Ligand nickel(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, 87.5% inhibition

2 mM abolishes enzyme activity completely

inhibits the light emission by dinoflagellate luciferase

0.5 mM, strong

IC50: 0.00071 mM, in the presence of Fe2+; IC50: 0.032 mM

671717

1.14.11.2

competitive versus Fe2+

695593

1.14.11.26

inhibition in decreasing order, Zn2+, Co2+, Ni2+

440380

1.14.11.28

more than 50% inhibition at 1 mM

664403

1.14.11.3

95% inhibition at 0.25 mM

439174

1.14.11.49

20% residual activity at 1 mM

734171

1.14.11.52

atalytic activity is affected by Ni2+. A significant reduction of activity is observed when the protein is purified using Ni-NTA column. The activity can be restored by dialysis of the protein in a buffer solution containing 0.1 mM EDTA, followed by the addition of 0.2 mM of Fe2+ to the protein solution

735945

1.14.11.55

more than 50% decrease in activity

binding structure with truncated enzyme mutant

Ni2+ renders the enzyme inactive

767029

1.14.12.13

25% inhibition compared to the activity without any metal

439074

1.14.13.244

0.1 mM, 21% residual activity

slight effect, crude enzyme extract

4% residual activity at 1 mM

42% inhibition

ionic or uncomplexed Ni2+ (2 mM) is inhibitory to the enzyme

717545

1.14.14.20

0.1 mM inhibits by 79%, 1 mM completely inhibits; complete inhibition at 1 mM

severely inhibits enzyme activity

inhibition in decreasing order, Zn2+, Co2+, Ni2+

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

slight inhibition

1 mM, 30% inhibition

inhibitory

complete inhibition at 1 mM

30-40% inhibition at 1.0 mM

slight

12% inhibition in the presence of 1 mM

690567

1.2.1.41

100% inhibition at 0.1 mM

390308

1.2.1.44

25% residual activity at 2 mM

inhibits NahF activity by 60%; inhibits NahV activity by 70%

both isoforms

1 mM, 12 h, 4°C, 58% loss of activity

moderate inhibition

moderately inhibited by 1 mM

766031

1.3.1.44

only after preincubation with cation

10 mM, 60% inhibition of reductive amination

349573

1.4.1.12

2% residual activity at 0.5 mM

2% residual activity at 0.5 mM

742928

1.4.1.3

1 mM, moderate inhibition of isozymes 1-3

391622

1.4.3.1

93.3% 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

0.5 mM, 92% inhibition

391945

1.4.4.2

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

5 mM, 73% inhibition

0.13 mM, complete inhibition

76% residual activity at 2 mM

392382

1.5.3.25

20 mM, 26% residual activity

strong inhibition at 1 mM

0.1 mM, 73% inhibition

722881

1.6.3.4

1 mM, 72% residual activity

764864

1.7.1.1

up to 0.1 mM, not inhibitory, 1 mM, 20% residual activity

654190

1.7.1.16

46.7% residual activity at 10 mM

50% inhibition at 0.1 mM

1 mM, 32% inhibition

stronger inhibition at pH 7.0 than at pH 3.0

slight

1 mM, 64.7% residual activity

764372

2.1.1.1

exposure of BEAS-2B cells to induces NNMT repression at both the protein and mRNA levels

5 mM, 18% inhibition

inhibits TNMT activity by 72%, can be prevented by the inclusion of EDTA; inhibits activity by 72%, inhibition prevented by inclusion of 10 mM EDTA

5 mM

1 mM, complete inhibition

5 mM, complete inhibition

strong inhibition

strong inhibition, Dnmt3a; strong inhibition, Dnmt3b

659080

2.1.1.395

83% inhibition at 5 mM

714532

2.1.1.396

83% inhibition at 5 mM

714532

2.1.1.402

84% inhibition at 2 mM

71% inhibition by 5 mM

676733

2.1.1.56

about 25 % residual activity at 5 mM

758535

2.1.1.63

purified protein is not very sensitive to this metal but the loss of AGT could contribute to the well-known carcinogenicity of nickel

