Literature summary for 2.1.1.6 extracted from

Patra, N.; Ioannidis, E.I.; Kulik, H.J.
Computational investigation of the interplay of substrate positioning and reactivity in catechol O-methyltransferase (2016), PLoS ONE, 11, e0161868 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
bidentate and monodentate binding modes of substrate catecholamine are close in energy but separated by a 7 kcal/mol free energy barrier. The driving force for monodentate catecholate orientations in classical molecular dynamics simulations is derived from stronger electrostatic stabilization afforded by alternate Mg2+ coordination with strongly charged active site carboxylates. Mixed semi-empirical-classical substrate C-O distances (2.7 A) for the bidentate case are in agreement with COMT X-ray crystal structures, as long as charge transfer between the substrates, Mg2+, and surrounding ligands is permitted. Free energy barriers for methyl transfer from bidentate and monodentate catecholate configurations are comparable at around 21-22 kcal/mol	Homo sapiens

Crystallization (Comment)

Organism

bidentate and monodentate binding modes of substrate catecholamine are close in energy but separated by a 7 kcal/mol free energy barrier. The driving force for monodentate catecholate orientations in classical molecular dynamics simulations is derived from stronger electrostatic stabilization afforded by alternate Mg2+ coordination with strongly charged active site carboxylates. Mixed semi-empirical-classical substrate C-O distances (2.7 A) for the bidentate case are in agreement with COMT X-ray crystal structures, as long as charge transfer between the substrates, Mg2+, and surrounding ligands is permitted. Free energy barriers for methyl transfer from bidentate and monodentate catecholate configurations are comparable at around 21-22 kcal/mol

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P21964	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + catecholamine	-	Homo sapiens	S-adenosyl-L-homocysteine + ?	-	?

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Release 2023.1 (January 2023)