Ligand Ag+

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Basic Ligand Information

Molecular Structure
Picture of Ag+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Ag
Ag+
FOIXSVOLVBLSDH-UHFFFAOYSA-N
Synonyms:
Silver ions

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (1 result)

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

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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

Substrate in Enzyme-catalyzed Reactions (2 results)

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

Product in Enzyme-catalyzed Reactions (2 results)

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

Inhibitor in Enzyme-catalyzed Reactions (762 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
complete inhibition at 1 mM
-
72% inhibition at 0.01 mM
-
0.005 mM, complete inhibition, prevented by 10 mM glutathione
-
78% inhibition at 0.01 mM
-
very powerful
-
complete inhibition of NAD dehydrogenase II at 0.018 mM
-
complete inhibition at 0.004 mM
-
IC50 = 0.005 mM
-
100% inhibition
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
0.1 mM, complete inhibition
-
D-carnitine dehydrogenase, 1 mM, complete inactivation
-
1 mM, 0.5% of initial activity with substrate diacetyl, 0.5% with substrate 2,3-butanediol, respectively
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM
-
decarboxylation of isocitrate and oxalosuccinate
-
1 mM, 99% inhibition
-
complete inhibition
-
strong inhibition
-
0.1 mM, complete inhibition
-
9.2% residual activity at 1 mM
-
complete inhibition at 1 mM
-
inhibition can be overcome by addition of dithiothreitol
-
1 mM, no residual activity
-
complete inhibition
-
0.1 mM AgNO3 complete inhibition
-
0.5 mM, 38% inhibition
-
1 mM, complete inhibition
-
98.1% residual activity at 2 mM
-
2 mM, 70% inhibition after 6 h
-
10 mM, 100% inhibition
-
1 mM, 60% inhibition
-
inhibition of intramolecular electron transfer, mechnanism
-
60% inhibition at 20 mM
-
98% inhibition at 0.01 mM
-
1 mM, about 80% inhibition of native enzyme, about 15% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
-
complete inhibition at 1 mM
-
inhibition of NADH oxidizing activity
-
1 mM, 97% inhibition
-
1 mM, 73% loss of activity
-
0.2 mM, complete inhibition
-
0.02 mM completely inhibits; complete inhibition at 0.02 mM
-
severely inhibits enzyme activity
-
100% inhibition at 0.5 mM
-
in ceruloplasmin, purified from sera of Ag-rats, two copper ions are substituted with two silver ions
-
complete inhibition at 1 mM
-
1 mM causes complete inhibition
-
100% inhibition with 1 mM
-
1 mM, complete inhibition
-
0.1 mM, no residual activity
-
1 mM, complete inhibition
-
1 mM, complete inhibition
-
67% inhibition at 1 mM
-
completely inhibits at 0.01 mM
-
1 mM, complete inhibition of the recombinant enzyme
-
0.1 mM, strong inhibition
-
0.01 mM in assay buffer
-
1 mM, no residual activity
-
strong inhibition
-
1 mM
-
0.13 mM, complete inhibition
-
strong inhibition at 1 mM Ag+
-
strong inhibition
-
45% inhibition at 1 mM
-
1 mM, about 85% inhibition
-
strong inhibition at 1 mM
-
1 mM
-
competitive inhibition
-
about 70% inhibition
-
1 mM, 92% inhibition
-
about 70% inhibition
-
0.01 mM, 90% inhibition
-
70% inhibition at 1 mM
-
1 mM, 94% inhibition
-
0.1 mM, no resiudal activity
-
strong
-
0.1 mM, 98% residual activity
-
0.000005 mM, almost complete inhibition, noncompetitive, irreversible, probably due to formation of a thiolate
-
; 26% remaining activity isoenzyme Nat-b; 30% remaining activity isoenzyme NAT-a
-
almost complete inhibition at 2 mM
-
at 0.4 mM
-
45% inhibition at 5 mM
-
0.75 mM, 40% inhibition
-
slight inhibition at 1 mM
-
weak
-
1 mM, strong
-
1 mM, complete inhibition
-
100% inhibition at 1 mM
-
complete inhibition at 0.1 mM
-
dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+
-
Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
-
13% inhibition at 1 mM
-
9.7% residual activity at 5 mM
-
33.2% residual activity at 1 mM
-
plasmalogen-specific PLA2
-
1 mM, complete inhibition
-
no activity at 1 mM AgNO3
-
5 mM, 77% inhibition
-
strong inhibition at 1 mM
-
1 mM, complete inhibition
-
potent inhibitor, inhibition reversed by adding an excess of dithiothreitol
-
strong, with p-nitrophenyl-beta-D-glucopyranoside as substrate
-
1 mM, 63% inhibition of endoglycoceramidase I, 94% inhibition of endoglycoceramidase II
-
1 mM AgNO3, 79% inhibition
-
1 mM, 80% inhibition
-
1 mM, 50% inhibition
-
0.3 mM, 20-25% inhibition
-
0.01 mM, 7% inhibition
no activity is detected after 1 h of incubation at 1mM Ag+
-
82% inhibition at 0.8 mM
-
5 mM, partial inhibition
-
AgNO3, recombinant and native enzyme
-
fast enzyme
-
more than 90% inhibition
-
5 min at 50ºC, 10mM, 100.0% of inhibition; 5 min at 50ºC, 1 mM, 100.0% inhibition
-
5 mM, complete inhibition of agarase AG-b
-
5 mM, 35% inhibition
-
extracellular enzyme, strong inhibition
-
1 mM, 34% residual activity
-
1 mM, 23% inhibition
-
1 mM, 68% inhibition
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase; at 2 mM 50% inhibition of NADase activity and 300% activation of cADPR activity
-
5 mM, more than 90% inhibition
-
complete inhibition at 0.1 mM
-
1 mM, 90% inhibition
-
1 mM, complete inhibition
-
1 mM AgNO3, complete inhibition
-
98% inhibition at 2 mM
-
1 mM: complete inhibition
-
complete inactivation at 1 mM
-
0.5 mM, complete inhibition of deamination of ATP
-
0.01 mM
-
6.5% inhibition at 2 mM
-
1 mM, inhibition 55%
-
0.01 mM, 93.8% of maximum activity, 0.1 mM: 2.5% of maximal activity
-
Ag+ concentrations in the range 0.001-0.01 mM lower the activity to less than 50% of its uninhibited value
-
0.02 mM
-
5 mM
-
complete inhibition at 20 mM
-
58.3% residual activity at 2 mM
-
over 90% inhibition at 1 mM
-
1 mM, 12% residual activity
-
complete inhibition at 1 mM
-
0.1 mM AgNO3, apoenzyme: 97% loss of activity, inactive enzyme complex with hydroxocobalamin: 19% loss of activity
-
irreversible
-
the inhibitory effect of metal ions is decreased in presence of 2-mercaptoethanol
-
100% reduced activity at 1 mM
-
0.1 mM, 92% inhibition
-
2 mM, 98.8% inhibition
-
complete
-
complete inhibition at 10 mM
-
1 mM, complete inactivation
-
88% inhibition at 1 mM
-
1 mM, about 90% inhibition
-
1 mM, complete inhibition
-
weak
-
1 mM
-
irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
-
9% residual activity at 1 mM
-
isoform Facl1 shows 64% residual activity and isoform Facl2 shows 71% residual activity at 1 mM
-
-
-
complete inactivation
-
1 mM, 100% inhibition
-
complete inhibition of Na+ transport at 0.1 mM
-

