Ligand Ag+

a robust inhibitor of the enzymatic acetylation mediated by AAC(6')-Ib in vitro. Addition of silver acetate to to AAC(6')-Ib harboring Acinetobacter baumannii and Escherichia coli cultures results in a dramatic reduction of the resistance to aminoglycosides

776428

2.3.1.84

3 entries

2.3.3.16

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

636851

2.5.1.39

complete inhibition at 0.1 mM

dose-dependent, reversible, non-competitive inhibition, complete inhibition at 0.1 mM Ag+

704733

2.7.4.3

Ag+ inhibits the adenylate kinase activity from 20% to 60% when its concentration varies from 0.01 to 0.5 mM

701686

2.8.2.24

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

64-87% inhibition

no activity at 1 mM AgNO3

5 mM, 77% inhibition

strong inhibition at 1 mM

about 20% residual activity at 10 mM

775454

3.2.1.100

1 mM, complete inhibition

potent inhibitor, inhibition reversed by adding an excess of dithiothreitol

not

strong, with p-nitrophenyl-beta-D-glucopyranoside as substrate

646668

3.2.1.123

1 mM, 63% inhibition of endoglycoceramidase I, 94% inhibition of endoglycoceramidase II

1 mM, 33.76% of initial activity

1 mM, inhibition to 15% of control

1 mM, 80% inhibition

1 mM, 50% inhibition

0.3 mM, 20-25% inhibition

654923

3.2.1.17

0.01 mM, 7% inhibition

81% inhibition at 1 mM

754434

3.2.1.194

complete inhibition at 100 mM

no activity is detected after 1 h of incubation at 1mM Ag+

1 mM, 23% inhibition

26846, 26849, 26875, 26876, 713791

3.2.1.32

3 entries

3.2.1.35

82% inhibition at 0.8 mM

complete inhibition at 10 mM

136615, 136618, 136625

3.2.1.55

9 entries

3.2.1.57

5 mM, partial inhibition

AgNO3, recombinant and native enzyme

fast enzyme

136762, 136763, 136766, 136767, 136769, 136770, 136771

more than 90% inhibition

5 min at 50ºC, 1 mM, 100.0% inhibition; 5 min at 50ºC, 10mM, 100.0% of inhibition

5 mM, inhibition to 93% of control

5 mM, 35% inhibition

extracellular enzyme, strong inhibition

171738

3.2.1.99

1 mM, 34% residual activity

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

326409

3.3.2.10

5 mM, more than 90% inhibition

complete inhibition at 0.1 mM

1 mM, 90% inhibition

647189, 647195, 647224

42% residual activity at 2 mM

733171

3.5.1.101

1 mM, complete inhibition

692156

3.5.1.105

1 mM AgNO3, complete inhibition

complete inhibition at 1 mM

complete inhibition

98% inhibition at 2 mM

1 mM: complete inhibition

complete inhibition at 1 mM

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

over 90% inhibition at 1 mM

1 mM, 12% residual activity

complete inhibition at 1 mM

715552

4.2.1.30

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

about 50% residual activity at 10 mM

747854

4.2.2.14

100% reduced activity at 1 mM

649368

4.2.2.18

slight inhibition (no less than 88% residual activity)

both enzyme forms IM3796 and IM1634 are completely inhibited by 5 mM Ag+

772952

4.2.2.21

complete inhibition at 5 mM

768746

4.2.2.3

complete inhibition at 1 mM

773868

4.2.3.2

0.1 mM, 92% inhibition

137597

4.2.99.22

2 mM, 98.8% inhibition

complete

complete inhibition at 10 mM

1 mM, complete inactivation

648796

5.1.1.15

88% inhibition at 1 mM

1 mM, about 90% inhibition

727188

5.3.1.14

1 mM, complete inhibition

weak

2740, 2747, 660647

1 mM

73% inhibition at 1 mM

768674

5.3.1.8

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

977, 978, 979

complete inactivation

706061

6.3.3.3

1 mM, 100% inhibition

complete inhibition of Na+ transport at 0.1 mM

732808

Metals and Ions (66 results)

