Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome.[1] A defining characteristic of these enzymes is the presence of a nucleophilic serine in their active site, which is used for the hydrolysis of substrates. Catalysis proceeds by the formation of an acyl-enzyme intermediate through this serine, followed by water/hydroxide-induced saponification of the intermediate and regeneration of the enzyme. Unlike other non-catalytic serines, the nucleophilic serine of these hydrolases is typically activated by a proton relay involving a catalytic triad consisting of the serine, an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine), although variations on this mechanism exist.

Superfamilies of serine hydrolases includes:

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  1. ^ Simon GM, Cravatt BF (April 2010). "Activity-based proteomics of enzyme superfamilies: serine hydrolases as a case study". J. Biol. Chem. 285 (15): 11051–5. doi:10.1074/jbc.R109.097600. PMC 2856978. PMID 20147750.