Enzymes play a crucial role in biological systems, facilitating a wide range of biochemical reactions necessary for life. Among the many classes of enzymes, oxidoreductases are of particular importance. Within this class, EC 1.17.7 enzymes, which act on CH-CH2 groups with an iron-sulfur protein as an acceptor, have garnered significant attention. These enzymes exhibit unique catalytic abilities that make them valuable tools in chemical and biological research. As a leader in enzyme assays, Creative Enzymes contributes significantly to the advancement of the study and use of these enzymes by assisting researchers in precisely determining the activity of these enzymes through the use of our spectrophotometric assays.

What do We Offer for Enzyme Activity Measurement?

We mainly utilize spectrophotometry for quantitative assessment in the activity assay of EC 1.17.7 enzymes. Spectrophotometry provides a non-invasive and highly sensitive method to monitor these electron transfer reactions, and in the activity assay of EC 1.17.7 enzymes Showing good results in activity assays, the technique relies on the ability of these enzymes to catalyze the transfer of electrons from substrates to iron-sulfur protein receptors. We can accurately monitor the progress of an enzymatic reaction by analyzing the change in absorbance of light at specific wavelengths, selecting the appropriate wavelength for the redox reaction involved, and then correlating the spectrophotometric measurements with the conversion of substrate to product to determine the enzyme Kinetics and activity.

Our procedure as follows:

• Preparation. Isolate the enzyme and substrate under controlled conditions.
• Baseline Measurement. Record the initial absorbance of the reaction mixture.
• Enzyme Addition. Introduce the enzyme to initiate the reaction.
• Monitoring. Continuously measure absorbance at appropriate wavelengths.
• Data Analysis. Calculate enzyme activity based on the rate of change in absorbance over time.

The Role of EC 1.17.7 With an Iron-Sulfur Protein as Acceptor

Enzymes of EC 1.17.7 are essential to numerous physiological and metabolic functions. The preservation of redox balance in cells depends on their capacity to catalyze the passage of electrons from CH-CH2 groups to an iron-sulfur protein acceptor. Numerous energy responses, such as the metabolism of lipids, carbohydrates, and amino acids, depend on this mechanism. Furthermore, the manufacture of essential cellular constituents including coenzymes and cofactors is aided by EC 1.17.7 enzymes. Furthermore, because they have the ability to catalyze the conversion of toxic substrates into less dangerous products, these enzymes play a crucial role in the detoxification of harmful substances. Given the abundance of EC 1.17.7 enzymes in liver and kidney cells, this detoxification mechanism is especially significant in these tissues.

Significance of Studying EC 1.17.7 With an Iron-Sulfur Protein as Acceptor

• Pharmaceutical Development. Understanding the enzymatic mechanisms of EC 1.17.7 offers insights into drug targets for metabolic disorders, cancer, and infectious diseases. Inhibitors or activators targeting this enzyme may serve as potential therapeutics.
• Biotechnological Applications. EC 1.17.7 finds applications in biotechnology, including the production of biofuels, pharmaceutical intermediates, and fine chemicals. Harnessing its catalytic capabilities enables the development of efficient biocatalytic processes.
• Environmental Bioremediation. By aiding in the breakdown of organic contaminants, enzymes such as EC 1.17.7 contribute to the repair of contaminated sites and the preservation of ecosystems in environmental bioremediation.

Our service workflow

Creative Enzymes has a wealth of service experience in enzyme assays, and we offer enzyme activity assays based on spectrophotometric methods. The methodology we offer plays various of roles in biosynthesis, energy metabolism and redox regulation, and provides reliable solutions for therapeutic interventions, biotechnological innovations and environmental management. If you are interested in us, please feel free to contact us.