Ligand manganese(2+)

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

1.13.11.55

1 mM, 65.5% inhibition

663712

1.13.11.71

inhibits by 13% at 5 mM

2 mM, 31% residual activity

strong inhibition

69.4% residual activity at 10 mM

0.5 mM, strong

60% inhibition at 0.25 mM

439174

1.14.11.48

0.04 mM, about 80% inhibition

731289

1.14.11.49

less than 15% activity at 1 mM

734171

1.14.11.55

more than 50% decrease in activity

slight inhibition

slight inhibition

1 mM, moderate inhibition

684641

1.14.13.24

complete inhibition at 5 mM

complete inhibition at 5 mM

0.001-0.01 mM, complete inhibition

50% inhibition at 0.01 mM

676182

1.14.16.4

50% inhibition at 0.01 mM

0.4 mM, 95% inhibition

439275

1.14.20.14

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

748728

1.14.20.6

about 85% inhibition at 1 mM; about 95% inhibition at 1 mM

weak inhibition

strong inhibitory effect, about 20% residual activity at 10 mM

inhibitory

1 mM, isozyme A, 20% inhibition, isozyme C, 44% inhibition

390215

1.2.1.22

50% inhibition at 10 mM

288133

1.2.1.23

30-40% inhibition at 1.0 mM

84.8% residual activity at 1 mM

690591

1CW3, 3D-view

1.2.1.36

50% inhibition at 0.024 mM

slight

inhibits and activates

741787

1.2.1.44

21% residual activity at 2 mM

partial

1 mM causes 37% inhibition

390325

1.2.1.5

89% residual activity at 1 mM

725948

1.2.1.78

10 mM, about 30% inhibition

1 mM, 12 h, 4°C, 44% loss of activity

1 mM, 15.2% inhibition

1 mM, about 65% of initial activity

moderately inhibited by 1 mM

1 mM: less than 20% inhibition

396193

1.3.1.31

1 mM, 21.7% loss of activity

only after preincubation with cation

complete inhibition at 1 mM

711884

1.3.1.98

markedly inhibits stimulatory effect of K+

286064

1.3.3.3

inhibition above 5 mM

390978

1.3.3.5

65.77% residual activity at 10 mM

765695

1.3.3.6

has no significant effect on enzyme activity up to 10 mM

746061

1.3.8.8

1 mM, 72% inhibition of the recombinant enzyme

1 mM, 60% inhibition

0.5 mM, 52% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9

696177

1.4.3.11

about 65% residual activity at 1 mM

5 mM, 45% inhibition

almost total inhibition at 0.1 mM

30% inhibition at 1 mM

394961

1.5.3.24

63% residual activity at 2 mM

moderate inhibition

0.1 mM, about 20% inhibition

722881

1.6.3.4

0.1 mM, about 20% inhibition

not inhibitory at 1 mM

strong inhibition

5 mM MnSO4, 82% loss of activity

394028

1.9.6.1

1 mM, 72.7% residual activity

moderate inhibition

1 mM, 59% inhibition

inhibits TNMT activity by 41%, can be prevented by the inclusion of EDTA; inhibits activity by 41%, inhibition prevented by inclusion of 10 mM EDTA

5 mM

above 1 mM

1 mM: 21% inhibition, 10 mM: 57% inhibition

1 mM, 48% inhibition

5 mM, complete inhibition

2.5 mM, 35% inhibition

5 mM, about 15% inhibition

725941

2.1.1.316

4-fold decrease of enzyme activity

729879

2.1.1.35

inhibits at low concentrations

31% inhibition at 5 mM

714532

2.1.1.396

31% inhibition at 5 mM

1 mM, 43% inhibition

26% inhibition by 5 mM

relative activity 24% of control

675589

2.1.1.9

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

723371

2.1.1.B75

complete loss of activity

5 mM, 31% inhibition

0.1 mM

20 mM, 50-60% inhibition

486245

2.3.1.125

35% inhibition at 2 mM

486246

2.3.1.15

2 mM, 82% residaul activity; slightly decreases activity, relative activity: 81.5% (2 mM)