Metals and Ions (50 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 3.2% residual activity
-
strong inhibition
-
strong inhibitor
-
1 mM, 1.6fold activation, G6PDH-2
-
0.01 mM, residual activity: 0.2%
-
up to 4fold induction
-
37% inhibition of activity
-
inhibits enzymatic activity
-
stimulation
-
decreases activity
-
activation
-
2 mM, slight activation
-
0.2 mM, complete inhibition
-
activates 12% at 10 mM
-
stimulates
-
5 mM, complete inhibition
-
activates 15% at 1 mM
-
1 mM AgNO3 activates
-
stimulation
-
103.6% activity at 1 mM
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase; at 2 mM 50% inhibition of NADase activity and 300% activation of ADPR activity
-
1 mM, 416% of initial activity
-
1 mM, 131% of initial activity
-
1 mM, stimulates actvity up to 120%
-
inhibitory
-
PDI binds Ag+
-
activates ATPase activity
-
induces the efflux of potassium ions from cells
-

3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

Enzyme Kinetic Parameters

KM Value (1 result)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0626
-
-

Ki Value (8 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0016
-
at pH 8.0 and 50°C
0.0028
-
at 25°C in 50 mM Tris-HCl buffer (pH 7.0)
0.5
-
40°C
0.00321
-
pH 5.5, 37°C

IC50 Value (15 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.005
-
IC50 = 0.005 mM
0.0029877
-
at pH 8.0 and 50°C
0.019
-
pH 7.5, 50°C
0.015
-
at 25°C in 50 mM Tris-HCl buffer (pH 7.0)
0.00334
-
pH 5.5, 37°C
0.00375
-
pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity

References & Links