Among the oxidoreductases, the EC 1.17.4 group serves a distinctive function by utilizing a disulfide molecule as an acceptor in reactions involving CH-CH2 groups. EC 1.17.4 enzymes, classified under the broader category of oxidoreductases, are distinguished by their ability to catalyze reactions where a disulfide serves as an acceptor. This subclass encompasses a diverse array of enzymes, each exhibiting unique substrate specificity and catalytic mechanisms. Creative Enzymes is an industry leader in the field of enzyme assays, and our spectrophotometric assays help researchers accurately determine the activity of these enzymes.

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The reaction catalyzed by EC 1.17.4 enzymes can often be coupled with a secondary enzymatic reaction or chemical reaction, allowing for the direct or indirect measurement of the enzyme's activity. To determine EC 1.17.4 enzyme activity, suitable assays have been devised to monitor the production or consumption of specific products or substrates, e.g. in the case of an oxidoreductase acting on a CH-CH2 group with a disulfide as the acceptor, we can monitor the reduction of the acceptor by measuring the decrease in absorbance at a specific wavelength.

Role of EC 1.17.4 With a Disulfide as Acceptor

• Metabolism of Lipids. Enzymes classified as EC 1.17.4 are involved in the oxidation of fatty acids in lipid metabolism. They catalyze the formation of a thioester link and the reduction of coenzyme A (CoA) disulfide to CoA by transferring electrons from fatty acyl-CoA molecules to CoA disulfide.
• Synthesis of Steroids. EC 1.17.4 enzymes are involved in the biosynthesis of steroids. These enzymes catalyze the reduction of a disulfide-containing molecule during the synthesis of steroid hormones, such as cortisol and testosterone.
• Detoxification of Xenobiotics. EC 1.17.4 enzymes play a role in the detoxification of xenobiotics by catalyzing redox reactions, thereby increasing their water solubility and facilitating excretion.
• Regulation of Cellular Redox Balance. EC 1.17.4 Enzymes participate in the redox reactions of thiol-disulfide exchange and influence changes in the intracellular redox state thereby contributing to the regulation of cellular redox homeostasis.

Significance of Studying With a Disulfide as Acceptor

EC 1.17.4 Enzyme assays and analyses are of great importance and have broad implications for chemical and biological research. In addition, elucidation of the catalytic mechanism and structural features of EC 1.17.4 enzymes can provide insights into enzyme evolution, protein engineering, and drug discovery, and guide advanced and reliable strategies for innovative therapeutic interventions and biotechnological applications.

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Creative Enzymes is dedicated to enzyme research, and based on our advanced enzyme activity analysis platform, we play an important role in helping researchers understand enzyme function and application. If you are interested in us, please feel free to contact us.