5 mM, 83% inhibition

2 mM, 28% residual activity

strong inhibition

1 mM, 68% inhibition

5 mM, strong

10 mM, 21% inhibition; 21% inhibition at 10 mM

inhibits CEFT-4

15% of maximal activity

strongly inhibits the sterol glucosyltransferase activity, IC50 (mM): 1.2

strong inhibition at 1 mM and 10 mM

about 30% inhibition of synthetic activity

over 90% inhibition

about 38% residual activity at 10 mM; about 5% residual activity at 10 mM

736240

2.4.1.22

inhibits the transfructosylation activity but not the hydrolysis activity of the enzyme

2 mM

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

723506

2.4.1.279

1 mM, 95.4% inhibition

721375

2.4.1.285

about 80% residual activity in the presence of 2 mM

less than 10% residual activity at 10 mM

1 mM, 88% inhibition

inhibits Mn2+-activated enzyme

destabilization, 30.2% activity at 1 mM

638271

2.4.1.88

in the presence of Mn2+

a concentration of 10 mM is deleterious for enzyme activity

99% inhibition at 10 mM

671831

2.4.2.42

20 mM, 90% loss of activity

10 mM

10 mM NiCl2, 75% inhibition

strong

complete inhibition at 5 mM

35% activity at 1 mM

5 mM, 50-80% inhibition

687716

2.5.1.39

3.15% of activity remaining at 10 mM

weak

1 mM, 24% decrease of activity

671716

2.5.1.6

about 1% residual activity at 10 mM

about 30% loss of activity

760121

2.5.1.65

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

AST II

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

637035

2.6.1.49

inhibition of ADT and GDT, not PDT

reduced activity

competitive versus ATP via replacement of Mg2+, noncompetitive versus D-glucose via a cysteine residue proximal to the D-glucose binding site, enzyme-nickel interactions with positive cooperativity via histidine residues, no saturation is reached, nickel binding induces conformational changes in the secondary structure of the enzyme modifying the monomer/dimer equilibrium and decreasing the activity, overview

1.6 mM, 43% inhibition; 1.6 mM, 60% inhibition

680522

2.7.1.165

68% activity in the presence of 10 mM Ni2+ compared to Mg2+

the enzyme remains nearly inactive (less than 5%) with Ni2+

760894

2.7.1.23

ATP-dependent activity is reduced to 60% or 7% in the presence of 5 or 20 mM Ni2+

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

5 mM

53% residual activity at 3 mM

inhibits in combination with MgCl2, stimulates without MgCl2

642006

2.7.1.82

inhibits activating effect of Mg2+

641350

2.7.1.90

642074, 642089, 642100

2.7.11.11

inhibits sperm protein phosphorylation by the enzyme

high inhibition at 1 mM

complete inhibition at 10 mM

2 mM

20 mM in presence of 10 mM Mg2+, more than 90% inhibition

inhibits uridylyl removing activity

643540

2.7.7.65

6.5% inhibitin at 10 mM

moderate inhibition

2 mM, 75% inhibition

more than 70% inhibition at 0.1 mM

645536

2.8.1.4

inhibits the synthesis of s4U

643806

2.8.1.5

slight inhibition at 1 mM

30% inhibition at 1 mM

strong inhibition

sensitive to metal ions, almost complete inhibition at 6.0 mM

55.4% residual activity at 1 mM

57% inhibition at 2 mM

64-87% inhibition

1 mM, 15.1% of initial activity; 1 mM, 44.5% of initial activity; 1 mM, 63% of initial activity

AChEA and AChEB are completely inhibited by 1 mM of Ni2+

750356

3.1.1.70

1.0 mM, 67% relative residual activity

10 mM, 28% inhibition

678879

3.1.1.79

10 mM, 50% loss of activity

0.5 mM, strong inhibition

effective competitive inhibitor

complete inhibition at 1 mM

679610

3.1.21.B1

1 mM, 50% residual activity

1 mM

about 40% residual activity

competitive towards Mg2+

slight inhibition

in absence of free Zn2+ in solution

135299

3.1.4.4

2.5 mM, complete loss of both hydrolytic activity and transphosphatidylation

678805

3.1.4.46

5 mM, complete loss of activity

24% inhibition at 1 mM

weak inhibition

1 mM, 59% loss of activity

2 mM, 47% of initial activtiy

737518

3.2.1.145

64.7% residual activity at 50 mM

slight inhibition at 1-5 mM

70.4% residual activity at 1 mM

10 mM, 36% loss of activity

1 mM, inhibition to 58.8% of control

1 mM, 19% inhibition

17% inhibition at 2 mM

1 mM, 25% of initial activity

47% inhibition at 50 mM for beta-D-.fucosidase I, 25% inhibition at 50 mM for beta-D-fucosidase II

