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Enzyme activity hinges on the ionization state of amino acid residues in the active site, which controls how well catalytic groups can donate or accept protons and stabilize transition states. In most enzymes operating in body fluids, the environment is near neutral, so the residues that act as acids, bases, or nucleophiles maintain the charge states needed for efficient catalysis. Around pH 7–8, these favorable charge states align to support proton transfer and substrate binding, yielding maximum activity. If the pH becomes more acidic (around 4–5), key groups may become over-protonated and lose their ability to participate in catalysis; if it becomes too alkaline (around 9–10), essential groups may be deprotonated and also hinder catalysis. That’s why the typical optimum for many enzymes is near neutral, roughly 7–8. There are exceptions, such as enzymes in the stomach that work best at acidic pH, but for the majority, neutral pH is where activity peaks.