Ligand Pb2+

lead inhibits in vitro the cytosolic and mitochondrial creatine kinase activity at 0.2 mM and that this inhibition is prevented by addition cysteamine to the assay at 0.1 mM and 0.5 mM final concentration

706831

2.7.7.9

complete inhibition

738481

2.8.2.1

recombinant enzyme form SULT1 ST5

35% inhibition at 2 mM

inhibits at 0.5-5 mM

13.9% residual activity at 1 mM

marked inhibition at 0.1 mM

208334

3.1.1.79

5 mM, 65% residual activity

750496

3.1.1.81

67% inhibition at 2 mM

665500

3.1.2.2

slightly inhibits the mitochondrial enzyme

80783

3.1.2.20

slightly inhibits the mitochondrial enzyme

1 mM

at 2.5 mM

severely inhibits activity

1 mM, 30-50% inhibition

about 2% residual activity at 5 mM

slight

1 mM, inhibition to 7% of control

1 mM, inhibition to 47.7% of control

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

10 mM, 30% residual activity

695797

3.2.1.51

effective inhibition at 5 mM

136688, 136691, 136694

3.2.1.60

Pb(OAc)2, recombinant and native enzyme

136735

3.2.1.62

about 10% residual activity at 1 mM

10 mM, 83.91% of initial activity

775437

3.2.1.70

208766, 208767, 208772

3.2.1.72

more than 90% inhibition

almost complete inhibition

complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase

some inhibition at 10 mM

3 mM, 79.4% of initial activity

5 mM, 68.5% of initial activity

85.5% inhibition at 10 mM

inhibits at 10 mM

69.27% residual activity at 100 mM

5.0 mM, complete inhibition

inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+

partial

1 mM: 5% inhibition

74% inhibition of isozyme I, 92% inhibition of isozyme II

656378

3.5.3.6

1 mM, 11% loss of activity

55.5% inhibition at 2 mM

slightly inhibits

0.2 mM

1-5 mM, strong inhibition

5 mM, inactivation

highly inhibitory at 20 mM

48% inhibition with 1 mM Pb2+

691118

4.1.3.27

33280, 33288, 33313

4.1.3.30

10 mM, in presence of 2.5 mM Mg2+, 14% inhibition. 11% activation, when added instead of Mg2+

11.9% inhibition at 1 mM

94.5% inhibition at 1 mM

complete inhibition at 10 mM

weak

enzyme form IM3796 is inhibited to about 60% residual activity by 5 mM Pb2+

772952

4.2.2.21

complete inhibition at 5 mM

1 mM, 82% inhibition

1 mM: 0% activity

0.1 mM, 75% inhibition

5 mM PbCl2, 88% loss of activity

6060

4.3.1.24

1 mM, 50% loss of activity

1 mM

up to 10 mM complete inhibibition

in deer mice exposed to Pb, or Pb together with Cu and Zn via drinking water for 4 weeks. GCL activities are not significantly affected by treatments. Metal-contaminated soils do not lead to significant effects in pups via lactation, 50-day exposure alters glutathione content marginally, while 100-day exposure results in marked GCL activity depletion. After 100-day exposure, GCL activities of the medium soil-, high soil- and Pb-treated deer mice are only 53%, 40% and 46% of the control, respectively

in presence of Mg2+

inhibitory effect of Pb2+ on the transport cycle of the Na+,K+-ATPase, overview. Pb2+ inhibits cycling of the enzyme, but it does not affect cytoplasmic Na+ binding and release of Na+ ions at the extracellular side at concentrations below 0.010 mM

