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Figure 3 | BMC Structural Biology

Figure 3

From: Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking

Figure 3

Substrate in a tetrahedral reaction intermediate form analogous to the transition-state stabilised by the enzyme. A tetrahedral intermediate form of substrate and enzyme. The activated serine O γ attacks the carbonly oxygen of the substrate. The transition-state is stabilised by four hydrogen bonds (- - -) between the N-H-groups of the oxyanion hole and the substrate oxyanion, the oxygen of the substrate alcohol moiety and a side chain N-H-groups of the catalytic histidine and between the serine O γ and a side chain N-H-group of the catalytic histidine. The substrate is docked as a tetrahedral intermediate and includes the O γ and C β atoms, which are identical to those of the serine residue.

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