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Enzyme Activity Measurement for Glycerophosphocholine Phosphodiesterase

Creative Enzymes conducts and provides efficient and reliable enzyme activity assays for the customers. Unsurpassed by any others, Creative Enzymes offers innovative enzymatic assay services with leading technical support found nowhere else in the industry. Herein, we are proud to offer the enzyme activity assay for glycerophosphocholine phosphodiesterase.

Glycerophosphocholine phosphodiesterase (EC; sn-glycero-3-phosphocholine glycerophosphohydrolase) is an enzyme that is ubiquitous in nature, found in various organisms including plants, bacteria and humans. This enzyme catalyzes the hydrolysis of sn-glycero-3-phosphocholine to glycerol-3-phosphate and choline. It resembles lipophosphodiesterase II in activity, hydrolyzing diesterified phosphate groups in a phospholipid or phosphate ester. Glycerophosphocholine phosphodiesterase is considered to be responsible for the degradation of intermediates, glycerophosphocholine (GPC) and glycerylphosphorylethanolamine (GPE) in the cellular phosphatidylcholine and phosphatidylethanolamine catabolic pathways. This enzyme enables the cell to utilize the glycerol-3-phosphate by degrading glycerophosphodiesters, which are unable to be assimilated by the cell without prior hydrolysis.

Functionally, glycerophosphocholine phosphodiesterase plays a pivotal role in many aspects of biotechnology, diagnostics, and drug development. The increased glycerophosphocholine phosphodiesterase activity because of the altered phosphatidylcholine metabolism in epithelial ovarian cancer cells can act as a diagnostic marker. In addition, glycerophosphocholine phosphodiesterase, serving as an estrogen-responsive uterine enzyme, can be present in the proestrous uterine secretion of several mammalian species. Besides, this enzyme has been suggested to have a critical function in the female reproductive tract. As the final product, glycerol-3-phosphate released on hydrolysis of seminal GPC by the enzyme has been found to be oxidized by epididymal sperm from most species of mammals. Therefore, to investigate the functional significance of this enzyme thoroughly, it is essential to be able to measure its activity accurately.

Equipped with the most advanced instrument, the leading techniques, and a group of extraordinary scientists, Creative Enzymes is completely qualified for providing the most precise enzymatic assay of glycerophosphocholine phosphodiesterase for our customers. The activity can be determined at 25℃ by measuring the production of glycerol-3-phosphate in a spectrophotometric assay. The results of our test are most reliable and trusted. Creative Enzymes has been partnering with its diverse and unique customers to support them in their process optimization needs. Overall, Creative Enzymes is your best partner who has been constantly promoting customers’ experience and improving the services and quality management system.

Enzyme Activity Measurement for Glycerophosphocholine PhosphodiesteraseFigure: The crystal structure of an Oleispira antarctica phosphodiesterase.

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