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Enzyme Activity Measurement of Diphosphate-Fructose-6-Phosphate 1-Phosphotransferase

Creative Enzymes’ current achievements are based on specialized enzymologist, the most advanced equipment, and the professional operations. Extensive experimental experiences have been accumulated in the past few years. The comprehensive understanding and standardized operation processes provide assurance for suitable assay methods and reliable results. The chromatographic assay for activity measurement of diphosphate-fructose-6-phosphate 1-phosphotransferase is one of our advanced services.

Diphosphate-fructose-6-phosphate 1-phosphotransferase (EC, PFK) catalyzes the reversible interconversion between fructose 6-phosphate and fructose 1,6-bisphosphate, using inorganic pyrophosphate, instead of ATP, as a phosphate group donor. The catalytic activity needs the participation of divalent cations, among which, Mg2+ is mostly used. Besides, Mn2+ and Co2+ may also take part in the reactions. This enzyme has been described in higher plants, primitive eukaryotes, bacteria, and archaea.

Diphosphate-fructose-6-phosphate 1-phosphotransferase participates in the glycolysis pathway and is the major regulator of this pathway flux. The usage of the PPi-dependent enzyme in glycolysis decreases ATP consumption and makes more ATP available for cellular processes, such as the generation of biosynthetic precursors and the maintenance of a transmembrane proton gradient. This enzyme also participates in carbohydrate metabolism such as fructose and mannose metabolism. Therefore, the enzyme is essential to achieve the maximal utilization of energy and resource. More and more studies are focused on the structural experiments, which could provide clues about the origin and evolution of this intriguing enzyme family. A group of data showed that this enzyme likely evolved from an ancestral ATP PFK and later acquired additional properties in plants. Associated with the site-direct mutagenesis, quantification of the enzyme activity would give an insight into the catalytic mechanism. To serve the purpose, Creative Enzymes offers excellent assay services to contribute to elucidation of the origin and mechanism of the enzyme.

 Figure: The crystal structure of a pyrophosphate-dependent phosphofructokinase from the  Lyme disease spirochete Borrelia  burgdorferi.
Figure: The crystal structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi.
Reference: Moore, S.A. et al. Structure 2002 10: 659-671.

Creative Enzymes persists in providing the best services of enzyme activity measurement. We have the capability to design proper approaches for each situation of activity tests. Having finished a myriad of assays, our customers are satisfied with the results and services quality. Creative Enzymes will constantly update our knowledge and upgrade devices to better accomplish enzyme activity measurement.

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