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Enzyme Activity Measurement for Galactokinase

After years of development and exploration, Creative Enzymes has ranked as a worldwide leader in providing enzyme assays. As a core value of our company tradition, we firmly believe that the quality of services is the fundamental requirement for our consecutive success. Creative Enzymes has continued to grow with that same entrepreneurial and innovative spirit bringing nature to science. Fully equipped with the most advanced spectrophotometric instruments, we are proud to offer the activity assay for galactokinase in a professional and timely manner.

In most organisms, the conversion of β-D-galactose to the more metabolically useful glucose 1-phosphate is accomplished by the action of four enzymes that constitute the Leloir pathway. Galactokinase (EC 2.7.1.6; ATP:alpha-D-galactose 1-phosphotransferase) catalyzes the second step in this pathway, namely the conversion of α-D-galactose to galactose 1-phosphate as indicated in figure 1. Galactokinase has attracted significant research attention for many years due to its important role in sugar metabolism and conversion. For example, defects in this enzyme in human result in the diseased state referred to as galactosemia. Also, most recently it has been developed via directed evolution to synthesize new natural and unnatural sugar-1-phosphates. Additionally, galactokinase-like molecules can serve as the sensors for the intracellular concentration of galactose and, under suitable conditions, function as transcriptional regulators.

Figure 1: The  Leloir pathway. The enzymatic steps involved in the conversion of b-D-galactose  1-phosphate. Figure 1: The Leloir pathway. The enzymatic steps involved in the conversion of b-D-galactose 1-phosphate.
Reference: Holden H M, et al. Cellular & Molecular Life Sciences Cmls, 2004, 61(19-20):2471-2484.

Galactokinases from various organisms including human, yeast, plants, and bacteria were isolated, expressed, and characterized. These enzymes exhibit distinct specific activities. For instance, galactokinase from Saccharomyces cerevisiae (ScGalK) is over 150 times more efficient than galactokinase from Escherichia coli (EcGalK). Moreover, substrate specificity studies revealed that galactokinase could tolerate modifications of galactose (Gal) at C-2 and C-6. For example, other than Gal, 2-deoxygalactose (Gal2D), and 6-deoxygalactose (Gal6D, also known as D-fucose) are possible substrates of EcGalK and ScGalK. Note that the galactokinases from mammals and from E. coli have no activity with N-acetyl-alpha-D-galactosamine. Probably because of the substrate diversity, the activity assays of galactokinase using spectrophotometry have not been well established in an industrial scale, although activity measurement using other methods was reported before. Creative Enzymes is fully competent to provide the most accurate enzymatic assay for galactokinase by spectrophotometric assays. The activity of galactokinase was measured spectrophotometrically by a coupled assay. The rate of conversion of alpha-D-galactose to alpha-D-galactose 1-phosphate was monitored by coupling the reaction with the formation of lactate from pyruvate in the presence of NADH. Therefore, the activity of galactokinase was determined at 340nm by measuring the formation of NADH.

Creative Enzymes is a leading company of high-quality bioanalytical services and contract research specialized in enzymatic analysis serving the needs of our clients from all over the world. The quality of our products is assured by many remarkable scientists who have been devoting their time on testing and optimizing the methods of enzymatic assays. Overall, Creative Enzymes is your best choice during development of products containing galactokinase.

Figure 2: The  crystal structure of galactokinase from S. cerevisiae
Figure 2: The crystal structure of galactokinase from S. cerevisiae.
PDB: 2AJ4



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CatalogEXWM-3090
ProductNamegalactokinase
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CAS No.9030-53-9
SourceE. coli
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