The research, published in the journal Nature, reveals a new mechanism by which enzymes can control chemical reactions. This mechanism, called "conformational selection," involves the enzyme changing its shape in order to bind to a substrate molecule and catalyze a reaction.
"This is a major breakthrough in our understanding of how enzymes work," said study lead author Dr. Andrei Tokmakoff, professor of chemistry in the UB College of Arts and Sciences. "For decades, scientists have believed that enzymes work by lowering the activation energy of a reaction, but our research shows that conformational selection is also a critical factor."
Activation energy is the energy required to start a chemical reaction. Enzymes lower the activation energy of a reaction by binding to the substrate molecule and providing a specific environment for the reaction to take place.
Conformational selection, on the other hand, is the process by which an enzyme changes its shape in order to bind to the substrate molecule. This change in shape allows the enzyme to more effectively catalyze the reaction.
The researchers studied the enzyme ketosteroid isomerase, which is involved in the metabolism of steroids. They used a variety of techniques, including X-ray crystallography and molecular dynamics simulations, to show that conformational selection is essential for the enzyme's activity.
"Our findings have important implications for the development of new drugs and treatments," said Dr. Tokmakoff. "By understanding how enzymes work, we can design drugs that can inhibit or activate specific enzymes, which could lead to new treatments for a variety of diseases."
The research team is now working to further investigate the role of conformational selection in enzyme catalysis. They are also developing new methods to use this knowledge to design new drugs.
