Ligand Cd2+

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Basic Ligand Information

Molecular Structure
Picture of Cd2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Cd
Cd2+
WLZRMCYVCSSEQC-UHFFFAOYSA-N
Synonyms:
cadmium, Cd/cytoplasm, Cd/vacuole

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
show the reaction diagram
-
-

Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Product in Enzyme-catalyzed Reactions (9 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Cd2+-protoporphyrin + H+ = protoporphyrin + Cd2+
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
cadmium-induced inhibition of apoplastic isozyme in barley roots, cationic isozyme C1 is activated by Cd2+
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stimulates enzyme expression
-
activation of aminopyrene-N-demethylase activity of CYP2B or CYP3A isoenzymes, which is increased 3- to 4-fold
-
100 mM, 111% and 100% enhancement of enzyme activity in root tissue after 7 and 14 days, respectively
-
the activity of PCS requires Cd and is enhanced by protein phosphorylation
-
intraperitoneal administration of 1 mg/kg/day for 14 days, increase in enzyme activity by 46% and decrease of total antioxidant status
-
treatment with Cd2+ results in increase in enzyme activitiy along with increase in total phenolics content and decrease in content of chlorophyll and carotinoids in the fronds
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Inhibitor in Enzyme-catalyzed Reactions (853 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.05 and 1.0 mM, 90% inhibition
-
inhibitory
-
IC50 = 0.95 mM
-
complete inhibition at 2 mM
-
complete inhibition at 2 mM
-
1 mM, complete inhibition
-
26-43% inactivation at 1 mM
-
0.1 mM, 33% inhibition
-
slight inhibition
-
500 nM
-
97% inhibition, reduction of 2-dehydropantolactone
-
more than 50% inhibition at 20 mM
-
strongly inhibitory
-
1 mM, 29% inhibition
-
50% inhibition at 8.33 mM; 50% inhibition at 8.3 mM
-
complete inhibition at 1 mM
-
the ERK1/2 inhibitor U0126 can block cadmium-induced inhibition of placental 11beta-HSD2. Cadmium does not alter activities of p38 MAPK, JNK, or PI3 kinase. Cadmium specifically activates the ERK1/2 signaling pathway in human trophoblast cells
-
weak
-
60% residual activity at 1 mM
-
mannitol oxidase is inhibited by heavy metals more than other oxidases
-
0.1 mM concentration 13% inhibition
-
60.6% residual activity at 2 mM
-
cadmium-induced inhibition of apoplastic isozyme in barley roots, 50% inhibition of root growth at 1.0 mM 72 h after the treatment, root growth inhibition due to excess Cd is accompanied by a corresponding loss of plasma membrane integrity in root cells, cationic isozyme C1 is activated by Cd2+
-
competitive inhibitor to Mn2+, uncompetitive to H2O2, reversibly inhibits oxidation of Mn2+ and Mn3+-mediated oxidation of 2,6-dimethoxyphenol, but not oxidation of phenols in absence of Mn2+, Cd2+ inhibits reduction of compound I and II by Mn2+ at pH 4.5 and binds at the Mn2+-binding site, kinetics of inhibition
-
complete inhibition at 1 mM
-
reversible inhibition
-
minimal inhibitory concentrations cadmium to Variovorax sp. 12S strain in different media, overview
-
0.5-1.0 mM, non-competitive
-
2 mM abolishes enzyme activity completely
-
0.4 mM, complete inhibition
-
0.5 mM, strong
-
at 0.001-0.005 mM, cadmium increases global histone H3 methylation, H3K4me3 and H3K9me2, by inhibiting the activities of histone demethylases, and aberrant histone methylation that occurs early (48 h) and at 4 weeks is associated with cadmium-induced transformation of BEAS-2B cells at the early stage
-
at 0.001-0.005 mM, cadmium increases global histone H3 methylation, H3K4me3 and H3K9me2, by inhibiting the activities of histone demethylases, and aberrant histone methylation that occurs early (48 h) and at 4 weeks is associated with cadmium-induced transformation of BEAS-2B cells at the early stage