711739

7.6.2.2

3 mM, 77% loss of activity

711295

Metals and Ions (75 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

761008

1.10.3.1

1 mM, slight stimulation

maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme

741635

1.13.11.1

1 mmol/l, 30°C, 15 min, 281% remaining activity

701207

1.6.5.2

increase of enzyme mRNA expression, via a transcriptional mechanism

673294

1.7.2.6

the enzyme activity is increased by 2.62% in the presence of 2 mM Pb2+

764339

1.8.1.9

10 mM, 220% of initial activity

activates slightly

1 mM, 130% of initial activity

698519

2.4.1.304

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

722531

2.4.1.8

1 mM, 50°C, 30 min, enhances the activity moderately

679537

2.5.1.20

maximal stimulation at 5 mM

40% of activity

67% of activity

CaMKII activity and expression are altered in the hippocampus of Pb2+-exposed rats, reaction velocity is reduced by 41% and substrate affinity is increased by 22%, the rats exhibit deficits in hippocampal log-term potentiation and spatial learning, the content of CaMKIIbeta, but not of CaMKIIalpha, in the cytosolic fraction is reduced

664472

2.7.11.24

slight induction of SIMK

activates at 1 mM

139.2% activity at 1 mM

stimulates

stimulation

inhibits enzymatic activity

731151

3.1.26.5

Pb2+ can replace Mg2+

692711

3.1.3.8

5 mM, enhances activity

114263

3.1.8.1

about 1.5fold enhancement of activity at 0.1 mM

1 mM, native enzyme is activated to 109.3% of control, recombinant enzyme is activated to 110.6% of control, beta-glucosidase activity

105.6% relative activity at 2 mM

activates

10 mM, enhances activity

772141

3.2.1.7

137.7% activity at 5 mM

slight stimulation

activates at 1 mM

slight activation

slight stimulation of protease I

stimulates activity

very slight activation

209205

3.5.1.77

slightly enhances activity to about 110% of the standard activity

31891

3.5.1.97

108.6% activity at 1 mM, substrate N-(3-oxooctanoyl)-L-homoserine lactone

774102

4.1.3.30

11% activation, when added instead of Mg2+. 10 mM, in presence of 2.5 mM Mg2+, 14% inhibition

activates

inhibit activity

2 mM, 1.35fold activation

753461

4.3.1.24

treatment of roots leads to increase in mRNA level and in enzyme activity. The increase in activity is not directly correlated with the increase in mRNA

inhibitory

0.1 mM, reduces the enzymatic activity by more than 60%

inhibitory

a significant increase in enzyme activity is observed after exposure to Pb2+ in a concentration-dependent manner (about 2.5fold increase in activity at 0.1 mg/l, about 4.5fold increase in activity at 1 mg/l)

752295

7.3.2.4

exposure to Pb specifically stimulates Nrt1.1-mediated nitrate uptake. Nrt1.1-mediated reduction of Pb2+ uptake is associated with increased pH in the rhizosphere

767219

3D Structure of Enzyme-Ligand-Complex (PDB) (38 results)

Enzyme Kinetic Parameters

K_M Value (6 results)

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7.2.2.12

6 entries

K_i Value (7 results)

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1.1.1.49

0.213

pH 6.0, 25°C

723747

1.14.18.1

0.0109

immobilized enzyme, at pH 6.8 and 25°C

766437

3.1.1.7

675

pH 7.4, 37.4°C

772703

3.2.1.21

0.0126

pH 5.5, 37°C

715732

4.2.1.1

3 entries

IC₅₀ Value (13 results)

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1.1.1.49

0.78

pH 6.0, 25°C

723747

1.14.18.1

0.05085

immobilized enzyme, at pH 6.8 and 25°C

766437

1.8.1.7

0.122

pH 8.0, 25°C

-999

80% inhibition at 1 mM

701794

3.1.8.1

0.049

pH 8.0, 37°C

729353

3.2.1.21

0.0053

pH 5.5, 37°C

References & Links

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Show Reference (713 entries)

Links to other databases for Pb2+

Ligand Pb2+

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 (3 results)

Activator in Enzyme-catalyzed Reactions (4 results)

Inhibitor in Enzyme-catalyzed Reactions (504 results)

Metals and Ions (75 results)

3D Structure of Enzyme-Ligand-Complex (PDB) (38 results)

Enzyme Kinetic Parameters

KM Value (6 results)

Ki Value (7 results)

IC50 Value (13 results)

References & Links

Literature References (713)

Links to other databases for Pb2+

K_M Value (6 results)

K_i Value (7 results)

IC₅₀ Value (13 results)