Ligand Cu2+

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Basic Ligand Information

Molecular Structure
Picture of Cu2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Cu
Cu2+
JPVYNHNXODAKFH-UHFFFAOYSA-N
Synonyms:
Cu(II), Cu2+in, Cu2+out, Cu2+[side 1], Cu2+[side 2], cupric ions, oxidized plastocyanin
Pathway Source
Pathways


Show all pahtways known for Show all BRENDA pathways known for Cu2+

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Substrate in Enzyme-catalyzed Reactions (52 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Product in Enzyme-catalyzed Reactions (32 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (554 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
the copper ion lies in an octahedral environment exhibiting Jahn-Teller distortion; the copper ion lies in an octahedral environment exhibiting Jahn-Teller distortion
-
about 130% activity at 1 mM
-
very rapid induction of enzyme accompanied by accumulation of both phosphatidic acid and phosphatidylbutanol. Highest activity 2 h after copper addition, decrease thereafter. Enhanced enzyme gene expression contributes to the increase in activity
-
5 mM, 1.42fold activation
-
activates at 1 mM, inhibits at above 5 mM
-
enhances the activity of the enzyme
-
stimulates activity at 5 mM by 20%
about 110% activity at 2 mM
-
0.1 mM, causes 4fold increase in activity
-
at longer exposure times (8 days) of Cu2+, the enzyme exhibits 2.3fold increased activity
-

Inhibitor in Enzyme-catalyzed Reactions (5387 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
10 mM, complete inhibition. Activity can partly be restored by addition of EDTA
-
0.05 mM to 0.5 mM, 50% inhibition with 0.1 mM, uncompetitive vs. NAD+, non-competitive vs. prostaglandin E2
-
21% inhibition at 0.1 mM
-
5 mM, complete inhibition, prevented by 5 mM glutathione
-
98% inhibition at 0.01 mM
-
IC50 = 0.4 mM
-
5 mM concentration
-
complete inhibition at 2 mM
-
1 mM, 14.0% residual activity; 1 mM, 44.2% residual activity
-
85% inhibition at 2 mM
-
47% inhibition at 1 mM
-
99% inactivation at 1 mM
-
100% inhibition at 0.1 mM
-
strong inhibitor
-
slight inhibition
-
slight inhibition
-
1 mM, less than 10% residual activity
-
strong inhibition at 1 mM
-
almost complete inhibition of activity at 10 mM
-
slight inhibition at 1 mM
-
complete inhibition at 5 mM
-
0.5 mM, strong inhibition
-
1 mM completely inactivates the enzyme
-
enzymes MGR I and MGR II
-
10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA
-
1 mM, 0.2% of initial activity with substrate diacetyl, 1% with substrate 2,3-butanediol, respectively
-
complete inhibition at 1 mM
-
activity is completely restored by addition of EDTA
-
strong inhibition at 2.5 mM
-
5 mM, 8% residual activity
-
complete inhibition at 0.1 mM
-
strong inhibition at 0.5 mM
-
67% inhibition at 0.5 mM
-
completely inhibits reduction of 2-dehydropantolactone
-
67% inhibition at 0.5 mM
-
1 mM, 40% loss of activity
-
50% inhibition at 12.96 mM; 50% inhibition at 13.0 mM
-
complete inhibition at 1 mM
-
5 mM, 88% inhibition
-
slight
-
weak inhibition
-
complete inhibition at 10 mM
-
specifically inhibits phenazine methosulfate coupled 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide reduction assay
-
complete inhibition at 1 mM
-
4% residual activity at 100 mM
-
10 mM, 90% inhibition
-
0.8 mM, complete loss of activity
-
1 mM, 90% inhibition; 90% inhibition at 1 mM
-
strong
-