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BRENDA support

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)

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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)

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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)

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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)

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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 (797 results)

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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
-
complete inhibition at 1 mM
-
IC50 = 0.005 mM
-
100% inhibition
-
complete inhibition at 1 mM
-
1 mM, complete inhibition
-
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
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complete inhibition at 1 mM
-
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
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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
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60% inhibition at 20 mM
-
98% inhibition at 0.01 mM
-
50% residual activity at 5 mM; 82% residual activity at 5 mM
-
complete inhibition at 1 mM
-
inhibition of NADH oxidizing activity
-
1 mM, 97% inhibition
-
1 mM, severely inhibited
-
1 mM, 73% loss of activity
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0.2 mM, complete inhibition
-
74.36% inhibition at 0.03 mM
-
0.02 mM completely inhibits; complete inhibition at 0.02 mM
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severely inhibits enzyme activity
-
complete inhibition at 1 mM
-
1 mM causes complete inhibition
-
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
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0.1 mM, strong inhibition
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0.01 mM in assay buffer
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1 mM, no residual activity
-
strong inhibition
-
1 mM
-
0.13 mM, complete inhibition
-
strong inhibition at 1 mM Ag+
-
45% inhibition at 1 mM
-
50% residual activity
-
1 mM, about 85% inhibition
-
strong inhibition at 1 mM
-
1 mM
-
competitive inhibition
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about 70% inhibition
-
1 mM, 92% inhibition
-
about 70% inhibition
-
0.01 mM, 90% inhibition
-
1 mM, 10.2% residual activity
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70% inhibition at 1 mM
-
1 mM, 94% inhibition
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0.1 mM, no resiudal activity
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strong
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0.1 mM, 98% residual activity
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0.000005 mM, almost complete inhibition, noncompetitive, irreversible, probably due to formation of a thiolate
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26% remaining activity isoenzyme Nat-b; 30% remaining activity isoenzyme NAT-a
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almost complete inhibition at 2 mM
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at 0.4 mM
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45% inhibition at 5 mM
-
0.75 mM, 40% inhibition
-
slight inhibition at 1 mM
-
weak
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1 mM, strong
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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+
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Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM
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13% inhibition at 1 mM
-
9.7% residual activity at 5 mM
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33.2% residual activity at 1 mM
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plasmalogen-specific PLA2
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1 mM, complete inhibition
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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
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strong, with p-nitrophenyl-beta-D-glucopyranoside as substrate
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1 mM, 63% inhibition of endoglycoceramidase I, 94% inhibition of endoglycoceramidase II
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1 mM AgNO3, 79% inhibition
-
1 mM, 80% inhibition
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1 mM, 50% inhibition
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0.3 mM, 20-25% inhibition
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0.01 mM, 7% inhibition
81% inhibition at 1 mM
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no activity is detected after 1 h of incubation at 1mM Ag+
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82% inhibition at 0.8 mM
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5 mM, partial inhibition
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AgNO3, recombinant and native enzyme
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fast enzyme
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more than 90% inhibition
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5 min at 50ºC, 10mM, 100.0% of inhibition; 5 min at 50ºC, 1 mM, 100.0% inhibition
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5 mM, complete inhibition of agarase AG-b
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5 mM, 35% inhibition
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extracellular enzyme, strong inhibition
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1 mM, 34% residual activity
-
1 mM, 23% inhibition
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1 mM, 68% inhibition
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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
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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
-
complete inhibition at 1 mM
-
complete inhibition
-
98% inhibition at 2 mM
-
1 mM: complete inhibition
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complete inactivation at 1 mM
-
0.5 mM, complete inhibition of deamination of ATP
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0.01 mM
-
6.5% inhibition at 2 mM
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1 mM, inhibition 55%
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0.01 mM, 93.8% of maximum activity, 0.1 mM: 2.5% of maximal activity
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Ag+ concentrations in the range 0.001-0.01 mM lower the activity to less than 50% of its uninhibited value
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0.02 mM
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5 mM
-
complete inhibition at 20 mM
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58.3% residual activity at 2 mM
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over 90% inhibition at 1 mM
-
1 mM, 12% residual activity
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complete inhibition at 1 mM
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0.1 mM AgNO3, apoenzyme: 97% loss of activity, inactive enzyme complex with hydroxocobalamin: 19% loss of activity
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irreversible
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the inhibitory effect of metal ions is decreased in presence of 2-mercaptoethanol
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100% reduced activity at 1 mM
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0.1 mM, 92% inhibition
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2 mM, 98.8% inhibition
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complete
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complete inhibition at 10 mM
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1 mM, complete inactivation
-
88% inhibition at 1 mM
-
1 mM, about 90% inhibition
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1 mM, complete inhibition
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weak
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1 mM
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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
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9% residual activity at 1 mM
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isoform Facl1 shows 64% residual activity and isoform Facl2 shows 71% residual activity at 1 mM
-
-
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complete inactivation
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1 mM, 100% inhibition
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complete inhibition of Na+ transport at 0.1 mM
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Metals and Ions (59 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 3.2% residual activity
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1 mM, no residual activity
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strong inhibition
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strong inhibitor
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1 mM, 1.6fold activation, G6PDH-2
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0.01 mM, residual activity: 0.2%
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up to 4fold induction
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1 mM, 1 h 30°C, partially reduced the activity to 88%
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37% inhibition of activity
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the enzyme activity is increased by 8.73% in the presence of 2 mM Ag+
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222.51% activity at 12.5 mM
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stimulation
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decreases activity
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activation
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2 mM, slight activation
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activates by 20% at 1 mM
-
0.2 mM, complete inhibition
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activates 12% at 10 mM
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stimulates
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5 mM, complete inhibition
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activates 15% at 1 mM
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1 mM AgNO3 activates
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stimulation
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103.6% activity at 1 mM
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1 mM, 3.2fold activation
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1 mM, no activity is retained
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1 mM, 416% of initial activity
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1 mM, 131% of initial activity
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1 mM, stimulates activity up to 120%
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inhibitory
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PDI binds Ag+
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activates ATPase activity
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induces the efflux of potassium ions from cells
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3D Structure of Enzyme-Ligand-Complex (PDB) (68 results)

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EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

KM Value (1 result)

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

Ki Value (8 results)

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

IC50 Value (20 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.005
-
IC50 = 0.005 mM
0.000662
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pH 4.0, 40°C
5
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at pH 4.0 and 50°C
0.0029877
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at pH 8.0 and 50°C
0.019
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pH 7.5, 50°C
0.015
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at 25°C in 50 mM Tris-HCl buffer (pH 7.0)
0.00334
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pH 5.5, 37°C
0.00375
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pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity

References & Links

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