Ligand Cu2+

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Basic Ligand Information

Molecular Structure

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Cu2+

JPVYNHNXODAKFH-UHFFFAOYSA-N

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Synonyms:

Cu(II), Cu2+in, Cu2+out, Cu2+[side 1], Cu2+[side 2], cupric ions, oxidized plastocyanin

Related pathways

BRENDA

photosynthesis

MetaCyc

cyclic electron flow, cytidylyl copper-molybdenum cofactor biosynthesis, NADPH to cytochrome c oxidase via plastocyanin, photosynthesis light reactions, succinate to cytochrome c oxidase via plastocyanin

Show all BRENDA pathways known for Cu2+

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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In Vivo Product in Enzyme-catalyzed Reactions (11 results)

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1.16.3.4

4 Cu+ + 4 H+ + O2 = 4 Cu2+ + 2 H2O

Substrate in Enzyme-catalyzed Reactions (17 results)

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1.16.3.4

4 Cu2+ + 2 H2O = 4 Cu+ + 4 H+ + O2

Product in Enzyme-catalyzed Reactions (13 results)

Activator in Enzyme-catalyzed Reactions (823 results)

the copper ion lies in an octahedral environment exhibiting Jahn-Teller distortion

741445

1.16.3.3

Cu2+ increases enzyme activation at low concentrations

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

682288

3.2.1.1

5 mM, 1.42fold activation

activates at 1 mM, inhibits at above 5 mM

750007

3.2.1.35

enhances the activity of the enzyme

stimulates activity at 5 mM by 20%

697502

2UWF, 3D-view

3.2.1.83

about 110% activity at 2 mM

slightly activating

0.1 mM, causes 4fold increase in activity

666325

7.1.2.1

at longer exposure times (8 days) of Cu2+, the enzyme exhibits 2.3fold increased activity

748613

Inhibitor in Enzyme-catalyzed Reactions (7111 results)

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

285929

1.1.1.142

21% inhibition at 0.1 mM

285940

1.1.1.144

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

740216

1.1.1.206

99% inactivation at 1 mM

100% inhibition at 0.1 mM

347984

1.1.1.214

1 mM, 67.8% residual activity

strong inhibitor

slight inhibition

slight inhibition

1 mM, less than 10% residual activity

almost complete inhibition of activity at 10 mM

slight inhibition at 1 mM

complete inhibition at 5 mM

702081

1.1.1.274

0.5 mM, strong inhibition

1 mM completely inactivates the enzyme

639094

1.1.1.283

enzymes MGR I and MGR II

10 mM, complete inhibition. Up to 80% renaturation by 100 mM EDTA

701082

1.1.1.304

1 mM, 0.2% of initial activity with substrate diacetyl, 1% with substrate 2,3-butanediol, respectively

737478

1.1.1.306

complete inhibition at 1 mM

strong inhibition at 2.5 mM

700822

1.1.1.334

5 mM, 8% residual activity

718331

1.1.1.345

complete inhibition at 0.1 mM

712292

1.1.1.346

strong inhibition at 0.5 mM

440304

1.1.1.357

67% inhibition at 0.5 mM

1 mM, 57% loss of activity. 5 mM, 64.8% loss of activity

1 mM, about 30% residual activity

760725

1.1.1.427

69% residual activity at 1 mM

10663

1.1.1.430

activity is completely restored by addition of EDTA

695731

1.1.1.431

strong inhibition at 2 mM

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

1 mM, 86% inhibition

5 mM, complete inhibition of activity

complete inhibition

complete inhibition at 10 mM

741032

1.1.5.3

specifically inhibits phenazine methosulfate coupled 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide reduction assay

