M3003
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 CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-743-3
NACRES:
NA.54
MDL number:
Nombre del producto
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
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
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.
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.
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.
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
Clase de almacenamiento
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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Myokinase, ATP-AMP Transphosphorylase.
Noda, L., and Kuby, S.A.
Methods in Enzymology, 6, 223-230 (1962)
Irmgard U Haussmann et al.
Nature communications, 13(1), 1209-1209 (2022-03-10)
Cap-adjacent nucleotides of animal, protist and viral mRNAs can be O-methylated at the 2' position of the ribose (cOMe). The functions of cOMe in animals, however, remain largely unknown. Here we show that the two cap methyltransferases (CMTr1 and CMTr2)
Qingfeng Chen et al.
The Journal of biological chemistry, 285(39), 29780-29786 (2010-07-20)
The GH3 family of acyl-acid-amido synthetases catalyze the ATP-dependent formation of amino acid conjugates to modulate levels of active plant hormones, including auxins and jasmonates. Initial biochemical studies of various GH3s show that these enzymes group into three families based
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
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)
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