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EC 1.3.5 is a classification within the Enzyme Commission numbering system that refers to oxidoreductases, a group of enzymes responsible for catalyzing oxidation-reduction reactions in various biological processes. Specifically, EC 1.3.5 encompasses oxidoreductases that act on CH-CH groups as donors and utilize quinone or related compounds as acceptors. Creative Enzymes is an industry leader in enzyme activity measurement. Based on our extensive experience and advanced technology, we provide accurate and reliable enzyme activity measurement services. Our enzyme activity measurements are characterized by high precision, especially for oxidoreductases including quinone or related compound as acceptor.
Figure: Porcine succinate dehydrogenase embedded in the mitochondrial inner membrane.
Reference: Van Vranken JG, et al. Crit Rev Biochem Mol Biol. 2015;50(2):168-80.
We can precisely determine EC 1.3.5 enzyme activity using spectrophotometry, which plays a crucial role in understanding the function and kinetics of oxidoreductases that act on the CH-CH moiety using quinone or related compounds as receptors. This method involves measuring the changes in absorbance of light at specific wavelengths resulting from enzyme-catalyzed reactions. To initiate the spectrophotometric assay, the enzyme, the CH-CH group-containing substrate, and the quinone or related acceptor compound are incubated together under controlled conditions. Over time, the enzyme catalyzes the transfer of electrons from the CH-CH group to the acceptor, resulting in measurable absorbance changes. By monitoring the absorbance at specific wavelengths corresponding to the characteristic peak of the reduced or oxidized form of the quinone compound, the enzyme activity can be determined quantitatively. This method allows us to measure the rate of the enzymatic reaction, infer the catalytic efficiency, and evaluate the effect of various factors, such as pH, temperature, and substrate concentrations.
EC 1.3.5 enzymes are engaged in multiple pathways within biological systems. One notable pathway is the respiratory chain, where they participate in the transfer of electrons during oxidative phosphorylation. In this process, electrons derived from the oxidation of CH-CH groups are transferred via quinone or related compounds to molecular oxygen, driving ATP synthesis. Another pathway involving EC 1.3.5 enzymes is the biosynthesis of coenzyme Q, an essential component of the electron transport chain. In this pathway, the enzyme catalyzes the transfer of electrons from CH-CH groups to quinone precursors, subsequently leading to the formation of coenzyme Q. Furthermore, in photosynthetic organisms, EC 1.3.5 enzymes are vital for the synthesis of plastoquinones. Plastoquinones participate in electron transfer reactions during photosynthesis, where they shuttle electrons from photosystem II to photosystem I, ultimately allowing for the generation of energy-rich molecules.
The study of EC 1.3.5 enzymes and their associated reactions holds significant importance in both chemical and biological research. Understanding the mechanisms by which these enzymes transfer electrons from CH-CH groups to quinone or related compounds expands our knowledge of energy metabolism, respiration, and photosynthesis. This knowledge facilitates the development of therapeutic strategies targeting enzymes involved in electron transfer processes. Furthermore, the ability to measure and characterize the activity of EC 1.3.5 enzymes through spectrophotometric assays aids in enzyme engineering, drug discovery, and the optimization of industrial bioprocesses. EC 1.3.5 enzymes with a quinone or related compound as an acceptor play a critical role in oxidation-reduction reactions involving CH-CH groups.
Creative Enzymes is able to rapidly test the activity of purified enzymes and other forms of enzyme-containing solutions. Our specialized protocols and extensive experience guarantee a high-quality service.