complete inhibition at 1 mM

725738

1.1.99.18

4% residual activity at 100 mM

10 mM, 90% inhibition

644544

1.1.99.32

0.8 mM, complete loss of activity

677427

1.1.99.36

1 mM, 90% inhibition; 90% inhibition at 1 mM

strong

slight inhibition

85% inhibition at 1 mM

395329

1.11.1.11

inhibits the enzyme at 1 mM, complete inhibition at 5 mM

5 mM, 18% of initial activity

1 mM, 30% residual activity

743032

1.11.1.22

complete inhibition at 1 mM

722255

1.11.1.5

inhibition of NADH oxidizing activity

1 mM, 95% inhibition

0.01 mM, 80% inhibition

439626

1.13.11.17

1 mM, CuSO4, 25% inhibition

90% inhibition at 0.01 mM, 100% inhibition at 0.1 mM

439546

1.13.11.27

10 mM, complete inhibition

727448

1.13.11.29

85% inhibition at 0.1 mM

85% inhibition at 0.1 mM

1 mM, strong inhibition

207895

1.13.11.5

incubation with Fe2+ plus Cu2+ in equimolar concentrations inhibits

439393

1.13.11.50

20 mM Tris/HCl buffer, pH 7.5, 25°C, 1.2fold molar excess, reversible inactivation of wild-type and mutant enzyme through competition with Fe2+, substrates 200 microM pentane-2,4-dione, 330 microM quercetin, 330 microM potassium oxalate, 330 microM 3,4-dihydroxyphenylacetate

696107

1.13.11.52

0.005 mM, 50% inhibition

0.1 mM, complete inhibition

649382

4HVO, 3D-view

1.13.11.74

2.9% residual activity at 2 mM

721454

1.13.11.76

2 mM, 2.9% residual activity

strong inhibition

3.17% residual activity at 5 mM

776855

1.13.12.13

0.001 mM, 98% inhibition

689868

1.13.12.18

inhibits the light emission by dinoflagellate luciferase

0.5 mM, strong

inhibits activity by 80-95% at 0.01-0.05 mM

95% inhibition at 0.25 mM

complete inhibition at 1 mM

729124

1.14.11.48

0.04 mM, complete inhibition

731289

1.14.11.49

less than 5% activity at 1 mM

734171

1.14.11.55

more than 50% decrease in activity

10 mM Cu2+ inhibits the enzyme to about 50% residual activity

100% inhibition compared to the activity without any metal

50% inhibition at 0.017 mM

439040

1.14.13.128

0.2 mM, complete inhibition

707235

1.14.13.130

1 mM, 5 min incubation, complete inactivation

708366

1.14.13.148

0.2 mM Cu2+ inhibits the enzyme strongly without any preincubation

1 mM, moderate inhibition

684641

1.14.13.20

0.1 mM, complete loss of activity

completely

severe inhibition at 1 mM

438911

1.14.13.29

94% inhibition at 1 mM,crude enzyme extract

the enzyme is strongly inhibited by 1 mM Cu2+

complete inhibition

inhibits the enzyme in vitro and inactivate it in vivo, but also induce the enzyme in vivo in the first 24 h, overview