706284

2.3.1.157

2 mM, inhibits D-glucosamine-1-phosphate N-acetyltransferase activity

slight

73% inhibition at 2.5 mM

673153

2.3.1.22

85.5% inhibition at 2.5 mM, inhibition of Mg2+ and bovine serum albumin is antagonistic

673153

2.3.1.222

0.1 microM, 82% residual activity; 0.2 microM, 40% residual activity

2 mM, 80% inhibition

in crude enzyme extract

50% inhibition above 10 mM

weak

relative activity: 71%

strong, above 5 mM

50% inhibition at 5 mM

in the presence of 2 mM MnCl2, the activity of the enzyme decreases to 34%. The enzyme activity is not detectable in the presence of 100 mM MnCl2

5 mM, 16% residual activity

above 25 mM

slight inhibition

0.1-10 mM: 20-80% inhibition

639510

2.4.1.128

40.9% residual activity at 1 mM, complete inhibition at 10 mM

above 10 mM, wild-type

at high concentration

2 mM, 20% inhibition

45% inhibition at 10 mM

weak effect

at concentrations above 40 mM

349719

2.4.1.218

10 mM, 24.7% inhibition

5 mM, 82% loss of activity

747674

2.4.1.269

divalent cation inhibit in decreasing order: Sr2+, Ni2, Co2+, Ca2+, Mn2+, Zn2+

723506

2.4.1.295

10% inhibition at 1 mM

strong inhibition at 5 mM

10 mM, 16% inhibition

47.41% residual activity at 5 mM

inhibitory in presence of optimal Mg2+-concentration

20 mM, 40% inhibition below pH 8.0

slight inhibition

10 mM, 16% decrease in activity

756726

2.4.1.7

5 mM, 5% loss of activity

5 mM, significant inhibition

777666

2.4.2.17

moderate inhibitory effect

1 mM, 80.3% inhibition

above 10 mM

10 mM, 98% inhibition

723806

2.4.2.6

reduces base exchange activity by 87-99% at 1 mM

10 mM

weak

90% inhibition at 5 mM

719293

2.5.1.106

inhibitory above 5 mM

723120

2.5.1.136

complete inhibition at 5 mM

13% activity at 1 mM

5 mM, 6% activity

required, activates up to 5 mM, inhibitory above 5 mM

above 2 mM

weak

about 35% loss of activity

760121

2.5.1.68

optimal at 0.1 mM, the enzyme absolutely requires a divalent cation, inhibition by Mn2+ at higher concentration of 5.0 mM

order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+

reduced activity

enzyme is inhibited by an excess of free divalent metal ion, Mg2+ or Mn2+

above 6 mM

about 70% activity at 2.5 mM

50 mM inhibit

3.5 mM, instead of Mg2+, almost complete inhibition

1.6 mM, 50% inhibition

680522

2.7.1.165

93% activity in the presence of 10 mM Mn2+ compared to Mg2+

696906

2.7.1.174

abolishes detectable DAG kinase activity

200 mM

strong inhibition above 1 mM

the enzyme remains nearly inactive (less than 5%) with Mn2+

760894

2.7.1.227

5 mM, 80% loss of activity

above 1 mM

in excess, activating below

excess free divalent cations inhibit the enzyme

can partially replace Mg2+ in activation, inhibition above 0.5 mM at 1 mM ATP

inhibits forward reaction above 0.5 mM

641628

2.7.1.45

divalent cation required, most effective at a ratio of Mn2+ and ATP of 1:3, deviation from this ratio is inhibitory at several concentration levels

