Ligand MnCl2

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Basic Ligand Information

Molecular Structure

H₂Cl₂Mn

MnCl2

GLFNIEUTAYBVOC-UHFFFAOYSA-L

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Synonyms:

manganese chloride

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Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (12 results)

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slightly activating

at 5 mM, 250% activity, oxidative deamination

391661

3.1.3.16

14 mM, 30°C, pH 7.5, relative activity 361% with glycogen synthase D as substrate and 280% with histone as substrate compared to no addition

655958

3.4.11.7

181% residual activity at a concentration of 1 mM

684091

3.4.13.9

stimulation of activity against substrates L-Pro-Gly, L-Pro-L-Glu, L-Pro-L-Leu, L-Pro-L-Ser, and L-Pro-L-Phe, inhibitory to hydrolysis of substrates L-Pro-L-Ala, L-Pro-L-Val, L-Pro-L-Met, and L-Pro-L-Asp

664626

3.6.1.5

stimulation in intact parasite, may substitute for MgCl2

1 mM, 1.4fold activation

708453

4.2.2.3

695268

Inhibitor in Enzyme-catalyzed Reactions (164 results)

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1.1.1.1

24% inhibition at 1 mM

1 mM, 50% inhibition

1 mM, 28.6% inhibition

668012

1.1.1.376

10 mM, 45% inhibition

10 mM, 48% inhibition

1 mM, 30 min at 4°C, 35% inhibition

656321

1.1.3.7

14% inhibition at 0.5 mM

1 mM causes 100% inhibition

389887

1.1.99.27

1 mM, 86.2% inhibition

10899

1.1.99.6

1 mM, complete loss of activity

1 mM, 70°C, 34.5% activity

663712

1.13.11.74

53% residual activity at 0.5 mM

722603

1.13.12.19

1 mM, 6% residual activity

715784

1.14.14.156

1 mM MnCl2 added to the CYP79B2 reconstitution assay inhibits the activity by 34%; 34% inhibition at 1 mM

715448

1.14.14.21

66% inhibition at 1 mM

735526

1.14.14.91

1 mM, 27% loss of activity

1 mM, 6% residual activity

715784

1.14.99.29

64% of initial activity at 0.005 mM

1 mM, slightly inhibited,less than 24%

720756

1.5.1.34

0.1 mM, complete inactivation

484963

1.5.1.8

1 mM, 52% loss of activity

392361

1.6.3.3

10 mM, slightly increases activity

0.1 M: 98% inhibition, 0.01 M: 65% inhibition

209729

2.3.1.1

0.1 mM, 30-50% inhibition

1 mM, 9% inhibition

1 mM, 28% inhibition

1 mM, 7% inhibition

10 mM, 29% inhibition

5 mM, 30% inhibition

weak

91% inhibition

20 mM decreases activity

727047

2.3.3.16

56% inhibition at 10 mM

stimulates at 1 mM, inhibits at higher concentration

7 mM, 30% inhibition

1 mM, 34% loss of activity

725294

2.4.1.234

1 mM: 62% inhibition, 10 mM: 43% inhibition

489559

2.4.1.33

at 0.25 mM: 15% increase of activity, above 0.75 mM: 80% inhibition

489052

2.4.1.5

54.05% inhibition of transferase activity at 100 mM; 59.46% inhibition of transferase activity at 100 mM; 64.29% inhibition of transferase activity at 100 mM

1 mM: inhibition to 87% of control, tagged enzyme, inhibition to 60% of control, untagged enzyme. 10 mM: inhibition to 87% of control tagged enzyme, inhibition to 56% of control, untagged enzyme