5 mM, 99% inhibition

complete inhibition at 0.1 mM

757086

1.14.14.18

0.2 mM, significant inhibition

438244

1.14.14.20

0.02 mM completely inhibits; complete inhibition at 0.02 mM

severely inhibits enzyme activity

0.0001 mM, 40% inhibition

25% inhibition at 1 mM

completely abolishes activity of WelO5 toward 12-epi-fischerindole U

748728

1.14.20.5

0.02 mM, complete inhibition in presence of 0.01 mM Fe2+

5 mM, xylanase activity decreases by 84%

767387

1.14.99.B10

5 mM, xylanase activity decreases by 84%

100% inhibition at 0.1 mM

strong inhibition

14% inhibition of hypoxanthine oxidation at 0.1 mM

1 mM, about 50% inhibition

strong inhibitor

inhibition is reversed by EDTA

complete inhibition at 1 mM

30-40% inhibition at 1.0 mM

44% inhibition in the presence of 1 mM

75% inhibition at 0.1 mM

390308

1.2.1.44

49% residual activity at 2 mM

inhibits NahF activity by 70%

691830

1.2.1.67

79% inhibition at 1 mM

762865

1.2.1.69

1 mM, strong inhibition

636460

1.2.1.70

1 mM CuCl2, 84% inhibition

655401

1.2.1.78

1 mM, complete inhibition

complete inhibition at 1 mM

1 mM, 12 h, 4°C, complete loss of activity

0.1 mM, no residual activity

partial inhibition

38% inhibition at 0.1 mM

0.36 mM, complete inhibition

40-50% inhibition

1 mM, about 55% of initial activity

slight inhibition

1 mM, 1% residual activity

0.5 mM 66% inhibition

390649

1.3.1.31

1 mM, 83% loss of activity

strong inhibition

inhibition at 0.1 mM

inhibitory

1 mM, 100% inhibition

739868

1.3.8.4

completely inhibits at 0.01 mM

1 mM, complete inhibition of the recombinant enzyme

656313

1.3.98.3

Cu2+ affects tetrapyrrole biosynthesis presumably at the level of the S-adenosyl-L-methionine and [4Fe-4S] containing HemN enzyme, copper targets the 4Fe-4S clusters in the anaerobic enzyme

10 mM

complete inhibition at 0.5 mM

742928

1.4.1.14

Cu2+ and Fe2+ are most inhibitory metal ions

slight

0.1 mM, strong inhibition

391694

1.4.1.26

complete inhibition at 0.5 mM

0.5 mM, 35% inhibition at pH 7.8, 30% inhibition at pH 8.9, cofactor NADP+

696177

1.4.2.1

55% inhibition at 1 mM

strong inhibition

90.7% residual activity at 1 mM

742035

1.4.3.10

inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme

complete inhibition at 10 mM

395986

1.4.3.14

59% residual activity at 1 mM

2.0 mM

inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation

0.13 mM, complete inhibition

strong inhibition at 1 mM Cu2+

1 mM, about 85% inhibition

741686

1.5.8.2

strong inhibition at 1 mM

0.03 mM, 65% inhibition, 0.1 mM, 90% inhibition, 1 mM, 100% inhibition

total inhibition at 1 mM

competitive inhibition

743879

1.6.3.2

92% inhibition at 0.1 mg/ml

743751

1.6.3.3

0.1 mM, complete inhibition

decrease of enzyme mRNA expression, via a transcriptional mechanism

673294

1.6.5.4

0.5 mM, complete inhibition

about 70% inhibition

81.76% residual activity at 5 mM

inhibition of dialyzed enzyme at 0.0005 mM

394261

1.8.1.13

relative activity less than 5%

strong inhibition

modeling of metal binding

394810, 394840, 394848

complete inhibition

0.15 mM, completely abolishes the rate of methylation of caffeoyl-CoA

0.1 mM, 58% inhibition

5 mM

1 mM, 96% inhibition

1 mM, 12% inhibition

1 mM, 93% inhibition

5 mM, complete inhibition

713321

2.1.1.239

0.1 mM, strong inhibition

715347

2.1.1.25

0.1 mM, no resiudal activity

5 mM, more than 90% inhibition

723404

2.1.1.276

5 mM, more than 90% inhibition

2.5 mM, 97% inhibition

complete inhibition

0.01 M, strong

5 mM, about 15% inhibition

725941

2.1.1.303

complete loss of activity

725380

2.1.1.316

completely inhibits the methylation reaction

729879

2.1.1.37

5 mM, 98% inhibition, inhibits both binding of DNA and activity

complete inhibition at 2 mM

1 mM, complete inhibition

441443

2.1.1.53

73% inhibition by 5 mM

above 1 mM

80% loss of activity

1 mM, 20-50% inhibition

complete inhibition

5 mM chloride salt, strong inhibitory effect, 50-100%, PpSABATH1

complete loss of activity

at higher concentrations

485776, 485777

2.1.3.1

inhibits AP3 production slightly at 0.5 mM

strong inhibition

1 mM, 75% inhibition

1 mM, complete loss of activity

96% inhibition at 2 mM

1 mM, strong

0.1 mM, complete inhibition

5 mM, strong inhibition

complete inhibition at 0.1 mM

720699

2.3.1.23

0.00001 mM, 50% inhibition, noncompetitive, irreversible, probably due to formation of a thiolate

