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M3003

Sigma-Aldrich

Myokinase from rabbit muscle

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

Sinónimos:

ATP: AMP phosphotransferase, Adenylate Kinase

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About This Item

Número de CAS:
9013-02-9
Comisión internacional de enzimas:
2.7.4.3 (BRENDA, IUBMB)
EC Number:
232-743-3
MDL number:
MFCD00131644
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

200

form

ammonium sulfate suspension

specific activity

1,500-3,000 units/mg protein (biuret)

mol wt

21 kDa

foreign activity

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

storage temp.

2-8°C

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.

Unit Definition

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

Physical form

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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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