-
1 mM, about 15% residual activity
-
strong inhibition
-
soluble enzyme form more than the membrane-bound form
-
strong inhibition of 7-ethoxyresorufin-O-deethylase, EROD, and a lower inhibition of 7-ethoxycoumarin-O-deethylase, ECOD, activity, cadmium causes damage to the protein structure
-
0.0001 mM, 66% inhibition
-
0.4 mM, 100% inhibition
-
no effect: 0.05 mM CdCl2 or Cd-EDTA in assay medium, pretreatment of 30-60 min, significant decrease of activity
-
strong inhibition
-
100% inhibition at 1 mM; 1 mM, 100% inhibition
-
1 mM Cd(Ac)2, 92% inhibition
-
1 mM, 12 h, 4°C, 93% loss of activity
-
0.032 mM, complete inhibition
-
probably bind the dithiol group in the lipoic acid
-
1 mM, no residual activity
-
1 mM: less than 20% inhibition
-
inhibits possibly due of interfering with energy transport mechanism
-
0.5 mM slightly decreases GOGAT activity in the absence of 2-oxoglutarate
-
inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
-
38% inhibition at 10 mM
-
2.0 mM
-
5 mM, 69% inhibition
-
0.13 mM, complete inhibition
-
0.05 mM, 66% inhibition. IC50: 0.024 mM, noncompetitive inhibition; 0.05 mM, 66% inhibition, noncompetitive
-
0.002 mM, 40% inhibition, 10 mM EDTA protects up to 0.1 mM metal concentration
-
1 mM, no residual activity
-
decreases in hydroxylamine oxidoreductase-specific oxygen uptake rate followed by a recovery of hydroxylamine oxidoreductase-specific oxygen uptake rate above steady-state levels do occur upon exposure to Cd2+ concentrations of 0.03 mM and greater
-
in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
-
5 mM CdCl2, complete loss of activity
-
5 mM, complete inhibition
-
1 mM, complete inhibition
-
1 mM, 99% inhibition
-
0.1 mM, 94% inhibition
-
1 mM, strong
-
complete inhibition at 0.1 mM
-
strong
-
weak
-
complete inactivation
-
slightly inhibitory
-
complete inhibition of wild-type and mutant enzymes
-
complete inactivation at 10 mM
-
about 96% residual activity at 1 mM
-
at 1 mM
-
partial inhibition at 1 mM
-
0.1 mM, 51% inhibition
-
25 mM, 1% residual activity
-
slight inhibition at 1 mM
-
23% inhibition at 2 mM
-
inhibits Mn2+-activated enzyme
-
10 mM, complete inhibition
-
10 mM
-
10 mM CdCl2, 85% inhibition
-
strong
-
strong
-
the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
-
55% inhibition at 1 mM
-
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
85% inhibition at 1 mM
-
in excess
-
2 mM, at least 80% inhibition of transphosphorylation
-
65% inhibition at 1 mM
-
Cd2+ conspicuously inactivates the activity of the muscle-type enzyme in a first-order kinetic process and exhibits non-competitive inhibition with creatine and ATP. Cd2+ induces tertiary structure changes in enzyme PSCKM with exposure of hydrophobic surfaces. The addition of osmolytes, such as glycine and proline, partially reactivates the enzyme. Molecular dynamics and docking simulations between PSCKM and Cd2+ show that Cd2+ blocks the entrance of ATP to the active site of the enzyme, computational modeling, overview
-
inhibits when incubated in presence of Mg2+ at the same concentration
-
only NDP-arsenolysis or NDP/phosphate-exchange reaction
-
inhibits uridylyl removing activity
-
more than 70% inhibition at 0.1 mM
-
inhibits the synthesis of s4U
-
1 mM, almost complete inhibition
-
recombinant enzyme form SULT1 ST5
-
strongly inhibited by 5 mM
-
5 mM, strong inhibition
-
strong inhibition in vitro and in vivo, 50% inhibition of purified enzyme at about 0.0025 mM, 50% inhibition in liver cytosol at about 0.025 mM
-
very potent inhibitor
-
complete inhibition at 2 mM
-
low inhibition at 1 mM
-
low inhibition at 1 mM
-
5 mM, 92% inhibition
-
in presence of equimolar Mg2+, polyhistidine-tagged enzyme