42.3% inhibition

strong

80% decrease of activity at 0.01 mM

complete inhibition

79.5% residual activity after 1 h at 1 mM

5 mM, enzyme form B

50% decrease above 1 mM

487471

2.3.1.82

the growth of an amikacin-resistant Klebsiella pneumoniae strain is inhibited when amikacin is supplemented by the addition of Zn2+ or Cu2+ in complex with the ionophore pyrithione

1 mM, complete inhibition

488026

2.3.2.B14

complete inhibition at 1 mM

1 mM, 55% inhibition

1 mM

1 mM, 63% inhibition

0.01 mM, over 80% reduction in quercetin glucosylation activity

51.5% residual activity at 1 mM, 12% residual activity at 10 mM

strong

wild-type

86% inhibition at 10 mM

30% of maximal activity

10 mM, complete inactivation

2 mM, 80% inhibition

50% inhibition at 1 mM

0.75 mM, 40% inhibition

488822

2.4.1.194

strong inhibition at 1 mM and 10 mM

at 1 mM

5 mM, 3% remaining activity

complete inhibition at 10 mM

complete inhibition

complete inactivation at 1 mM

0.1 mM, complete inhibition. The observed enzyme inhibition by Cu2+ and Hg2+ may not solely be attributed to their effects on the enzyme itself because these heavy metal ions are known to destroy substrate anthocyanins

704415

2.4.1.279

1 mM, 98.7% inhibition

complete inhibition at 1 mM

720780

2.4.1.297

1 mM, 10% residual activity

2.2% residual activity at 5 mM

complete inhibition at 5 mM

749324

2.4.1.368

complete inhibition at 5 mM

750726

2.4.1.375

complete inhibition at 3 mM

758069

2.4.1.38

complete inhibition in presence of Mn2+

489555

2.4.1.384

less than 20% residual activity at 10 mM

1 mM, 49% inhibition of hydrolysis reaction, complete inhibition of transfer reaction; strong inhibition

735507

2.4.1.395

Cu2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)

25 mM, complete inhibition

489227

2.4.1.49

slight inhibition at 1 mM

20 mM, complete inhibition

637636

2.4.1.66

inhibits Mn2+-activated enzyme

1 mM, 50°C, 30 min, abolishes the phosphorolytic activity almost completely

in the presence of Mn2+

5 mM, significant inhibition

777666

2.4.2.1

41.5% residual activity at 5 mM

high inhibition when applied in high concentrations

20 mM, complete loss of activity

698648

2.4.2.49

high inhibition at 1 mM

1 mM, 99% inhibition

10 mM

strong

10 mM CuCl2, complete inhibition

strong

5 mM, about 90% loss of activity

strong inhibition

complete inhibition at 5 mM

17% activity at 1 mM

complete inhibition

1 mM, 68% decrease of activity

strongly inhibits O-acetyl-L-serine sulfhydrylation, moderately inhibites O-phospho-L-serine sulfhydrylation

655576

2.5.1.7

metal ions do not enhance the activity of enzymes, activity is inhibited by 10 mM

strong inhibition

strong

strong inhibition

0.004 M, 80% inhibition

ATP protects

1.6 mM, 3% inhibition; 1.6 mM, 97% inhibition

641084, 641086, 641090

2.7.1.222

the enzyme remains nearly inactive (less than 5%) with Cu2+

2 mM, 90% inhibition

strong

weak, 0.1 mM

0.5 mM, 50% inhibition in the presence of 3 mM Mg2+

0.25 mM CuCl2, complete inhibition

1 mM Cu2+ lowers the activity to 33%

copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview

58% residual activity in the presence of 4 mM

0.1 mM, 92% inhibition, 1 mM, complete inhibition

strong inhibition at 10 mM

inhibits uridylyl removing activity

strong inhibition

complete inhibition

strong inhibition at concentrations above 0.5 mM in presence of Mg2+

644293

2.8.1.1

more than 70% inhibition at 0.1 mM

645536

2.8.1.6

1 mM, almost complete inhibition

10 mM, complete inhibition

657791

2.8.2.21

above 1 mM, complete inhibition above 2 mM

elevated copper levels in the diet result in reduced enzyme levels in rat liver, strong inhibition in vitro and in vivo, 50% inhibition of purified enzyme at about 0.0025 mM, 50% inhibition in liver cytosol at about 0.025 mM

about 70% residual activity at 10 mM

753524

3.1.1.11

114105, 751232, 751541

0.001 mM, 30% inhibition

35% residual activity at 1 mM

1 mM, 55.6% of initial activity; 1 mM, 57.6% of initial activity; 1 mM, 8.5% of initial activity

