Enzyme Activity Measurement for 3-Hydroxypropionate Dehydrogenase Using Spectrophotometric Assays

Creative Enzymes is an expert in enzyme activity measurement for oxidoreductases, including 3-hydroxypropionate dehydrogenase. The quality of our results is assured with the most advanced spectrophotometric instruments and the outstanding team of brilliant scientist. We have been focused on enzyme activity assays for years and promise to deliver satisfactory results.

3-Hydroxypropionate dehydrogenase (EC1.1.1.59) is an enzyme that catalyzes the oxidation reaction of 3-hydroxypropanoate to produce 3-oxopropanoate, using the NAD⁺ as the redox cofactor. This enzyme exists in bacteria and eukarya, such as Bacillus cereus, Escherichia coli, Gallus gallus, and Sus scrofa. This enzyme is a member of the group of oxidoreductases that catalyze the CH-OH group of the substrate and use NAD⁺ or NADP⁺ as the cofactor. The systematic name of this enzyme class is 3-hydroxypropanoate: NAD⁺ oxidoreductase. The enzyme plays an important role in multiple pathways, including:

• acrylate degradation;
• alanine metabolism;
• beta-alanine biosynthesis II;
• beta-Alanine metabolism;
• Metabolic pathways;
• Propanoate metabolism;
• propanoyl-CoA degradation II

3-Hydroxypropionate dehydrogenase is the third enzyme of the acrylate degradation pathway. Acrylate is a product during dimethylsulfoniopropanoate (DMSP) and acrylonitrile degradation Some organisms are able to utilize acrylate as the sole carbon source, such as Halomonas sp. First, acrylate is converted to 3-hydroxypropanoate, which is then catabolized by 3-hydroxypropionate dehydrogenase to 3-oxopropanoate. In the end, 3-oxopropanoate is further converted to acetyl-CoA and CO2. Then the products of this pathway will participate in the tricarboxylic acid (TCA) cycle I pathway. Due to its valuable function in various biological processes, the enzyme activity measurement for 3-hydroxypropionate dehydrogenase becomes critically important. The spectrophotometric assay is demonstrated to be a reliable method for activity quantification of the enzyme. The catalytic activity of 3-hydroxypropionate dehydrogenase can be measured by following either the reduction of NAD⁺ at 260nm or the oxidation of NADH at 340nm, using the spectrophotometric analysis. Creative Enzymes has been working hard to provide the unparalleled service for our customers. We surpass our competitors with a quick turnover of the activity assays in response to the request of either a typical activity determination or a customized request. Overall, Creative Enzymes is your trustworthy partner during development of products containing 3-hydroxypropionate dehydrogenase.

Figure: The pathway: acrylate degradation which 3-hydroxypropionate dehydrogenase catalyzed. (From BsubCYC)