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M3003

Sigma-Aldrich

Myokinase from rabbit muscle

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

Sinônimo(s):

ATP: AMP phosphotransferase, Adenylate Kinase

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About This Item

Número CAS:
9013-02-9
Número da licença da enzima:
2.7.4.3 (BRENDA, IUBMB)
Número CE:
232-743-3
Número MDL:
MFCD00131644
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

fonte biológica

rabbit muscle

Nível de qualidade

200

forma

ammonium sulfate suspension

atividade específica

1,500-3,000 units/mg protein (biuret)

peso molecular

21 kDa

atividade externa

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

temperatura de armazenamento

2-8°C

Descrição geral

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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.

Definição da unidade

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

forma física

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

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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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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