1 mM, 25% inhibition

34% remaining activity after 5 min, 1 mM

85% inhibition at 1 mM

strong inhibition

1.0 mM, 72% relative residual activity

inhibits muscle isoform, not inhibitory to brain isoform

10 mM, 94.5% loss of activity

5 mM, 16% inhibition

required for activity, but inhibitory at 1 mM, two Cu2+ binding sites. Cu2+ ions function as a switch for its phosphodiesterase activity

1 mM, 100% inhibition

23906

3.1.2.4

at 1 mM causes more than 90% inhibition of activity

1 mM, no residual activity

1 mM

in presence of Mg2+, inhibition

134661, 719781, 727733, 751129

0.1 mM, 30% inhibition

5 mM

competitive

is effective only after preincubation, suggesting that the effect of the metal may be derived from lipid peroxidation due to Cu2+-induced oxyradical production

complete inhibition at 2 mM

38% reduction of enzyme activity at 10 mM

135474

3.1.4.45

reduces activity by 30-40%

135491

3.1.4.46

40% inhibition at 5 mM

646467

3.1.4.52

complete inhibition at 10 mM

135567, 135575, 135576

3.1.6.18

above pH 4.2, activation over pH-range 3-4.2, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate

646499

3.1.6.21

82.9% residual activity at 10 mM

1 mM decreases activity to 12% of control activity

288764

3.11.1.3

5 mM, 41% loss of activity

1 mM, complete inhibition

1.33 mM, 1.7% relative activity

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

strong inhibitory effect

88% inhibition at 1 mM

15.8% residual activity at 50 mM

64% residual activity at 2 mM

about 70% residual activity at 1 mM

inhibits activity at 1 mM, 1% relative activity compared with activity without any addition of effector

10 mM, 94% inhibition

about 30% residual activity at 5 mM

21% residual activity is detected after 24 h of incubation at 1mM Cu2+

1 mM, complete inactivation

1 mM, 50% inhibition

1 mM, 6% of initial activity

5 mM Cu2+ reduces the activity to 10%

about 10% residual activity at 1 mM

136762, 136763, 136767, 136768, 136771

208766, 208767, 208772, 208775

3.2.1.72

more than 90% inhibition

171555, 171557, 171568

almost complete inhibition

moderate inhibition at 1 mM

731044

3.2.1.85

5 mM, complete inactivation

about 5% residual activity at 5 mM

1 mM, 81% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 36% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis

10 mM, more than 90% loss of activity

749672

3.2.1.B50

60% inhibition at 5 mM

1 mM

10.6% residual activity at 0.1 M using inosine as substrate, 9.67% residual activity at 0.1 M using guanosine as substrate, complete inhibition at 0.1 M using adenosine as substrate

713705

3.2.2.21

5 mM, almost complete loss of activity

770698

3.2.2.23

preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA

slight inhibition

2 mM, complete inhibition

771930

3.2.2.29

complete inhibition at 5 mM

710481

3.2.2.5

the enzyme has two classes of Cu2+ binding sites, one activator site with high affinity and approximately six inhibitor sites with low affinity

marked inhibition at 1 mM

1 mM, complete inhibition

65-90% inhibition at 1 mM

1 mM, 51% of initial activity; 1 mM, 51% of initial activity

19.73% residual activity at 1 mM, complete inhibition at 5 mM

730765

3.4.11.3

35897, 35900, 35901, 35908

0.5 mM

about 50% residual activity at 1 mM

strong

36177, 36178, 36195, 586911

CuSO4

inhibits activity

69% inhibition at 0.01 mM

100% inhibition at 1 mM

0.2 mM, about 90% loss of activity, the inhibitory effect is not overcome by the presence of Co2+

