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Ligand CuCl2

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Basic Ligand Information

Molecular Structure

Picture of CuCl2 (click for magnification)

H₂Cl₂Cu

CuCl2

ORTQZVOHEJQUHG-UHFFFAOYSA-L

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (4 results)

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Activator in Enzyme-catalyzed Reactions (5 results)

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stimulation of activity, 123% relative activity to no addition

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1 mM, 2fold activation

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increase in enzyme mRNA due to transcriptional activation of enzyme gene’s promoter

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1 mM, 107% activity compared to control without any metal ion

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Inhibitor in Enzyme-catalyzed Reactions (184 results)

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1 mM, 100% inhibition

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complete inhibition at 2 mM

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only enzyme forms CR2, CR3

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1 mM, complete inhibition

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1 mM, 66% inhibition

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1 mM, 10% residual activity

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1 mM, 89.8% inhibition

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about 40% loss of activity within 60 min

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strong

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10 mM, 40% inhibition

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strong inhibition

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6.5% activity remains at 10 mM

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1 mM, 30 min at 4°C, 29% inhibition

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completely inhibits the enzyme at 0.01 mM

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1 mM, complete loss of activity

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0.2 mM, complete inhibition

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0.1 mM, 41% inhibition

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1 mM, 70°C, 0.7% activity

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31% loss of activity

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1 microM, inhibition of 95%

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0.4 mM, 67% inhibition

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1 mM, complete inhibition

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complete inhibition at 1 mM

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above 0.01 mM

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1 mM, 10 min at 35°C, complete loss of activity

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1 mM

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1 mM cuprous chloride: slight inhibition

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tested at 0.1 mM, 100% inhibition

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5 mM, about 80% loss of activity

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0.1 mM, complete inhibition

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strong inhibition of apo and holo forms at 0.1 mM

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strong inhibition at 1 mM

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1 mM, strongly inhibited,more than 90%

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with 1 mM 11.2% activity

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1 mM, 41% inhibition

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0.01 mM,70% inhibition; 0.1 mM, 69% inhibition

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0.1 mM, complete inhibition

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10 mM

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0.1 mM

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1 mM, 100% inhibition

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5-10 mM, more than 90% inhibition

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25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction

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complete inhibition at 1 mM or higher

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remaining activity 0.1%

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0.1 mM, 50% inhibition

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1 mM, 59% residual activity

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the recombinant enzyme shows about 20% residual activity at 1 mM

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1 mM, 37% loss of activity

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slight

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10 mM, 24% inhibition

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0.1 mM, 53% inhibition

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10 mM, 69% inhibition

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2 mM, 7% residual activity

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1 mM, 93% inhibition

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1 mM, 65% loss of activity

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20 mM, 20% residual activity

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1 mM, 83% inhibition

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82% inhibition

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5 mM, 37% inhibition

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326393, 326394, 326395

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at 1 mM: inhibition less than 10%

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1 mM, 96% inhibition in presence of 1 mM CoCl2

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0.1 mM, 91% inhibition. 0.01 mM, 87% inhibition

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1 mM, 9% residual activity

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1 mM, 39% inhibition

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complete inhibition at 1 mM

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81296, 81298, 81304

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94% inhibition at 1 mM

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significant inhibition at 1 mM

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

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171922, 171924, 171933

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20% inhibition at 1 mM, 17% at 0.1 mM

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ceramide synthesis activity, 1 mM, total inhibition

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1 mM: 74.4% inhibition

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93% inibition at 1 mM

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85% inhibition at 1 mM

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2.5 mM, 91% loss of activity

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1 mM, 70% loss of carboxylation activity, 14% loss of decarboxylation activity

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1 mM, complete inhibition

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1 mM, 97% inhibition

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1 mM, complete inhibition

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0.1 mM, complete inhibition

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inhibits 37% at 5 mM

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0.1 mM, 70% loss of activity

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97% inhibition at 1 mM

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1 mM causes inhibition enzyme activity (92% relative activity)

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0.7 mM, 50% inhibition

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strong

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Metals and Ions (25 results)

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activates

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1 mM, increases activity by 28.5%

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5 mM, activation to 166% of control

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stimulates enzyme activity in vitro

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1 mM, 123% of initial activity

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10 mM, 3-4fold stimulation

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2.5 mM, stimulation

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1 mM, elevates hydrolysis activity by 40%

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0.05 mM and 0.5 mM increases activity of GPOX

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5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity

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activity 136%

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inhibition

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high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo

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1 mM, 107% activity compared to control without any metal ion

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1 mM, 19% enhancement of activity

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1 mM

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5 mM, 87.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C; 5 mM, 96.4% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C

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1 mM, 236% of initial activity

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5 mM, 79.5% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-glucopyranoside as substrate, pH 4.6, 40°C; 5 mM, 83.6% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-glucopyranoside as substrate, pH 4.6, 42°C

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1 mM, 36% inhibition, isoenzyme MpiCP-1; 1 mM, 73% inhibition, isoenzyme MpiCP-2

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5 mM, complete inhibition

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activates

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10 mM, activates

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relative activity of ACY is 22.9% when dipicolinic acid is removed; relative activity of ACY is 26.4% when EDTA is removed

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no significant activity with 5-oxo-D-proline, stimulates activity with D-glutamate

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Enzyme Kinetic Parameters

K_i Value (2 results)

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0.0021

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with acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin

24514

0.7

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39960

IC₅₀ Value (4 results)

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References & Links

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Show Reference (215 entries)

Links to other databases for CuCl2

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ChEBI