. Author manuscript; available in PMC: 2015 May 3.

Published in final edited form as: Pharmacogenet Genomics. 2009 Jan;19(1):87–89. doi: 10.1097/FPC.0b013e32830fbde4

Table 3.

The binding energy of 2-OH-E₂ and 4-OH-E₂ with the wild-type human S-COMT and the mutant S-COMT (D51G/S60F/K162R).

Genotype	Substrate	Site of O-methylation	ΔE_binding
Wild-type	2-OH-E₂	2-O-methylation	−124.5
	2-OH-E₂	3-O-methylation	−121.9
	4-OH-E₂	3-O-methylation	−122.9
	4-OH-E₂	4-O-methylation	−123.2
Mutant (D51G/S60F/K162R)	2-OH-E₂	2-O-methylation	−135.4
	2-OH-E₂	3-O-methylation	−148.7
	4-OH-E₂	3-O-methylation	−138.5
	4-OH-E₂	4-O-methylation	−143.4

ΔE_binding was calculated with this equation: ΔE_binding = Ecomplex − (E_COMT + E_substrate), where E_complex is the potentical energy for the complex of COMT with substrate, E_COMT is the potential energy of the enzyme itself and E_substrate is the potential energy for the substrate itself.