complete inhibition at 5 mM

5 mM, strong inhibition

F1 form 62%, F2 form 67% inhibition

136729

3.2.1.62

about 5% residual activity at 1 mM

732073

3.2.1.63

1.0fold decrease of activity at 10 mM

54.7% residual activity at 1 mM

70.55% residual activity at 5 mM

752111

3.2.1.98

1 mM, 59.7% loss of activity

1% residual activity at 10 mM

732434

3.2.1.B44

10 mM, about 35% loss of activity

749672

3.2.1.B50

slight inhibition at 5 mM

0.001 mM

complete inhibition at 5 mM

30% inhibition at 1 mM

92.5% inhibition at 1 mM

1 mM, 90% inhibition

25% inhibition at 1 mM

89% inhibition at 1 mM

15.52% residual activity at 0.2 mM, complete inhibition at 1 mM

35902, 35908, 35912

0.5 mM

3.3 mM, no residual activity

partial

at 0.01 mM 44.6% activity relative to control

684959

3.4.17.B4

0.2 mM, about 75% loss of activity, the inhibitory effect is not overcome by the presence of Co2+

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

50% inhibition at 0.011 mM

0.06 mM, 30% inhibition

17% inhibition

inhibition of amidolytic activity

order of decreasing inhibitory effect: Cu2+, Hg2+, Zn2+, Ni2+, Co2+

649673

3.4.22.1

26.7% residual activity at 1 mM

residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain

strong inhibition

inhibits 85% at 0.2 mM and precipitates the enzyme at 1 mM

730765

3.4.22.B8

inhibitory below 5 mM

weak

introduction of Ni2+ into milk inhibits the coagulation ability of moose chymosin

39% inhibition at 1 mM, 87% at 5 mM

2 mM, more than 70% inhibition

768748

3.4.24.40

at pH 10, not at pH 7

1 mM

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

719761

3.4.24.B10

low concentrations of Ni2+ inhibit ADAM12-S drastically

678344

3.4.24.B2

41% inhibition at 1 mM

734466

3.4.24.B26

inhibits the caseinolytic and elastinolytic activities

695765

3.4.26.1

52% residual activity at 0.087 mM

649971

3.4.99.B1

0.087 mM, 48% inhibition

slight

partial inhibition at 0.050 mM

33% inhibition at 1 mM

85% inhibition at 10 mM

1 mM: 66.8% inhibition

172070

3.5.1.69

promotes the hydrolytic activity but inhibits the synthetic activity of the enzyme

1 mM: 60% inhibition

2 mM, 80% inhibition

1 mM, plus 0.1 mM Mn2+ complete inhibition

at pH 6.5

48% residual activity at 1 mM

734047

3.5.4.28

5 mM, inhibition to 30.25% of control

weak

2 mM, complete inhibition

736354

3.5.99.2

0.01 mM 73% inhibition

complete inhibition at 1 mM

0.1 mM

rapid decreases in relative enzyme activity at 2 mM. The enzyme activity is completely lost at 16 mM

778524

3.8.1.5

1-5 mM, complete inhibition

5 mM

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

weak

slight

2 mM inhibitor in presence of 1 mM Mn2+, 40% inhibition

664936

4.1.1.12

10 mM, over 90% inhibition

677736

4.1.1.22

0.1 mM, 15% decrease of activity

4145

4.1.1.25

1 mM, 64.3% residual activity

1 mM, complete loss of activity

weak

cells stressed by 8 microM Ni(II) for 20 min lose 75% of their FbaA activity. In presence of 8 microM Ni(II), purified FbaA loses 80% of its activity within 2 min. Inhibition is due to Ni(II) binding to a secondary zinc binding site

64% inhibition at 1 mM

about 80% inhibition

about 10% residual activity in the presence of Ni2+

687737

4.1.3.24

6% specific activity at 10 mM

704322

4.1.3.43

2.6% activity at 0.1 mM and 17.5% activity at 1 mM chloride salt

721615

4.1.99.2

complete inhibition at 1 mM

95.0% inhibition at 1 mM

inhibits slightly

0.5 mM, 8% inhibition

90% inhibition

0.1 mM, 83% inhibition

5 mM

10 mM, 40-100% inhibition

about 80% residual activity at 1 mM

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

2 mM, 98% inhibition

strong

61.1% residual activity at 10 mM

0.1 mM, weak

648732, 648733, 648734

4.4.1.16

648741, 648743

4.4.1.21

1 mM, 23% of initial activity, respectively; 1 mM, 7.8% of initial activity, respectively

