CHE242 FA18 Activity05_ 091918 Name: nformation ne way the enzyme-bound states a
ID: 147458 • Letter: C
Question
CHE242 FA18 Activity05_ 091918 Name: nformation ne way the enzyme-bound states are stabilized is through formation of non-covalent interactions etween the enzyme and the substrate. 11. Compare the magnitude of AGs and AGes. Which form of the substrate does the enzyme bind best? How do you know? 12. As develop a summary statement about the source of the free energy stabilization for the a group, enzyme-transition state complex. Consider the change in enthalpy (energy associated with non covalent interactions) when non-covalent interactions (very weak "bonds") are formed. rnto vn more tightly than the enzyme shown in maExplanation / Answer
The enzyme's ability to make the reaction faster depends on the fact that it stabilizes the transition state. The transition state's energy or, in terms of a reaction, the activation energy is the minimum energy that is needed to break certain bonds of thereactants so as to turn them into products.
Catalysts lower the activation energy for reactions. The lower the activation energy for a reaction, the faster the rate. Thus enzymes speed up reactions by lowering activation energy. Many enzymes change shape when substrates bind.
In summary, enzymes are proteins that lower the activation energy of a chemical reaction. Enzymes are not consumed or produced in a reaction, but they are catalysts that allow the reaction to proceed at a faster rate. ... Together, they form the enzyme-substrate complex.