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1.1.1.184

1 mM, 3.2% residual activity

724049

1.1.1.214

1 mM, no residual activity

strong inhibition

strong inhibitor

1 mM, 1.6fold activation, G6PDH-2

688308

1.1.1.90

0.01 mM, residual activity: 0.2%

724027

1.1.3.15

up to 4fold induction

687389

1.1.3.6

1 mM, 1 h 30°C, partially reduced the activity to 88%

763627

1.1.99.29

37% inhibition of activity

activates

the enzyme activity is increased by 8.73% in the presence of 2 mM Ag+

222.51% activity at 12.5 mM

stimulation

decreases activity

5 mM, 157.4% of initial activity

770866

3.1.4.3

1 mM, activation to 149.8% of control

activation

2 mM, slight activation

activates by 20% at 1 mM

753408

3.2.1.158

10 mM, slightly promotes the enzymatic activity

activates

0.2 mM, complete inhibition

720759

3.2.1.2

activates 12% at 10 mM

stimulates

2.5-3.0fold activation at pH 6.5 and 10.0, respectively

772096

3.2.1.51

5 mM, complete inhibition

666408

3.2.1.52

activates 15% at 1 mM

1 mM AgNO3 activates

stimulation

10 mM, slightly promotes the enzymatic activity

773891

3.2.1.B1

103.6% activity at 1 mM

1 mM, 3.2fold activation

756271

3.8.1.2

1 mM, no activity is retained

757261

4.2.2.10

1 mM, 416% of initial activity

747235

4.2.2.11

1 mM, 131% of initial activity

730133

4.2.2.2

1 mM, stimulates activity up to 120%

inhibitory

PDI binds Ag+

activates ATPase activity

246928

7.2.2.6

induces the efflux of potassium ions from cells

3D Structure of Enzyme-Ligand-Complex (PDB) (69 results)

Enzyme Kinetic Parameters

K_M Value (1 result)

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7.2.2.15

0.0626

210452

K_i Value (8 results)

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1.6.2.4

0.0016

at pH 8.0 and 50°C

743879

2.7.3.3

0.0028

at 25°C in 50 mM Tris-HCl buffer (pH 7.0)

704733

3.1.1.20

0.5

40°C

653585

3.2.1.21

0.00321

pH 5.5, 37°C

715732

4.2.1.1

4 entries

IC₅₀ Value (26 results)

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1.1.1.188

0.005

IC50 = 0.005 mM

389454

1.1.3.4

0.000662

pH 4.0, 40°C

at pH 4.0 and 50°C

0.0029877

at pH 8.0 and 50°C

743879

1.8.1.9

0.019

pH 7.5, 50°C

0.015

at 25°C in 50 mM Tris-HCl buffer (pH 7.0)

704733

3.2.1.21

0.00334

pH 5.5, 37°C

0.00375

pH 6.0, 30°C, inhibition of ferredoxin:NAD+ oxidoreductase activity

732808

References & Links

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Show Reference (1128 entries)

Links to other databases for Ag+

Ligand Ag+

Basic Ligand Information

Roles as Enzyme Ligand

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

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

Substrate in Enzyme-catalyzed Reactions (2 results)

Product in Enzyme-catalyzed Reactions (2 results)

Inhibitor in Enzyme-catalyzed Reactions (845 results)

Metals and Ions (66 results)

3D Structure of Enzyme-Ligand-Complex (PDB) (69 results)

Enzyme Kinetic Parameters

KM Value (1 result)

Ki Value (8 results)

IC50 Value (26 results)

References & Links

Literature References (1128)

Links to other databases for Ag+

K_M Value (1 result)

K_i Value (8 results)

IC₅₀ Value (26 results)