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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
F J Grundy et al.
Journal of bacteriology, 175(22), 7348-7355 (1993-11-01)
The Bacillus subtilis gene encoding acetate kinase was identified on the basis of sequence similarity to the Escherichia coli ackA gene and to a second E. coli gene closely related to ackA. Insertional inactivation of this region of the B.