1 mM, 93% inhibition

strong inhibition

inhibits S102H/G131H mutant at 0.76 mM, inhibition can be restored by addition of EDTA

650610

3.4.21.117

inhibition at low micromolar concentrations, structural basis for inhibition, overview; strong inhibitory effect

682553

2QXJ, 3D-view

3.4.21.19

gradual inhibition of enzyme expression in recombinant Bacillus subtilis strain at 1-10 mM

0.06 mM, 26% inhibition

23% inhibition of amidolytic activity at 1 mM

87% inhibition at 1 mM

at equilibrium two to three copper ions bind stoichiometrically to PK and destroy its activity. Initial reversible and weak binding phase and a slower, irreversible abolition of activity with a half-time of 6 min at saturating copper ion concentrations. PK digestion of cellular prion proteins and other proteins in brain homogenate is inhibited in a concentration-dependent manner at concentrations of more than 1 mM. Presence of calcium ions, up to 10 mM, has no effect on copper inhibition

inhibition of amidolytic activity

1 mM, 50% inhibition

competitive to other metal ions

1 mM, 77% of initial activity

inhibits at 2 mM

order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+, 50% inhibition at 0.012 mM

strong inhibition

Cu2+ inhibits the proteolytic activity of mature SpeB

residual activity in the presence of 20 mM: 0% free papain, 20% immobilized papain

5 mM decreases protease activity remarkably relative to the level of activity before the extra cations were added

1 mM, almost complete inhibition

24.86% residual activity at 5 mM

11.6% residual activity at 5 mM

inhibits 57% at 0.2 mM, 81% at 1 mM, and precipitates the enzyme at 5 mM

inhibitory below 5 mM

647645

3.4.23.12

strong inhibition of nepenthesin I and II by diazoacetyl-DL-norleucine in presence of cupric ions, no inactivation in absence of cupric ions

70% inhibition at 1 mM

39% inhibition at 1 mM, 52% at 5 mM

protease II

1 mM, complete inhibition

about 95% inhibition at 5 mM

0.1 mM

10 mM, 46% inhibition

5 mM, 37% inhibition

83.8% residual activity at 3.2 mM

731371

3.4.24.B4

10 mM, 15% residual activity

755300

3.4.26.1

3% residual activity at 0.087 mM

1 mM CuCl2, 53% inhibition

1 mM, 60% inhibition in presence of Mg2+

5.0 mM, complete inhibition

slight inhibition at 1 mM

strong inhibitor

288899, 770606, 771538

3.5.1.48

nearly complete inhibition at 1 mM

slight inhibition

1 mM: 74.4% inhibition

1 mM: 12% inhibition

1 mM

complete inhibition

2 mM, complete inhibition

1 mM

strain A, 1 mM: slight inhibition

0.2 mM, 33% inhibition

1 mM plus 0.1 mM Mn2+ complete inhibition

1 mM: 98% inhibition

10 mM

64% residual activity at 1 mM

0.01 mM

5 mM, inhibition to 22.58% of control

5 mM, almost complete loss of enzyme activity

777225

3.5.4.5

209644, 209649, 209660, 209661

2-mercaptoethanol partially protects

0.01 mM, 75% of maximal activity, 0.1 mM: 31.3% of maximal activity

slightly inhibits

no activity in the presence of Cu2+

complete inhibition at 10 mM

72% inhibition at 1 mM

719804

3.7.1.23

complete inhibition at 1 mM

slight inhibition

0.1 mM

1-5 mM, strong inhibition

5 mM

complete inhibition, not due to displacement of the native active site metal ion Fe2+