749224

4.4.1.29

5 mM, complete inhibition

674771

4.4.1.31

5 mM, complete inhibition

severe inhibition of wild-type PI-PLC

substrate inhibition occurs when assayed in the absence of metal ion-complexing buffer components

715572

5.1.1.1

10 mM, about 95% inhibition

775413

4BF5, 3D-view

5.1.1.10

slight inhibition of both activities

almost complete inhibition at 0.1 mM

748592

5.1.3.B12

almost complete inhibition at 1 mM

slight inhibition

1 mM, 14% residual activity

0.2 mM Ni2+ in presence of 0.5 mM Mn2+, 29% inhibition

1 mM, 15% inhibition; 1 mM, 22% loss of activity

60-70% relative activity in the presence of 0.1 mM Ni2+ compared to Mg2+

691386

5.5.1.25

about 55% residual activity at 1 mM

the authors favor a mechanism in which methylation occurs first to Ni(p0 -) or Ni(pI -)[Fe4S4]+, followed by coordination of CO to form Ni(pII)(CO)(CH3) which breaks one of the S(Nid) bonds (forming the bis square planar Ni(II) species, as if the Ni(d)N2S2 unit were acting as a biological pseudodiphosphine, mimicking behavior common to a bidentate phosphine). The CO-insertion/CH3-migration occurs on one metal forming the trigonal planar Ni(pII)-acetyl intermediate. Finally, addition of thiolate produces the thioester. The authors disfavor the unprecedented bimetallic, CO-insertion/CH3-migration mechanism (both in its diamagnetic and paramagnetic guise) and disfavors CO, CH3+, or thiolate (CoA) binding to the distal Ni. Finally, Ni in the proximal site produces a better catalyst than does Cu

661935

6.2.1.11

589, 592

6.2.1.13

about 3% residual activity at 20 mM

744820

6.2.1.3

isoform Facl1 shows 1.3% residual activity and isoform Facl2 shows no activity at 1 mM

1000, 996

complete inactivation

complete inhibition

in the presence of NiCl2 no gamma-F420-2 is formed

1 mM, 80% inhibition

in presence of dithiothreitol inhibition at concentrations below 0.2 mM

649002

6.4.1.8

1 mM: 50% inhibition of ATPase activity. 2.5 mM: 50% inhibition of carboxylation activity

708932

6.5.1.1

5 mM, abolishes ligation reaction in presence of 5 mM Mg2+

662041

6.5.1.6

1 mM, about 70% loss of activity

672745

6.6.1.2

50% inhibition at 0.003 mM

653078

7.1.1.2

1 mM, potent inhibitor

674694

7.1.2.2

1 mM reduces ATPase activity 47% in the presence of 5 mM MgSO4

1 mM, 28% inhibition

Metals and Ions (6862 results)

0.1 mM reactivates EDTA-100% inhibited enzyme by 30%

698673

1.1.1.119

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

inhibition

located near active site, crystallization data. The activity with 1,3-propanediol is highly dependent on the presence of Ni2+

721395

1.1.1.214

1 mM, 88.5% residual activity

strong inhibition

activates less than Zn2+

activates at 1 mM

activates by 35% at 1 mM

721879

1.1.1.332

5 mM, addition to EDTA-treated enzyme, 73% of control activity

720397

1.1.1.38

requirement for divalent cation

286697

1.1.1.39

divalent metal ion required, NADP+-linked activity exhibits a maximum at 5 mM Ni2+

25% activation at 1 mM

about 110% activity at 5 mM (isoform G6PD2), about 115% activity at 2 mM (isoform G6PD1)

