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Acid–base catalysis is one of the most common and fundamental strategies used by enzymes to accelerate biochemical reactions. In this mechanism, specific groups within the enzyme’s active site participate directly in the making and breaking of bonds by donating or accepting protons. Unlike reactions in solution, where acids and bases are usually limited to hydronium or hydroxide ions, enzymes employ functional groups of amino acid side chains to act as acids or bases, thereby increasing reaction rates under mild physiological conditions. A key general feature of enzymatic acid–base catalysis is the involvement of ionizable amino acid residues such as histidine, aspartate, glutamate, lysine, tyrosine, cysteine, and sometimes _______ _____ ________ ___ __________ _________ _________ _____.
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