-
slight stimulation
-
10 mM, more than 90% inhibition
-
complete inhibition
-
1 mM, 40% residual activity
-
1 mM, 45% inhibition
-
1 mM, no activity
-
50% inhibition at 1 mM
-
effective inhibition at 5 mM
-
97% inhibition at 5 mM
-
1 mM, strong inhibition
-
no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 12% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
1 mM
-
preferentially binds to DNA bases rather than phosphates, the presence of the metal ions causes the enzyme to lose the ability for preferential binding to damaged DNA
-
1 mM, complete inhibition
-
1 mM,% inhibition
-
enzyme from lymphocyte
-
0.06 mM, 29% inhibition
-
10 mM, 48% inhibition
some inhibition at 1 mM
-
inhibition of amidolytic activity
-
competitive to other metal ions
-
inhibits esterase activity
-
anti-apoptotic cell survival function of cadmium, cadmium inhibits apoptosis induced by benzo[a]pyrene-7,8-diol-9,10-epoxide (BPDE) at non-cytotoxic concentrations, 40% and 52% inhibition at 10 and 20 microM cadmium chloride, respectively
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strong inhibition
-
33% inhibition at 0.5 mM
-
at pH 10, not at pH 7
-
weak, 0.1 mM, peptide I as substrate
-
inhibits at 10 mM
-
1 mM, complete inhibition
-
complete inhibition at 1 mM
-
complete inhibition at 50 mM
-
0.5 mM, complete inhibition , characteristic of enzymes with essential vicinal sulfhydryl groups
-
65% inhibition at 2 mM
-
18% inhibition at 1 mM
-
1 mM: 15% inhibition
-
2 mM, 86% inhibition
-
2 mM, 60% inhibition
-
1 mM
-
44% residual activity at 1 mM
-
53% inhibition at 1 mM Cd2+
-
at pH 6.5
-
1 mM, 100% inhibition
-
2-mercaptoethanol partially protects
-
0.01 mM 88% inhibition
-
complete inhibition at 1 mM
-
1 mM
-
0.5 mM, reduces the enzymatic activity to 25%
-
partial
-
1 mM, no residual activity; 1 mM, no residual activity
56.0% activity at 0.1 mM and 5.4% activity at 1 mM chloride salt
-
71.6% inhibition at 1 mM
-
complete inhibition at 1 mM
-
the inhibitory effect of metal ions is decreased in presence of 2-mercaptoethanol
-
8% inhibition at 1 mM
-
2 mM, 25% residual activity
-
26-29% reduced activity at 1 mM
-
1 mM
-
0.1 mM, 100% inhibition
-
inhibits the enzyme to a variable degree in the cell extract
-
CdCl2, 1 mM, 100% inhibition
-
strong
-
strong inhibition at 1 mM, activates at 0.1 mM
-
57% inhibition at 1 mM
-
0.5 mM in presence of 1 mM Mg2+, complete inhibition
-
in presence of 0.2 mM CoCl2
-
weak inhibition
-
slight inhibition
-
about 30% residual activity at 1 mM
-
in presence of 0.1 mM Mg2+
-
0.5 mM, activity is reduced by 60%
-
inhibits activation by Mn2+
-
1 mM, 70% inhibition
-
in presence of Mg2+
-
5 mM, abolishes ligation reaction in presence of 5 mM Mg2+
-
low concentrations of Cd2+ strongly inhibit revers transhydrogenation
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1 mM, potent inhibitor
-
complete loss of ATP hydrolysis and proton transport. Exposure does not enhance the lipid peroxidation in plasma membrane, but causes an increase in the saturation of plasma membrane fatty acids and a decrease of the fatty acid chain length
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Ki: 0.004-0.008 mM, competitive inhibition
-
the nrt1.8-1 mutant shows a nitrate-dependent Cd2+-sensitive phenotype
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Metals and Ions (694 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
about 20% of the activity with Zn2+
-
stimulation
10 mM, 2fold increase in activity
-
absolute requirement for divalent cations
the activity of 6PGD is stimulated after three days in the liver at a dose of 1 mg/l Cd and on the first day in gill, liver and kidney tissues at doses of 3 and 5 mg/l Cd. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished
-
inhibits enzymatic activity
-