741369

1.1.1.56

about 108% activity at 1 mM

738926

1.1.1.67

about 230% activity at 1 mM

740876

1.1.1.71

required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol

761529

1.1.3.10

5 mM, 119% of initial activity

activates

113.5% activity at 2 mM

no activity

activates

below 0.01 mM, activation, inhibition above

activates

contains 1.0 mol of nickel ions per mol of enzyme

contains 0.9 atoms nickel per mol enzyme

contains less than 0.1 mol Ni per mol of enzyme

1 mmol/l, 30°C, 15 min, 74.6% remaining activity

activates

activates by 7% at 5 mM

744574

1.13.11.78

partial activation compared to Fe2+

activates

restored the activity after an incubation with EDTA to 52%

778660

1.13.12.7

influences the interaction with triazine dyes

484855

1.14.11.4

can substitute for Fe2+

required

protein B contains 0.04 mol Ni2+ per mol protein

increase of activity

nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+

717545

1.14.14.173

slight activation at 0.1 mM

62% of the activity with Mg2+

5 mM chloride salt, 183.9% activity compared to untreated control

719179

1.2.1.79

2 to 3-fold activation at saturating concentration

contains nickel

1 mM, 12.3% increase in activity

762858

1.3.1.32

35.25% activity compared to no addition 100%

719179

1.4.1.27

0.1 mM, 84% inhibition of the exchange of glycine carboxyl carbon with CO, catalyzed by glycine decarboxylase (P-protein) and aminomethyl carrier protein (H-protein)

slight stimulation

treatment of root with Ni2+ results in significant increase in level of membrane lipid peroxidation, content of H2O2, the production rate of superoxide radicals and the activity of the PM NADPH oxidase. Effects of Ni2+ are inhibitied by treratment with enzyme inhibitors diphenylene idonium, imidazole and pyridine

676665

1.7.1.1

a significant improvement of activity is achieved after cyanide treatment by addition of 5 mM NiCl2 which increases the enzyme recovery in leaf extract up to 63%

673360

1.7.1.13

0.01 mM, 77% residual activity

0.76 atoms per mol

the enzyme contains approximately 0.6 mol nickel

655398

2.1.1.151

absolute requirement for the presence of a metal ion within the tetrapyrrole substrate

644434

2.1.1.228

can substitute Mg2+ to lesser extent

756631

2.1.1.336

the highest rate of reaction for the formation of isovanillin from 3,4-dihydroxybenzylaldehyde is observed in the presence of Ni2+

778066

2.1.1.373

contains up to 0.5 Ni2+ per protein

778512

2.1.1.6

can substitute for Mg2+

stimulation

absolute requirement for a divalent metal ion. 1 mM Ni2+ stimulates 24fold

485507

2.1.1.90

metal-free enzyme preparation has no activity, addition of Ni2+ restores 21% of the original activity

485660

2.1.1.B173

Ni2+, and Co2+ also recover methylation activity by approximately 20-60% compared to that with Mg2+

required, less efficient

the enzyme requires a divalent metal ion for activity. It exhibits a preference for Ni2+ followed by Mn2+ and very poor activity with Mg2+

749881

2.3.1.30

0.1 mM, 12fold activation

659095

2.3.1.43

stimulates phospholipase reaction and cholesterol esterification, EDTA suppresses stimulation

activation

activates nearly equivalent to Mn2+

activation

109% activity at 5 mM

very slightly activation

activation, can replace Mn2+ with 16% efficiency

activates, best at 1.5 mM

657584

2.4.1.218

required, metalloenzyme

some activity

57% of the activity with Mg2+

5 mM, highest stimulation of activity in the presence of Mn2+. Ca2+, Pb2+, Ni2+ and Mg2+ are also effective

addition of cation stimulates, efficiency in descending order: Mn2+, Co2+, Mg2+, Fe2+, Ca2+, Ni2+, K+, Na+

489227

2.4.1.48

20 mM, required, 4% of activity compared to Mn2+

stimulates

activates, soluble enzyme

activation

slight activation

activates

may substitute for iron

745168

2.4.2.6

significantly stimulates the LhNDT activity up to 138% at 10 mM

activates

10% of Mg2+ activation at 0.5 mM, inhibition above

1.5fold activation

154.7% activity at 5 mM

the enzyme requires Mg2+ and is inactive in the absence of metal. Optimal concentration of Mg2+ is 0.1 mM. Co2+ and Mn2+ activate the synthesis of farnesyl diphosphat at lower concentrations (0.005-0.05 mM) than does Mg2+ (0.05-0.5 mM). The enzyme also utilizes Ca2+, Ni2+, and Zn2+ as cofactors, but only at low concentrations (0.001-0.05 mM)

