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Results 1 - 7 of 7
EC Number
Metals/Ions
Commentary
Reference
Ca2+
interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects
Ca2+
isoform ROMT-15, poorly substitutes for Mg2+; isoform ROMT-17, poorly substitutes for Mg2+
Co2+
isoform ROMT-15, may substitute for Mg2+; isoform ROMT-17, may substitute for Mg2+; the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 41% of the activity with Mg2+ (with quercetin as substrate); the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Co2+ shows 82% of the activity with Mg2+ (with quercetin as substrate)
Mg2+
interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects
Mg2+
isoform ROMT-15, required; isoform ROMT-17, required; the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (with quercetin as substrate); the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity (with quercetin as substrate)
Mn2+
the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 69% of the activity with Mg2+ (with quercetin as substrate); the enzyme is metal-dependent, Mg2+ is the best cation for catalytic activity, Mn2+ shows 74% of the activity with Mg2+ (with quercetin as substrate)
Zn2+
isoform ROMT-15, poorly substitutes for Mg2+; isoform ROMT-17, poorly substitutes for Mg2+
Results 1 - 7 of 7