1 mM, slight activation
-
induction
-
can replace Ca2+ in reactivation after thermal inactivation
-
activates
-
or Ca2+, Sr2+, or Mn2+, 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
-
maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
-
Cd2+ exhibizs octahedral, hexacoordinate ligation geom,etry similar to that of Mn2+. Cd2+ also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein
-
in liver, by 24 h, exposure to alow dose of Cd causes 13% loss of Gpx4a expression. At higher dose, Cd leads to 40% decrease in Gpx4a expression. Longer exposure periods cause about 20% loss of liver Gpx4a expression by low Cd dose; olfactory isoform Gpx4b mRNA expression is not extensively modulated by presence of cadmium ions. In liver, by 24 h, exposure to alow dose of Cd causes 18% loss of Gpx4b expression. At higher dose, Cd leads to 37% decrease in Gpx4b expression. Longer exposure periods cause about 22% loss of liver Gpx4b expression by low Cd dose, whereas at higher Cd exposures, a 33% loss in Gpx4b expression is observed
-
activates by 127% at 3 mM
-
induces LOX activity. Cd-induced intracellular LOX activity increases equally along the barley root tip, while Cd-induced apoplastic LOX activity is associated mainly with the differentiation zone of the barley root tip. Cd-induced LOX activity in plants growing at 21°C increases with increasing temperatures
-
at 10 mM strong inhibition
-
activates
-
0.007-0.1 mM, maximal stimulation at 0.007 mM
-
0.2 mM, induction of enzyme and 4.5fold enhancement of activity, biliverdin partly prevents
-
slightly activating at 1 mM
-
inhibitory effect
-
Cd2+ weakly inhibits enzyme activity at low pH values
-
5 mM sulfate salt, 58.9% activity compared to untreated control
-
increases activity
-
39.52% activity compared to no addition 100%
-
0.5 mM increases GOGAT activity in the presence of 2-oxoglutarate
-
increases both GDH aminating and deaminating activity, accumulating in roots and shoots of seedlings not only increases GDH activity, but also modifies its coenzymatic specificity
-
highly, specifically stimulating for ubiquinone reduction, optimal at 0.5 mM
-
0.05 mM, 2fold stimulation
-
a cadmium ion is found within the active site of each monomer, crystallization data
-
can substitute for Mg2+
-
absolute requirement for a divalent metal ion. 1 mM Cd2+ stimulates 14fold
-
activation, can replace Mn2+ to some extent, 0.5-1 mM
-
CdCl2 slightly stimulates
-
activation
-
CdCl2, slightly stimulates
-
activates
-
20% of activation by Mg2+
-
stimulates
-
activation
-
6-7% of the activity with Mn2+
-
activation, can replace Mn2+ to some extent
-
can partially replace Mg2+
-
activates
-
weak activation with thiamine and aniline as substrates
-
1 mM, 30% increase of activity
-
substitution of the active site zinc with cadmium increases the affinity of the peptide substrate and decreases the rate constant for the chemical step
-
requirement, can be replaced by Mg2+, Mn2+, Ca2+, Zn2+, Ni2+, Co2+
-
slight activation
-
slight activation
-
8% of the activation with Mg2+, at 1.3 mM
-
can partially replace Mn2+ in activation
-
0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively
-
38% of the activation with Zn2+
-
can partially replace Mg2+ in activation
-
multiphasical activation, at pH below physiological value, inhibits at physiological pH
-
less effective
-
requirement for Mg2+ can partially be replaced by Mn2+, Ca2+, Co2+ and Cd2+
-
can partially substitue Mg2+
can partially substitue Mg2+
-
can partially substitue Mg2+
-
can partially substitue Mg2+
-
can partially substitue Mg2+
-
can partially substitue Mg2+
-
increased content in soil decreases enzyme activity
-
causes severe precipitation problems in the phosphate buffer; precipitates in phosphate buffer
can partially replace Mg2+ in activation
