Hexokinase/Glucose-6-phosphate dehydrogenase

High purity Hexokinase (yeast) / Glucose-6-phosphate dehydrogenase (G6P-DH) (Leuconostoc mesenteroides) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

EC (Hexokinase)
CAS: 9001-51-8

hexokinase; ATP:D-hexose 6-phosphotransferase

EC (Glucose-6-phosphate dehydrogenase)
CAS: 9001-40-5

glucose-6-phosphate dehydrogenase (NADP+); D-glucose-6-phosphate:NADP+ 1-oxidoreductase

Hexokinase: Recombinant. From yeast.
G6P-DH: Recombinant. From Leuconostoc mesenteroides.
In 3.2 M ammonium sulphate.

Hexokinase: ~ 420 U/mL.
G6P-DH: ~ 210 U/mL.

Stability: > 4 years at 4oC.

Product Code
10 mL Hexokinase (420 U/ml) +
G6P-DH (210 U/ml)

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Hexokinase/Glucose-6-phosphate dehydrogenase

EC (Hexokinase)
CAS: 9001-51-8

EC (Glucose-6-phosphate dehydrogenase)
CAS: 9001-40-5

(Hexokinase): Hexokinase; ATP:D-hexose 6-phosphotransferase
(G6P-DH): glucose-6-phosphate dehydrogenase (NADP+); D-glucose-6-phosphate:NADP+ 1-oxidoreductase

In 3.2 M ammonium sulphate.

> 4 years at 4oC.

Hexokinase: ~ 420 U/mL.
G6P-DH: ~ 210 U/mL.

Unit definition:
One Unit of hexokinase activity is defined as the amount of enzyme required to produce one μmole of NADH from NAD+ in the presence of D-glucose and glucose-6-phosphate dehydrogenase at pH 7.4 and 25oC. 

One Unit of Glucose-6-phosphate dehydrogenase activity is the amount of enzyme required to convert one μmole of glucose-6-phosphate to 6-phosphogluconate per minute, in the presence of NADP+ at pH 7.4 and 25oC. 

Catalyses the reaction:
ATP + D-hexose = ADP + D-hexose 6-phosphate

Phopshorylates D-glucose, D-mannose, D-fructose, sorbitol and D-glucosamine.

Glucose-6-phosphate dehydrogenase:
Catalyses the reaction:
D-glucose 6-phosphate + NADP+ = 6-phospho-D-glucono-1,5-lactone + NADPH + H+

Applications for the measurement of glucose and other hexoses in carbohydrate research and in the food and feeds, fermentation, wine, beverage and dairy industries.

A novel enzymatic method for the measurement of lactose in lactose‐free products.

Mangan, D., McCleary, B. V., Culleton, H., Cornaggia, C., Ivory, R., McKie, V., Delaney, E. & Kargelis, T. (2018). Journal of the Science of Food and Agriculture, In Press.

Simple purification method for a recombinantly expressed native His-tag-free aminopeptidase A from Lactobacillus delbrueckii.

Stressler, T., Tanzer, C., Ewert, J., Claaßen, W. & Fischer, L. (2017). Protein Expression and Purification, 131, 7-15.

A novel glutamyl (aspartyl)-specific aminopeptidase A from Lactobacillus delbrueckii with promising properties for application.

Stressler, T., Ewert, J., Merz, M., Funk, J., Claaßen, W., Lutz-Wahl, S., Schmidt, H., Kuhn, A. & Fischer, L. (2016). PloS one, 11(3), e0152139.

A fusion protein consisting of the exopeptidases PepN and PepX - production, characterization, and application.

Stressler, T., Pfahler, N., Merz, M., Hubschneider, L., Lutz-Wahl, S. Claaßen, W., & Fischer, L. (2016). Applied Microbiology and Biotechnology, 1-17, 7499-7515.

During yeast chronological aging resveratrol supplementation results in a short-lived phenotype Sir2-dependent.

Orlandi, I., Stamerra, G., Strippoli, M. & Vai, M. (2017). Redox Biology, 12, 745-754.

Influence of the metal ion on the enzyme activity and kinetics of PepA from Lactobacillus delbrueckii.

Ewert, J., Glück, C., Strasdeit, H., Fischer, L. & Stressler, T. (2017). Enzyme and Microbial Technology, 10, 69-78.