1 mM, 95% inhibition

1 mM, 26% loss of activity

0.1 mM, strong inhibition

4145

4.1.1.25

1 mM, 9.2% residual activity

partial

1 mM, 96% loss of activity

1 mM, 5.2% residual activity

strong

highly inhibitory at 20 mM

661799

4.1.1.90

free Cu2+ and Cu2+-complexes inhibit the reaction

695615

4.1.1.96

treatment severely affects the activity

strong

73% inhibition at 0.81 mM, complete inhibition at 8.06 mM

complete inhibition in the presence of Cu2+

687737

4.1.3.1

isoforms ICL1 and ICL2 are 60-80% inhibited by 5 mM Cu2+

748480

4.1.3.16

93% inhibition at 2 mM

10 mM, in presence of 2.5 mM Mg2+, 10% inhibition

5346

4.1.99.2

complete inhibition at 1 mM

complete inhibition at 1 mM

715552

4.2.1.11

leads to complete inhibition at 10 mM

716180

4.2.1.130

maximal inhibition below 0.025 mM

CuSO4

5 mM, strong inhibition; strong inhibition at 5 mM

0.1 mM, 100% inhibition

the inhibitory effect of metal ions is decreased in presence of 2-mercaptoethanol

above 0.01 M

10 mM, 19% residual activity

730968

4.2.2.13

10 mM, complete inactivation

inhibitory

1 mM, 50% inhibition

0.1 mM, 94% inhibition

suppresses the formation of geosmin by factor 3 or more

complete inhibition

about 85% residual activity at 1 mM

no activity when Zn2+, Ni2+ or Cu2+ is used as divalent metal ion

0.1 mM, about 20% of maximal activity

inhibition of both activities

strong

0.1 mM, 70% inhibition

partial inhibition

at 1 mM, 13.5% inhibition

648709

4.3.3.6

potent inhibitor, 26.8% residual activity at 10 mM

strong

strong inhibition

1 mM, 6.1% of initial activity, respectively; 1 mM, 7.5% of initial activity, respectively

749224

4.4.1.29

5 mM, complete inhibition

slight inhibition

5 mM, complete inhibition

1 mM, complete inactivation

inhibition of both activities

1 mM, complete inhibition

2507, 2511, 749062

weak

0.1 mM, 57% inhibition

1 mM, 8% residual activity

strong inhibition

1 mM, complete inhibition

0.5 mM in presence of 1 mM Mg2+, complete inhibition

in presence of 0.2 mM CoCl2

3340

5.4.2.8

in Tris buffer, no inhibition in histidine buffer

3350

5.4.3.10

has strong inhibitory effect on the enzyme activity

strong inhibition

5 mM, complete inhibition

723209

5.5.1.25

about 40% residual activity at 1 mM

inhibits ATPase activity, IC50: 0.13 mM

10 mM, complete inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+

192

6.2.1.11

589, 592

6.2.1.13

about 15% residual activity at 20 mM

744820

6.2.1.3

isoform Facl1 shows 64% residual activity and isoform Facl2 shows 33% residual activity at 1 mM

778, 779

0.13 mM, 50% inhibition

977, 978, 979

27% residual activity

0.04-4 mM: strong

1 mM, 100% inhibition

1333

6.3.4.2

inhibition is not reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM

forward reaction

partially inhibitory, ligation activity in presence of Mg2+

50% inhibition at 0.002 mM

competitive with plastoquinol

complete inhibition of Na+ transport at 0.08 mM

binding of approximately eight Cu2+ or Zn2+ ions inhibits basal ATPase activity

752057

7XUM, 3D-view

7.2.2.9

shown to inhibit the transport of cisplatin

689075

Metals and Ions (25967 results)

activates

increases the intracellular activity of mannitol dehydrogenase 1.6fold

activates the enzyme activity in vivo by 45% after a 40 days treatment of roots with over 0.05 mM Cu2+

670620

1.1.1.214

1 mM, 29.7% residual activity

strong inhibition

strong inhibitor

activates less than Zn2+

741455

1.1.1.30

10 mM, 2fold increase in activity

286515

1.1.1.365

135.3% activity at 5 mM

activates

weak activation

inhibits enzymatic activity

711501

1.1.1.6

presence of Mn2+ enhances the enzyme activity by 37.0%

740856

1.1.1.73

100% activity at 1 mM

slight inhibition

0.1 mM, residual activity: 1.3%

activates

rapid inactivation, can be restored by addition of dithiothreitol

389628

1.1.3.15

exposure of cells to mM copper sulfate, strong induction. Highest induction at 0.3 mM, about 16-fold increase in activity. Identification of a copper-response element in the 5'-region of the LctO gene

active site bound, required

726413