Neha Patil (Editor)

Serine hydrolase

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Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. 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:

  • Serine proteases, including trypsin, chymotrypsin, and subtilisin
  • Extracellular lipases, including pancreatic lipase, hepatic lipase, gastric lipase, endothelial lipase, and lipoprotein lipase
  • Intracellular lipases, including hormone sensitive lipase, monoacylglycerol lipase, adipose triglyceride lipase, and diacylglycerol lipase
  • Cholinesterases, including acetylcholinesterase and butyrylcholinesterase
  • Small molecule thioesterases, including fatty acid synthase and the acyl-CoA thioesterases
  • Some phospholipases, including phospholipase A2 and platelet activating factor acetylhydrolase
  • Protein and glycan hydrolases, including protein phosphate methylesterase 1, acyloxyacyl hydrolase and sialic acid acetylesterase
  • Some amidases, including fatty acid amide hydrolase
  • Some peptidases, including dipeptidyl peptidase 4, fibroblast activation protein, and prolylendopeptidase
  • References

    Serine hydrolase Wikipedia


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