M3003

Myokinase from rabbit muscle

Name: Myokinase from rabbit muscle
Brand: SIGMA

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

Synonym(s):

ATP: AMP phosphotransferase, Adenylate Kinase

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About This Item

CAS Number:

9013-02-9

UNSPSC Code:

12352204

eCl@ss:

32160410

EC Number:

232-743-3

NACRES:

NA.54

MDL number:

MFCD00131644

EC Number:

2.7.4.3 (BRENDA, IUBMB)

Key Documents

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Product Name

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

biological source

rabbit muscle

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

Quality Level

200

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This Item	P1506	P9136	T2391
Sigma-Aldrich M3003 Myokinase from rabbit muscle	Sigma-Aldrich P1506 Pyruvate Kinase from rabbit muscle	Sigma-Aldrich P9136 Pyruvate Kinase from rabbit muscle	Sigma-Aldrich T2391 Triosephosphate Isomerase from rabbit muscle
specific activity 1,500-3,000 units/mg protein (biuret)	specific activity 350-600 units/mg protein	specific activity 350-600 units/mg protein	specific activity ≥4,000 units/mg protein
biological source rabbit muscle	biological source rabbit muscle	biological source rabbit muscle	biological source rabbit muscle
form ammonium sulfate suspension	form ammonium sulfate suspension	form lyophilized powder	form ammonium sulfate suspension
mol wt 21 kDa	mol wt 237 kDa	mol wt 237 kDa	mol wt calculated mol wt 53.2 kDa
storage temp. 2-8°C	storage temp. 2-8°C	storage temp. −20°C	storage temp. 2-8°C
foreign activity 3-phosphoglyceric phosphokinase ≤0.05%, lactic dehydrogenase and pyruvate kinase ≤0.01%	foreign activity lactic dehydrogenase, creatine phosphokinase, and myokinase ≤0.01%, phosphoglucomutase ≤0.05%	foreign activity lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%	foreign activity 3-phosphoglyceric phosphokinase ≤0.01%, glyceraldehyde-3-phosphate dehydrogenase ≤0.01%, pyruvate kinase, lactic dehydrogenase, phosphoglucose isomerase, α-glycerophosphate dehydrogenase and aldolase ≤0.001%

Application

Myokinase has been used:

in a study to assess its reaction with the mercurials p-hydroxymercuribenzoate and p-mercuribenzenesulfonate [1]
in a study to investigate the ligand-binding properties of its peptide fragments [2]
as one of the components in the ATP generation solution for the quantification of 3’3’-c-di-AMP using an AMP-Luciferase assay [3]

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.[4]

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. [5]

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.[4] Myokinase is an enzyme that can be found in skeletal muscle and acts as a phosphotransferase agitator. [6]

Other Notes

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

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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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)

Studies on adenosine triphosphate transphosphorylases. XVIII. Synthesis and preparation of peptides and peptide fragments of rabbit muscle ATP-AMP transphosphorylase (adenylate kinase) and their nucleotide-binding properties.

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

Mapping the biosynthetic pathway of a hybrid polyketide-nonribosomal peptide in a metazoan.

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)

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)

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