In a typical enzyme-catalyzed reaction, the enzyme binds one of the substrates with hydrogen bonds in its binding pocket. The substrate is activated (bonds stretch or deform) in the binding process.
The type of bonds which are never formed when a substrate fits into the active site of an enzyme are: C) Hydrophobic interactions.
An enzyme can be defined as a biological catalyst that typically speeds up or accelerates the rate of a chemical reaction by lowering the activation energy of its reactants.
This ultimately implies that, the rate of a chemical reaction is faster when its activation energy is low. Thus, an enzyme speeds up or catalyzes the rate of a chemical reaction by lowering its activation energy.
Furthermore, the ability of an enzyme to be joined (bind) with its substrates is limited when the conditions for the enzyme are not optimal.
Hence, enzyme structures are highly dependent on the particular chemical reaction and specific to the type of substrate they actively bond to.
On a related note, the type of bonds which are formed when a substrate fits into the active site of an enzyme are:
In conclusion, hydrophobic interactions are never formed when a substrate fits into the active site of an enzyme.
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