Literature summary for 2.1.1.6 extracted from

Sparta, M.; Alexandrova, A.N.
How metal substitution affects the enzymatic activity of catechol-O-methyltransferase (2012), PLoS ONE, 7, e47172.

Crystallization (Commentary)

Crystallization (Comment)	Organism
quantum mechanical/molecular mechanical dynamics analysis of the effect of metal substitution on the rate determining step in the catalytic cycle of COMT, the methyl transfer. In full accord with experimental data, Mg(II) bound to COMT is the most potent of the studied cations and it is closely followed by Fe(II), whereas Fe(III) is unable to promote catalysis. Ca(II) induces a repacking of the protein binding site, leading to a significant increase in the activation barrier and higher energy of reaction. The effect of metal substitution is different for different metals: for Fe(III) it is the electronic effect, for Ca(II) it is the effect of suboptimal protein structure	Homo sapiens

Crystallization (Comment)

Organism

quantum mechanical/molecular mechanical dynamics analysis of the effect of metal substitution on the rate determining step in the catalytic cycle of COMT, the methyl transfer. In full accord with experimental data, Mg(II) bound to COMT is the most potent of the studied cations and it is closely followed by Fe(II), whereas Fe(III) is unable to promote catalysis. Ca(II) induces a repacking of the protein binding site, leading to a significant increase in the activation barrier and higher energy of reaction. The effect of metal substitution is different for different metals: for Fe(III) it is the electronic effect, for Ca(II) it is the effect of suboptimal protein structure

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
Ca2+	quantum mechanical/molecular mechanical dynamics study	Homo sapiens
Fe3+	quantum mechanical/molecular mechanical dynamics study	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	may partly substitute for Mg2+	Homo sapiens
Mg2+	Mg(II) bound to COMT is the most potent of the studied cations	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P21964	-	-

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Release 2023.1 (January 2023)