758863

2.5.1.39

partly effective for activity

0.02 mM stimulates activity

685392

2.5.1.71

5% of the activity with Mg2+

676566

2.5.1.97

pseudaminic acid synthase requires the presence of a divalent metal ion for catalysis. Addition of 10 mM Mg2+ results in 26% of the activity obtained with 10 mM Co2+

stimulates

requirement, can be replaced by Mg2+, Mn2+, Ca2+, Zn2+, Co2+, Cd2+

slight activation

slight activation

15% of the activation with Mg2+, at 1.3 mM

activity rate 11% compared to Mg2+

1 mM, 4% relative activity compared to Mg2+

broadly accepts Ca2+, Fe2+, Co2+, Mn2+, Zn2+, or Ni2+ in place of Mg2+

722842

2.7.1.17

activation, half as effective as Mg2+

activates

can partially substitute for Mg2+

641136

2.7.1.23

6% activity at 5 mM compared to Mg2+

no stimulatory effect

641329

2.7.1.33

activation, can replace Mg2+ with about 50% efficiency

divalent cation required, at 1 mM Ni2+ activation results in 2% of the activity with Mg2+

less effective

40% of the activity with Mg2+

641894

2.7.1.71

divalent cation required, Mg2+ and Mn2+ are most effective, Ca2+ activates to a lesser extent

can restore activity of the metal-free apoenzyme to a minor extent

5 mM, 60% as effective as Mg2+ in activation

642127

2.7.1.B19

5 mM, activates. No activity in absence of cations

activates

required for the phosphorylation of CMP, IUMP and dCMP by either ATP or dCTP. With CMP as phosphate acceptor and ATP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+ but are less effective. The relative rates are Mg2+ (100%), Mn2+ (42%), Ni2+ (16%), and Ca2+ (13%)

645139

2.7.4.2

4.7% of activity with Mg2+

645180

2.7.4.6

requirement, in decreasing order of activity: Mn2+, Mg2+, Co2+, Zn2+, Ni2+, Ca2+, Fe2+

activation

84% activity at 7.5 mM

absolute requirement for bivalent cations, at pH 10.0 Mg2+ is most effective, while Mn2+, Co2+ and Zn2+ show little activity. At pH 7.0, Co2+ is most effective and Mg2+, Mn2+, Ni2+ and Fe2+ show little activity

activates slightly

Ni2+ yields approximately 9% of the activity seen with Mg2+, the cation preference of CCT1 is Mg2+ > Mn2+/Co2+ > Ca2+/Ni2+ > Zn2+

690911

2.7.7.2

weak stimulation of activity

activates slightly

activates slightly

activates

1 mM, 8fold activation

can partially replace Mg2+ in activation

1 mM of this ion promotes pyruvate formation

645419

2.7.9.2

requires divalent cations in the forward reaction, 15% of the activity with Mg2+

645478

2.8.2.15

markedly activated by 5 mM divalent cations

331.8% activity at 1 mM

729080

3.1.1.2

catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)

the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)

730097

3.1.1.3

172.5% activity at 2 mM

110.32% activity at 0.5 mM

752327

3.1.1.68

21% activity compared to Mg2+

5 mM, 1.4fold activation

680323

3.1.1.74

activates isozyme Tfu 0882 5% and isozyme Tfu 0883 7% at 1 mM

slight activation of ssDNA nuclease activity of RecB30

activates

minimally stimulates activity

681823

3.1.2.32

1.9fold stimulation of EDTA-treated protein

737671

3.1.2.6

no activity of glxII, re-addition of Zn2+ results in a further inhibition of the residual enzyme activity of the incompletely demetalled apo-GlxII

can replace Mn2+ but yields a much lower activity than Mg2+, highest activity at 0.1 mM, inhibitory at high concentrations

679610

3.1.21.7

supports oxanosine-containing DNA cleavage to a small extent

666476

3.1.21.8

compared to Mg2+, relative nicking activity is 0.1 with top strand, 0.1 with bottom strand