5 mM

21% residual activity at 3 mM

738585

2.7.1.66

complete inhibition at 0.01 M

at a Mn2+/ATP ratio of more than 2

at 1 mM, in presence of 1 mM Mg2+, strong inhibition, but activation in absence of Mg2+

at 1 mM or above

inhibitory above 1 mM

663291

8F6M, 3D-view

2.7.10.4

inhibitory at concentrations higher than 3 mM

free Mn2+

492113, 492129, 492135

2.7.11.21

10 mM Ca2+ inhibits the enzyme activity, 5 mM is used in assay conditions

above 20 mM

at high concentrations noncompetitive inhibition of MgATP2-

642459

2.7.3.8

1.67 mM, 49% inhibition

slight inhibition

complete inhibition above 0.4 mM

5 mM

strong inhibition at 10 mM

53% of the activation with Mg2+, excess of Mn2+ inhibits the reaction in both directions

can partially replace Mg2+ in activation, inhibits in presence of Mg2+

643471

1CKN, 3D-view

2.7.7.53

weak, NDP-arsenolysis or NDP/phosphate-exchange reaction

643510

2.7.7.65

18% inhibitin at 10 mM

RNA synthesis with the Thermococcus kodakaraensis primase complex is stimulated about 2fold by the presence of Mn2+, whereas the size of RNA chains is marginally affected. DNA synthesis is slightly inhibited by Mn2+

slight stimulation, in presence of Mg2+ inhibition

above 2 mM

4 mM, about 40% inhibition

at high concentration inhibits the phosphate, diphosphate exchange reaction

645432

2.7.9.2

divalent metal ion Mg2+ or Mn2+ required for forward reaction, inhibition at high concentrations of Mg2+ or Mn2+

645468

2.8.2.11

1-10 mM: enhances activity, 20-35 mM: inhibition

645698

2.8.2.20

above 30 mM, activation below

645805

2.8.2.24

inhibitory at 10 mM, stimulating at 1 mM

61% residual activity at 100 mM

730283

3.1.1.117

1 mM, slight inhibition; slight inhibition at 1 mM

58% residual activity at 1 mM

716353

3.1.1.25

22.7% residual activity at 1 mM

713789

3.1.1.26

12.2% residual activity in the presence of 50 mM Mn2+

low inhibition at 1 mM

729073

3.1.1.42

1 mM, 83% of initial activity

1.0 mM, 79% relative residual activity

2 mM, complete inactivation

3 mM gradually decreases activity about 5fold

with RNA core as substrate

1 mM, 50% inhibition

addition to the medium reduces the activity in vivo

at pH 8.5, a Mn2+ concentration of 2.5 mM and higher inhibits activity

752190

3.1.21.B1

1 mM, 90% residual activity

5 mM, about 90% inhibition

3 mM, 64% inhibition

addition of MN2+ decreaseds the reaction rate both without and in combination with Mg2x05

inhibition above 0.4 mM

at 1 mM inhibitory effect

6.5% of maximal activity with 0.1 mM denaturated DNA, 8.4% with 0.5 mM polydeoxythymidylic acid as substrate, competitive inhibition

isozyme Nuc1 activity drops sharply at 5 mM concentration; isozyme Nuc2 activity decreases with an increase in Mn2+ concentration

at 0.05-5 mM, inhibition is completely reversed by Ca2+

90% inhibition at 1 mM

20.5% inhibition at 2 mM

slight inhibition at lower concentrations

IC50: 0.1 mM for 65 kDa BPP hydrolase, 15.0 mM for 20 kDa BPP hydrolase

95170

3.1.7.5

1.0 mM, complete inhibition of isoenzyme PII, 4% inhibition of isoenzyme PI

2 mM, 93% inhibition

addition of 0.1 mM MgCl2 increases the activity 1.5-fold. 10 mM MnCl2 results in greater than 90% inhibition