779079

2.4.1.99

99% residual activity at 10 mM

701834

2.4.2.51

4% inhibition at 0.1 mM

720781

2.5.1.7

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

706916

2.6.1.70

retains 65% activity at 10 mM

640191

2.6.1.71

57% activity retained at 1 mM, 3% activity retained at 10 mM

in presence of 10 mM MgCl2

643562

2.8.2.17

75% inhibition at 5 mM

5 mM, 24% inhibition

1 mM, 6% loss of activity

no effect at a concentration of 3.3 mM

94343

3.1.1.78

50% inhibition at 0.25 mM

638950

3.1.1.79

50 mM, 45% inhibition

1 mM, 37% inhibition

10 mM, 50% of inhibition

above 200 mM

1 mM, 77.4% of initial activity

772615

3.1.3.16

14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 51% remaining activity

655958

3.1.3.2

10 mM, 65% inhibition

2.5 mM, 17% inhibition

2.5 mM, 17% inhibition

2 mM, 92% inhibition

inhibits activity by 30%

1 mM, 71% activity compared to control without any metal ion

671015

3.2.1.14

1 mM, 91.67% of initial activity

1 mM, 19% inhibition

2 mM, 43% loss of activity

1 mM, 27% inhibition

0.001, 24% loss of activity

749735

3.2.1.212

0.001, 24% loss of activity

749735

3.2.1.22

1.0 mM, 18.4% inhibition

655765

3.2.1.28

over 90% inhibition at 10 mM

704913

3.2.1.31

2 mM, 31.9% inhibition

1 mM, 5.1% loss of activity; 1 mM, 6.8% loss of activity

768832

3.2.1.52

1 mM, complete inhibition

654313

3.2.1.54

10 mM, 33% inhibition

664779

3.2.1.58

136670, 136672, 136681

3.2.1.68

5 mM, 80% residual activity

654414

3.2.1.73

5 mM, 63.12% relative activity

775562

3.2.1.8

1 mM, 29% inhibition of xylanase 2, 20% inhibition of xylanase 1

738127

3.2.1.82

at 1 mM causes 57% inhibition of PGI, at 5 mM causes complete inhibition of PGI

G-6, slight inactivation

IFO 3134, completely

1 mM, 14% inhibition

0.1 M, 4% activity

1 mM, incubation at 30°C for 10 min, complete inhibition

664820

3.5.1.2

22% inhibition at 1 mM, 13% at 0.1 mM

relative activity 94.4%, incubated for 10 min

209116

3.5.1.73

10 mM, 24% loss of activity

5 mM, 50% inhibition

2 mM, 20% inhibition

slight inhibition

excess ogf MnCl2 over ATP is inhibitory

0.5 mM

slight

22% inhibition at 5 mM; 5 mM, 22% inhibition

1 mM, 60% residual activity

766331

5.1.1.2

1 mM, 60% residual activity; 1 mM, 60% residual activity

0.001 mM, 45% inhibition

648883

Metals and Ions (108 results)

activation

1 mM, stimulates

10 mM, increase of activity by 100%

655092

1.1.3.21

10 mM, 7.6 fold activation

287564

1.1.3.6

1 mM, 30 min at 4°C, 35% inhibition

656316

1.10.3.2

1 mM, increases activity by 11.7%

741648

1.14.13.161

upon treatment of sage suspension cultures with 30 mM MnCI2, camphor-6-hydroxylase activity is induced up to 7fold

718227

1.2.1.5

2 mM, 2.1fold stimulation of activity of ALDH1

348783

1.5.1.30

with 1 mM 97.0% activity

stimulates

addition of MnCl2 up to 1 mM results in a two-fold stimulation of activity but greater concentrations result in decreased activity

776509

2.4.1.10

22% activation of the immobilized enzyme at 0.1 mM, 30% activation at 0.1 mM of the free enzyme