727747

3.1.21.B3

or Mn2+, Co2+, absolutely required

770689

3.1.26.12

RNase E requires a divalent metal ion for its activity. Mg2+ is the physiological divalent metal ion supporting activity of RNase E in vivo. Ni2+ and Zn2+ permits low levels of activity in vitro

similar levels of activity are detected in the presence of 1 mM Mg2+, Mn2+, Co2+

766513

3.1.3.12

activates about 1.4fold

cations tested, in decreasing order of efficiency: Mn2+, Co2+, Mg2+, Ni2+

for Ni2+, the catalytic efficiency is approximately half of that for Mg2+

partial activation

can substitute for Mg2+ in activation

can substitute for Mg2+ in activation

81085

3.1.3.36

activates, competitive binding to other metal ions, KM 0.0064 mM and turnover number 5.48 s-1 at pH 7.0, 30°C, recombinant enzyme

activates, competitive binding to other metal ions, KM 0.0064 mM and turnover number 5.48 s-1 at pH 7.0, 30°C, recombinant enzyme

activates

KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP

656266

3.1.3.68

can replace Mg2+ in activation, with 35% of the efficiency

25144

3.1.3.7

activates, best at 0.5 mM

772242

3.1.3.70

activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme

657584

3.1.3.71

can fully substitute for Mg2+

at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+

activates slightly at 0.05 mM

restore activity if EDTA or EGTA used

95148

3.1.4.3

1 mM, activation to 123.6% of control

0.75 mM Mn2+ shows a 1.5fold activation of hydrolysis of bis(4-nitrophenyl) phosphate

718857

3.1.4.59

about 55% of the activity with Mn2+

751027

3.1.4.61

can replace Co2+ to 71%

760445

3.1.6.1

1 mM, stimulates ArySMA1 activity

activation

alpha-mannosidase III, little activation

1 M, 119% of initial activity

1 mM NiCl2, activates

208558

3.2.1.151

slight activation at 5 mM

752566

3.2.1.157

128% activation at 1 mM

731522

3LMW, 3D-view

3.2.1.158

10 mM, slightly promotes the enzymatic activity

773891

3.2.1.168

reduces the activity in the range of 10-50%

about 193% activity at 1 mM

769883

3.2.1.196

about 118% activity at 5 mM

0.1 mM, enhances activity to 119% of control

646644

3.2.1.28

122% activity at 20 mM

731011

3.2.1.3

11% activation at 1 mM

664653

3.2.1.36

has positive effect on the activity

strong inhibition

inhibitory at 1 mM

activates

1.5fold activity in the presence of 10 mM NiSO4

116.2% activity at 5 mM

751309

3.2.1.75

1 mM, enhances activity

10 mM, slightly promotes the enzymatic activity

773891

3.2.1.89

about 145% activity at 5 mM

activates at 5 mM

stimulates activity

inhibitory above 0.05 mM, but to lesser extent than Cd2+ or Zn2+. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate

30% inhibition at 1 mM

81194, 81195, 81196, 81197

3.4.11.15

can partly replace Co2+

dinuclear metal-enzyme derivative, structure

664582

3.4.11.3

stimulation, reverses EDTA inhibition

enhances activity

activates

about 75% of the activation with Co2+

activates

may substitue for Zn2+

can partially replace cobalt

81313

3.4.19.12

0.5 mol per mol of protein, native isozyme ISOT-S

slight activation

trypsin N143H/E151H hydrolyzes the peptide AGPYAHSS exclusively in presence of Ni2+ or Zn2+ with high levels of catalytic efficiency

95451

1SLW, 3D-view

3.4.21.47

promotes a stable C3bB complex

activates 12% at 1 mM

activates

at 2 mM 12% less active than Ca2+

0.2 mM, 84% inhibition of protease activity

730765

3.4.23.18

slight activation at 10 mM

inhibits activity at 10 mM

664291

3.4.24.68

zinc-dependent endoproteinase, can replace zinc

stimulates at 1 mM

1 mM Ni2+ enhances the extent of substrate cleavage by about 15%

activates

functional association

activates

incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+)

696193

3.5.1.114

Co2+ and to a lesser extent Ni2+ increases activity several times in comparison with intact wild type AA3. Co2+ drastically increases the rate of deacetylation of N-acetyl-1,2-dichlorovinyl-L-cysteine and significantly increased the toxicity of Ac-DCVC in the HEK293T cells expressing wt-AA3. Aminoacylase 3 is a metalloenzyme significantly activated by Co2+ and Ni2+

711284

3.5.1.136

the Kd values of Zn2+, Cd2+ and Ni2+ binding are similar

required

enhances activity

129.81% activity at 1 mM

slightly activating

required, highly activating, Ni2+ occupies the same position as Mn2+, inducing changes near the metal ion. Binding structure analysis and comparison with Mn2+, overview

772561

3.5.1.38

slightly enhanced activity

209094