Final answer:
The statement is false; amino and hydroxyl groups are activating groups, but enzymes, which act as biological catalysts, are often necessary to lower the activation energy for biochemical reactions to proceed.
Step-by-step explanation:
The statement 'Amino and hydroxyl groups are so activating that catalysts are often not necessary' is false. While amino and hydroxyl groups are indeed activating, meaning they increase the reactivity of certain chemical species towards others, the presence of enzymes, which are biological catalysts, is often required to lower the activation energy of chemical reactions to a level where the reaction can occur at a biologically feasible rate. Enzymes have active sites with specific functional groups that catalyze the reaction by activating the substrate as a nucleophile, electrophile, acid, or base. These functional groups often include amino acid residues like histidine, cysteine, aspartic acid, arginine, and glutamic acid which are critical for the enzyme's catalytic action.
For instance, in amino acid activation, aminoacyl tRNA synthetases catalyze a reaction where ATP is hydrolyzed to form a high-energy bond between an amino acid and adenosine monophosphate (AMP), allowing the amino acid to be further transferred to tRNA in the process of protein synthesis. This reaction is essential for the stabilization of the resulting molecule and plays a critical role in the activation of the amino acid.