71% inhibition at 1 mM

slight inhibition

1 mM, 18% loss of activity

1 mM, 25.45% of initial activity

2 mM, 40% of initial activtiy

737518

3.2.1.145

68.4% residual activity at 50 mM

about 75% residual activity at 5 mM

768769

3.2.1.152

34% residual activity at 2 mM

strong inhibition

86.7% residual activity at 5 mM

5 mM, 39.6% residual activity

reduces activity

1 mM, 14% inhibition

significantly reduces the activity of BiAF96A_Aq at the concentration of 10 mM

1 mM, 4% loss of activity

1 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited

strong inhibition at 10 mM

slight inhibition at 50 mM, beta-D-fucosidase II less affected

strong inhibition at 5 mM

136690, 136691, 136693

about 50% residual activity at 1 mM

136758, 136769, 136770, 136771

more than 90% inhibition

moderate inhibition at 1 mM

731044

3.2.1.85

5 mM, inhibition to 28% of control

5 mM, 14% inhibition

6 mM, 46% inhibition

IFO 3134, completely

MnCl2 inhibits activity of, 5 mM, 26% inhibition

692397

3.2.1.B44

10 mM, about 40% loss of activity

2 mM, 22% residual activity

771950

3.2.2.29

complete inhibition at 5 mM

1 mM, 69% inhibition

7-DMATS shows 84.0% relative activity at 5 mM Mn2+, FgaPT1 shows 69.7% relative activity at 5 mM Mn2+

0.1 mM, more than 80% of the residual activity

19.38% residual activity at 5 mM

0.5 mM

1 mM, 30% inhibition

partial

10 mM

at 0.1 mM 76% activity relative to control

weak inhibition

partially inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 85.3% and 48.9% residual activity for chymotrypsin A and B, respectively

inhibition at 10 mM

0.06 mM, 14% inhibition

0.01 mM, 73% residual activity

717858

3.4.21.96

1 mM, 78% of initial activity

753957

3.4.21.B66

11% inhibition at 5 mM

addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition

above 1 mM, activates below 1 mM

5 mM, about 47-67% residual activity

moderate inhibition

2.5 mM, strong

slight inhibition

slight inhibition

inhibits 81% at 5 mM, 42% at 1 mM

730765

3.4.22.B8

inhibitory concentration: 5-10 mM

647645

3.4.23.18

85.9% residual activity at 10 mM

752341

3.4.23.20

98% residual activity at 10 mM

753904

3.4.23.21

about 36% residual activity at 10 mM

protease II

above 1-2 mM, native or apoenzyme

1 mM, weak, reactivates after inhibition with chelating agents

ADAMTS13 activity is decreased in the presence of 0.9 mM Ni2+

51% inhibition at 1 mM

5 mM, 37% inhibition

10 mM, 2.5% residual activity

755300

3.4.25.1

inhibits peptidylglutamyl peptide hydrolase activity

partial loss of activity is observed with the combination Mn2+

659296

3.5.1.137

96% residual activity at 1 mM

60% inhibition at 1 mM

strong inhibitor

50% inhibition, 1 mM

slight inhibition

2 mM, 58% inhibition

slight

low inhibition

1 mM: 13% inhibition

81% residual activity at 1 mM for IsoI and 51% residual activity at 1 mM for IsoII; inhibition of isozymes IsoI and IsoII

689405

3.5.2.6

49% residual activity at 0.01 mM

1 mM, 11% loss of activity

769827

3.5.3.7

5 mM complete inhibition

1 mM, 58% inhibition

5 mM, inhibition to 72.62% of control

5 mM, reduces activity by 34.3%

addition of 0.002 M reduces activity by 50% or more

2 mM, 20% inhibition

0.01 mM 30% inhibition

PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2

about 90% residual activity at 10 mM

inhibitory at all concentrations tested

strong inhibitor

at higher concentrations

210137

3.6.1.6

complete inhibition at 10 mM

2.5 mM Mn2+ blocks the helix unwinding by the enzyme

0.2 mM

Saccharolobus solfataricus recombinase RadA can utilize Mn2+ to stimulate strand invasion and reduce ADP-binding stability

