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. 2013 Feb 4;110(8):E653–E661. doi: 10.1073/pnas.1221050110

Fig. 1.

Fig. 1.

The acylation mechanism of a Ser protease. After substrate binding, the Ser side chain attacks the scissile peptide bond to generate a tetrahedral oxyanion intermediate. Protonation of the amine leaving group allows collapse of the intermediate and formation of an acyl-enzyme species. Dashed bonds represent the hydrogen bond of the oxyanion hole. See text for details.