Which statement about enzymes and their interactions is not correct?
The precise three-dimensional shape of an enzyme's active site is determined by its tertiary structure, which is maintained by hydrogen bonds, disulfide bridges, and ionic interactions between amino acid side-chains.
An enzyme will catalyze the hydrolysis of both the L\text{L}L- and D\text{D}D-enantiomers of a chiral dipeptide at identical rates because the covalent amide linkage being cleaved is planar and achiral.
A competitive inhibitor drug acts by binding to the active site of an enzyme, blocking the substrate from entering, and its design can be optimized using computer-aided molecular modeling.
Enzymes are highly stereospecific catalysts because they are constructed from chiral L\text{L}L-amino acids, resulting in an asymmetric active site.