776822

3.7.1.25

the activity of isoform HODHI is decreased by about 50% in the presence of Mn2+

247051

3.7.1.9

isoenzyme HODHI is inhibited, isoenzyme HODHII is activated

MnSO4

1-5 mM, strong inhibition

5 mM

slight

10 mM, over 90% inhibition

1.0 mM, 50% inhibition

strong

slightly

50% inhibition at 1 mM

720149

4.1.2.10

10 mM, 17% inhibition

about 20% inhibition

strong inhibition above 1 mM

65% inhibition at 10 mM; kidney enzyme, 65% inhibition at 10 mM

5255

4.1.3.3

20% residual activity at 10 mM

33337

4.1.3.43

100% activity at 0.1 mM and 1 mM chloride salt

721615

4.1.99.2

complete inhibition at 1 mM

45% inhibition at 1 mM

high concentrations

0.2 mM, about 50% loss of activity

90% inhibition

completely abolishes activity with 5-oxo-D-proline, stimulates activity with D-glutamate

above 0.01 M

about 62% residual activity at 1 mM

enzyme form IM3796 is inhibited to about 15% residual activity by 5 mM Mn2+

1 mM, 63% of initial activity; 1 mM, 63% of initial activity

about 58% residual activity at 1 mM

771346

4.2.2.7

1 mM, about 30% inhibition

inhibitory

inhibitory above 0.5 mM

663768

4.2.3.25

maximal activity is obtained with Mn2+ at 0.5 mM, but is inhibited as Mn2+ concentration increases to 10 mM

775848

4.2.3.27

activates at low concentration below 0.1 mM, inhibits at higher concentrations

667375

4.2.3.38

activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate

694926

4.2.3.39

highly activating at 0.060 mM, inhibiting at 0.12 mM

above 0.03 mM

above 0.02 mM

0.01 mM, can partially replace Mg2+, inhibition at higher concentration

648334

4.2.3.66

inhibitory above 0.2 mM, stimulation below

713324

4.2.3.7

divalent metal required, Mg2+ or Mn2+, inhibition above 2.5 mM

648597

4.2.3.70

may substitute for Mn2+ at 0.1 mM, inhibitory above

above 0.2 mM

concentrations higher than 0.1 mM are inhibitory

50 mM, 50% loss of activity

747154

4.3.1.2

2 mM, 9.6% loss of activity

at 1 mM, 92.8% inhibition

648709

4.3.3.6

32.7% residual activity at 10 mM

0.1 mM, weak

5 mM, 12% inhibition

25 mM, complete inhibition

2-5 mM, 50% inhibition

above 3 mM

10 mM, about 40% inhibition

causes 20% inhibition at 5 mM; causes 20% inhibition at 5 mM; causes 20% inhibition at 5 mM

0.8 mM

slightly inhibitory at 1 mM

slight inhibition of enzyme form I and II, strong inhibition of enzyme form III

80% reduced activity

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

3300

5.4.2.8

complete inhibition above 2 mM

649781

5.4.99.15

51% residual activity at 1 mM, at 50°C in 50 mM phosphate buffer (pH 7.0)

activates, best divalent metal ion, optimal at 0.08 mM, about 20% of maximal activity at 1 mM, complete inhibition at 5 mM; activates, best divalent metal ion, optimal at 0.08 mM, about 20% of maximal activity at 1 mM, complete inhibition at 5 mM; activates, best divalent metal ion, optimal at 0.08 mM, about 25% of maximal activity at 1 mM, complete inhibition at 5 mM

5 mM, 43% inhibition

at concentrations about 0.1 mM

25% reversible inhibition of Mg-ATPase activity

289226

5.6.2.3

9% inhibition of DNA helicase activity, the RNA helicase activity is not affectd by Mn2+ at 1 mM

