9
Numéro de classification (Commission des enzymes):
2.7.4.3 (BRENDA, IUBMB)
Numéro CE :
232-743-3
Numéro MDL:
MFCD00131644
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

rabbit muscle

Niveau de qualité

200

Forme

ammonium sulfate suspension

Activité spécifique

1,500-3,000 units/mg protein (biuret)

Poids mol.

21 kDa

Activité étrangère

3-phosphoglyceric phosphokinase ≤0.05%
lactic dehydrogenase and pyruvate kinase ≤0.01%

Température de stockage

2-8°C

Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

One unit will convert 2.0 μmoles of ADP to ATP+AMP per min at pH 7.6 at 37°C.

Forme physique

Suspension in 3.2 M (NH4)2SO4 solution containing 0.001 M EDTA, pH 6.0

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Inactivation of rabbit muscle adenosine triphosphate-adenosine 5'-phosphate phosphotransferase by alkylation of methionine residues.
L F Kress et al.
The Journal of biological chemistry, 242(4), 558-564 (1967-02-25)
Secretion from dense granules: luminescence method for adenine nucleotides.
M Fred Heath
Methods in molecular biology (Clifton, N.J.), 272, 89-93 (2004-07-01)
Likui Feng et al.
Nature communications, 12(1), 4912-4912 (2021-08-15)
Polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS) hybrid systems typically use complex protein-protein interactions to facilitate direct transfer of intermediates between these multimodular megaenzymes. In the canal-associated neurons (CANs) of Caenorhabditis elegans, PKS-1 and NRPS-1 produce the nemamides, the only known
The sulfhydryl groups of rabbit muscle adenosine triphosphate-adenosine monophosphate phosphotransferase. Activity of enzyme treated with mercurials.
L F Kress et al.
The Journal of biological chemistry, 241(10), 2293-2300 (1966-05-25)
S A Kuby et al.
Journal of protein chemistry, 8(4), 549-562 (1989-08-01)
Two peptide fragments, derived from the head and tail of rabbit muscle myokinase, were found to possess remarkable and specific ligand-binding properties (Hamada et al., 1979). By initiating systematic syntheses and measurements of equilibrium substrate-binding properties of these two sets
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Instructions for working with enzymes supplied as ammonium sulfate suspensions

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