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Bacillus stearothermophilus Acetate Kinase

 Product Information

Cat #
MBS-0298
CAS No.
9027-42-3
Enzyme Commission Number
EC 2.7.2.1
Product Overview
High-quality enzyme products. Well-defined strains can be also provided for our clients to manufacture fermented products in a cost-effective way.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating)
Type
Function
Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate.
Applications
Research Use
Storage
2-8°C
Storage Buffer
Shelf Life
Strains
Bacillus stearothermophilus
Source
Bacillus stearothermophilus
Appearance
Molecular Weight
Color / Form
Instruction
Enzyme Class
Transferases
Production Methods
Fermentation
Activity
400-1,200 units/mg solid
Specific Enzyme Activity
Purity
Unit Definition
One unit will phosphorylate 1.0 μmole of acetate to acetyl phosphate per min at pH 7.2 at 30°C.
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
ATP + acetate = ADP + acetyl phosphate
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage

 Description

In molecular biology, acetate kinase (EC 2.7.2.1), which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation. Short-chain fatty acids (SCFAs) play a major role in carbon cycle and can be utilized as a source of carbon and energy by bacteria. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydRate. A related enzyme, butyRate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyRate in the presence of ATP to form butyryl phosphate

For Research Use Only.
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