Ligand Cu+

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Basic Ligand Information

Molecular Structure
Picture of Cu+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Cu
Cu+
VMQMZMRVKUZKQL-UHFFFAOYSA-N
Synonyms:
Cu(I), Cu+[side 1], Cu+[side 2], reduced plastocyanin
Pathway Source
Pathways


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

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (19 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cu+/in = ADP + phosphate + Cu+/out
show the reaction diagram

In Vivo Product in Enzyme-catalyzed Reactions (23 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cu+/in = ADP + phosphate + Cu+/out
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cu+/in = ADP + phosphate + Cu+/out
show the reaction diagram

Product in Enzyme-catalyzed Reactions (37 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cu+/in = ADP + phosphate + Cu+/out
show the reaction diagram
-

Inhibitor in Enzyme-catalyzed Reactions (22 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
60-70% inhibition
-
1 mM, 70% residual activity
-
0.001-0.01 mM, 93% loss of activity
-
soluble enzyme form sMMO
-
pMMO
-
strong, complete inhibition at 0.1 mM
-
presence of Cu+ inhibits noncompetitively with respect to the substrate GSSG and NADPH and inactivates with the cleavage of a peptide bond of the enzyme. Inactivation/fragmentation is prevented by addition of catalase
-
13.6% residual activity at 1 mM
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
-
1 mM, CuCl, 56% inhibition
-
1 mM, 83.1% loss of activity
-
inhibition of phosphatase activity and epoxide hydrolase activity
-
0.087 mM, 97% inhibition
-
complete inhibition at 20 mM
-
strong inhibition at 1 mM, activates at 0.1 mM
-

Metals and Ions (80 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 234% activity
-
0.14 molecules of Cu+ per enzyme molecule for the purified enzyme, and 0.23 molecules of Cu+ per enzyme molecule after dialysis against Ag+, Ni2+, Zn2+, and Cu+ ions
-
108.6% activity at 1 mM
-
activates
-
5 mM, 2fold activation
-
1 mM, stimulates
-
the enzyme can bind 10 Cu+/mol and form a tetramer
-

3D Structure of Enzyme-Ligand-Complex (PDB) (91 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (5 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (9 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.007
-
pH and temperature not specified in the publication

Ki Value (3 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.00035
-
pH 7.8, 37°C

References & Links

Links to other databases for Cu+

ChEBI
PubChem
ChEBI
PubChem