The discovery of ribozymes (RNA catalysts) disproved the long-held belief that all enzymes are proteins.
When substrate is in excess, the reaction rate is directly proportional to enzyme concentration because every additional enzyme molecule can contribute to the product formation rate.
An enzyme accelerates both forward and reverse reactions equally by lowering activation energy without changing the equilibrium point or free energy.
Non-allosteric enzymes follow Michaelis-Menten kinetics, where the plot of V₀ vs. [S] is a rectangular hyperbola: first-order at low [S] and zero-order at high [S].
The triad allows histidine to act as a powerful general base catalyst, abstracting a proton from the serine hydroxyl group to make it a nucleophile.
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