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About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
MDL number:
Specific activity:
400-1,200 units/mg solid
Biological source:
bacterial (Bacillus stearothermophilus)
Pricing and availability is not currently available.
biological source
bacterial (Bacillus stearothermophilus)
Quality Level
form
lyophilized powder
specific activity
400-1,200 units/mg solid
storage temp.
2-8°C
Application
Acetate kinase is used to phosphorylate acetate to acetyl phosphate. Acetate Kinase from Bacillus stearothermophilus has been used to study allosteric activation.[1] [32P]-acetyl phosphate was generated by incubating potassium acetate in the reaction mixture with acetate kinase from Sigma. This [32P]-acetyl phosphate was used to label BldM, BldM D-54N or BldM D-54A loci during the study of the effect of bldM gene on Streptomyces coelicolor development.[2]
Biochem/physiol Actions
Acetate kinase plays an important role in glycolysis. Acetate kinase phosphorylates acetate in the presence of ATP and a divalent cation, which ultimately results in the production of acetyl-CoA.[3] Acetate kinase is also involved in the metabolism of propanoate, pyruvate and taurine. Acetate Kinase from Bacillus stearothermophilus is a thermostable tetramer of identical subunits with molecular weight of 40,000 Da each. The enzyme does not have a -SH group and is composed of 36% β-structure, 21 % α-helix and 43 % unordered structure.[4]
Involved in the metabolism of propanoate, pyruvate and taurine.
Physical form
Contains Tris-HCl buffer.
Other Notes
One unit will phosphorylate 1.0 μmole of acetate to acetyl phosphate per min at pH 7.2 at 30 °C.
signalword
Warning
hcodes
pcodes
Hazard Classifications
Met. Corr. 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Storage Class
11 - Combustible Solids
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H Nakajima et al.
Journal of biochemistry, 86(5), 1169-1177 (1979-11-01)
Fructose 1,6-bisphosphate (FBP) stimulates the reaction of Bacillus stearothermophilus acetate kinase (AK). FBP changes the reaction curve for ATP from a sigmoidal type to a Michaelis-Menten one. The binding of FBP to AK was studied by an equilibrium dialysis method
H Nakajima et al.
Journal of biochemistry, 84(1), 193-203 (1978-07-01)
1. Acetate kinase [EC 2.7.2.1] from an thermophile, B. stearothermophilus, was purified and crystalized. 2. This enzyme was shown to be a tetramer of identical subunits which had a molecular weight of about 40,000. Amino acid analysis showed no SH
Kuo-Hsiang Tang et al.
The Journal of biological chemistry, 285(46), 35848-35854 (2010-07-24)
The anoxygenic green sulfur bacteria (GSBs) assimilate CO(2) autotrophically through the reductive (reverse) tricarboxylic acid (RTCA) cycle. Some organic carbon sources, such as acetate and pyruvate, can be assimilated during the phototrophic growth of the GSBs, in the presence of