769158

5.6.2.5

9% inhibition of DNA helicase activity, the RNA helicase activity is not affectd by Mn2+ at 1 mM

769158

6.2.1.3

isoform Facl1 shows 28% residual activity and isoform Facl2 shows 40% residual activity at 1 mM

can satisfy the metal ion requirement at low concentrations, at high concentrations Mn2+ markedly inhibits

inhibition above 5 mM

977

1N2H, 3D-view

6.3.2.3

the enzyme activity is strongly inhibited by Mn2+ even in the presence of 10 mM Mg2+

weak

above 2 mM

above 2 mM

in presence of Mg2+

in presence of Mg2+

can partially replace Mg2+ at 1 mM. At 5 mM inhibition of NAD+ formation

above 2.0 mM

above 2.0 mM

10 mM: 50% inhibition

activation at 0.2-1.0 mM, inhibition at higher concentration

1 mM, about 50% loss of activity

1 mM

1 mM reduces ATPase activity 50% in the presence of 5 mM MgSO4

in presence of Mg2+

at room temperature

Metals and Ions (53534 results)

activates

required

maximally active at 20 mM

639110

1.1.1.119

besides KCl/NaCl, the activity also depends on presence of bivalent cations. Mn2+ is less effective than Mg2+ and more effective than Ni2+

inhibition

15% activation at 5 mM only in D-mannitol oxidation

required

activates

2fold activation at 5 mM, no activation of ethanol oxidation

39% activation at 2 mM

286154

1.1.1.2

1 mM, less than 15% increase of activity

about 20% of the activity with Zn2+

740738

1.1.1.264

slight activation at 1 mM

required. Pure APDH contains 4.05 ions of Mn2+

667463

1.1.1.304

activates by 201.6 to 265.6% at 2 mM

activates

20 mM, maximal activation of enzyme inactivated by dialysis against Mg2+-free 20 mM-triethanolamine/HCl buffer, pH 7.0

639110

1.1.1.37

24% activation at 5 mM

740198

1.1.1.375

in the presence of NADPH, 10 mM MgCl2, MnCl2 or CaCl2 is required to support full activity. When using NADH as coenzyme enzymatic activity is insensitive to salt concentration

1 mM required for optimal activity

activity increases slightly with 7.5 mM MnCl2

286822

1.1.1.431

Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%

activates

most favorable metal ion for enzymatic activity

weak stimulation

1 mM, increases the activity to 127%

389572

1.1.1.71

moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol

761529

1.1.1.73

185% activity at 1 mM

Mn2+ or Co2+ required

1 mM, activity enhanced to 128%

required

enhances diacetyl and (3S/3R)-acetoin reduction

activates

21% activation at 1 mM, and 61% inhibition at 10 mM

5 mM, 113% of initial activity

required

5 mM and 10 mM, enzymatic activity of wild-type enzyme is above 100%

activates

can replace Ca2+ in reactivation after thermal inactivation

activates

104.2% activity at 2 mM

no activity

or Ca2+, Sr2+, or Cd2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH

contains Mn2+

activates

inhibitory

221% relative activity

22% of the activity with Fe2+

stimulates

activates

sulfate, similar binding as Fe2+ in wild-type enzyme

the Ni2+ bound protein catalyzes the reaction of EC 1.13.11.53

741923

1.13.11.77

the enzyme contains 25 mmol Mn2+ per mol of protein

723962

1.13.11.78

partial activation compared to Fe2+

manganese 9S-lipoxygenase, 9S-LOX contains catalytic manganese, Mn:protein ratio is about 0.2:1, while the Mn:Fe ratio is 1:0.05

725658

1.13.12.18

increases the flash height and the total light emitted by dinoflagellate luciferase

710987

1.13.12.7

influences the interaction with triazine dyes

484834, 484853, 484855

1.14.11.17

isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD

765089