702972

2.4.1.122

20 mM are included in assay medium

703884, 703895

2.4.1.123

5 mM are included in assay medium

706379

2.4.1.126

0.006-0.01 mM: stimulation of about 10%

slight stimulation

stimulation

glycosyltransferase assay with 20 mM MnCl2

673753, 659454

2.4.1.155

up to 3fold stimulation

658721

2.4.1.195

activity is stimulated by thiol reducing agents

644892

2.4.1.33

no essential requirement, at 0.25 mM: 15% increase of activity, inhibition above 0.75 mM

no activity in absence of divalent cations, 20% of the activation with MgCl2

489211

2.4.1.53

absolute requirement for the addition of a divalent cation, optimal concentration 0.01 M

489287

2.4.1.87

707367, 708604, 707599

2.4.3.1

702879

2.5.1.27

dependent on presence of divalent cation, addition of 2 mM MnCl2 is 1.3 times more effective than that of 10 mM MgCl2

671796

2.7.1.146

2 mM ADP and 2 mM D-fructose 6-phosphate, increase in enzyme activity with the increase in MnCl2 concentration from 2.5 to 7 mM is observed

698924

2.7.1.2

MnCl2 yields 40% of the activity observed when MgCl2 is included in the assay

in the presence of MnCl2 the saturation kinetics of recombinant purified UMP kinase are hyperbolic for UMP and sigmoidal for ATP

663945

2.7.7.7

sustitution of MgCl2 by MnCl2 produces a slight decrease of activity. Optimal activity is obtained in the presence of 0.4 mM MgCl2

747685

2.7.8.41

requires divalent cations for activity. Highest activities are measured in the presence of 20 mM MnCl2, while MgCl2 or CoCl2 stimulate the activity only slightly

727507

2.8.2.20

required, maximal activity at 20 mM

activates at 0.2 mM

1 mM, 86% compared to activity with 1 mM MgCl2

750559

3.1.1.3

28% activation at 1 mM

10 mM, stimulates

can substitute for MgCl2, less efficient

10 mM, activity is enhanced to 138% of control

can replace MnCl2, at 1 mM

652107

3.1.3.33

divalent metal required, 60% the rate observed with MgCl2

81080

3.1.3.5

10 mM, 170% of initial activity. 50 mM, 80% of initial activity

increases activity

1 mM, 71% activity compared to control without any metal ion

activates

1 mM, activates

1 mM, 1.6fold activation

748424

3.2.1.28

7.5 mM, 4.2fold activation

1 mM

slight activation

1 mM, weak activation

activation

stimulates at 5 mM

partially restores activity after EDTA treatment

activates

10 mM, activates

allows some peptidase and caseinase activity in the absence of any nucleotide, however Mn2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate

metal ion removal from the purified Sumo-ArgE decreases enzyme activity by nearly 90% in reactions without added CoCl2 in comparison with those containing 0.2 mM CoCl2. MnCl2 (0.2 mM) added to the reaction in place of CoCl2 restores activity to about 40 % of that seen with CoCl2

754657

3.5.1.62

1 mM: slight activation

172070

3.5.1.68

5 mM: most effective activation

activates

up to 40% of the activity with MgCl2

722230

3.6.1.5

5 mM, stimulation up to 10fold

655301

3.6.5.3

10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness

2.5 mM, 112% stimulation of activity

677849

4.1.2.13

the enzyme requires divalent cation for activity. The highest activity is obtained with MnCl2 (100%, 50 U/mg), which can be partially replaced by FeSO4 (40% residual activity)

activates

inhibits activity

the enzyme displays apurinic/apyrimidinic endonuclease activity both in the presence of MnCl2 or MgCl2

769001

6.4.1.1

7.5 mM, can partially replace MgCl2

649509

7.6.2.2

1 mM, increases the activity by 10%, respectively

711295

Enzyme Kinetic Parameters

References & Links

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Show Reference (285 entries)

Links to other databases for MnCl2

Ligand MnCl2

Basic Ligand Information

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (12 results)

Inhibitor in Enzyme-catalyzed Reactions (164 results)

Metals and Ions (108 results)

Enzyme Kinetic Parameters

References & Links

Literature References (285)

Links to other databases for MnCl2