-
no activity at 7.5 mM
-
S0.5 value 0.74 mM in direction of synthesis of ADP-glucose
-
slight activation
-
inhibitory
-
121% activity at 1 mM
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
-
can substitute for Zn2+
-
inhibitory in the presence of Mg2+
-
2 mM, activates reaction, can modulated the substrate length requirement
-
with 0.2 mM, at 37°C, pH 7.4, 28% relative activity when compared to Co2+
-
changes the cleavage pattern
-
inhibitory effect
-
can replace Mg2+ in activation, with less than 15% of the efficiency
-
G6Pase is not a target of Cd2+ insult, the G6Pase activity measured at 37°C is high only in 1-month Cd2+-treated group (0.84mg/kg, 35% increase of activity), in 1-week Cd2+-treated group measurements of G6Pase activity at 25°C show marginal increase
-
only marginal stimulating effects
-
fully restored activity if chelating agents used
-
slight stimulation
-
complete inhibition
-
activation
-
activation, 1 mM, inhibits at 10 mM
-
preferred divalent cation
-
activates
-
114.2% activity at 100 mM
-
highly stimulated
-
5 mM, about 5% inhibition
-
inhibitory above 0.05 mM. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate
-
functional in the presence of, highest activity at pH 9
-
isoform MAP, may substitute for Co2+
-
the bimetallic enzyme contains eihter 2 Zn2+ or 2 Cd2+ or Zn2+ and Cd2+
-
activates
-
can reverse the inhibition by chelating agents
-
slight activation
-
stabilizes
-
can replace Ca2+
-
1 mM: increase of activity by factor 1.7
-
conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI
-
restores activity after EDTA treatment
-
0.3 mM Cd2+ lead to a 1.6 and 2.3fold increase in the 20S proteasome activity after 3 and 10 days, respectively, in leaves, the chymotrypsin activity of the 20S proteasome is maximally increased only after 3 days of treatment with 0.03 mM and 0.3 mM Cd2+ (1.5 and 2.5fold, respectively), no major effect of Cd2+ on the chymotrypsin activity of the 20S proteasome is observed in roots or leaves of plant treated with low Cd2+ concentrations (0.0003 mM and 0.003 mM)
-
65% of activity with Zn2+
-
activates
-
activates
-
very slight activation
-
active site-bound
apoenzyme reconstituted with Co2+ has 15.8fold lower activity than the native Zn-containing enzyme
-
can replace Zn2+
-
can replace Mn2+, 85% of activity measured in the presence of Mn2+
-
0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89
4 Cd2+ sites per subunit, enzyme activity lower compared to Mg2+
-
stimulated in the micromolar range to a lower extent than Cu2+ and Mn2+
-
no activity in the presence of 1.0 mM Cd2+, weak enzyme activation at 5 mM (4.% compared to 1.5 mM Mn2+)
-
inhibitory at high concentrations
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
-
0.002-0.005 mM, 3.5fold stimulation
-
Cd2+ can partially replace Mn2+, 16%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Cd2+, 38%
-
no effect
-
enzyme can perform its cycle in the absence of Mg2+, using CdATP2- in the place of MgATP2-
-
activates
-
28% of the activation with Mg2+
-
MgCd2, activates at 37% of the activity of Mn2+
-
the enzyme activity is also promoted with 1 mM Cd2+
-
0.5 mM chloride salt, 4% relative activity, with 4-hydroxy-2-oxopentanoate as substrate
-
5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, fluorescence spectra, and glutaraldehyde crosslinking)
-
absolute requirement for divalent metal ion: Mg2+, Mn2+, Co2+, Zn2+ or Cd2+; Km: 0.0034 mM, reaction with L-4-carboxy-4-hydroxy-2-oxoadipate
-
highest activity at 50 mM
-
14% of the activation with Mg2+
enzyme is up-regulated in plants treated with Cd2+. Overexpression in Arabidopsis and Solanum lycopersicum confers tolerance to cadmium stress
-
the enzyme is activated by the presence of Co2+, Mg2+, Ni2+, Cd2+
-
stimulates
-
0.01 mM, stimulates
-
activates
-