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Ligand Cd2+
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Basic Ligand Information
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open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
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Cd/cytoplasm + ATP + H2O = Cd/vacuole + ADP + phosphate
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ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
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In Vivo Product in Enzyme-catalyzed Reactions (8 results)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Substrate in Enzyme-catalyzed Reactions (9 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
685477, 246907, 246925, 246928, 654606, 685144, 685314, 685173, 655856, 246929, 656669, 668627, 667735, 670581
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Cd/cytoplasm + ATP + H2O = Cd/vacuole + ADP + phosphate
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ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
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Product in Enzyme-catalyzed Reactions (10 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Activator in Enzyme-catalyzed Reactions (14 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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activation of aminopyrene-N-demethylase activity of CYP2B or CYP3A isoenzymes, which is increased 3- to 4-fold
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100 mM, 111% and 100% enhancement of enzyme activity in root tissue after 7 and 14 days, respectively
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intraperitoneal administration of 1 mg/kg/day for 14 days, increase in enzyme activity by 46% and decrease of total antioxidant status
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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 (999 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
in pea leaves treated with 0.05 mM cadmium, GSNOR expression and activity are decreased by about 30%
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in the presence of Mn2+, Cd2+ ions almost completely inhibit the enzyme activity (5.9% residual activity)
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above 0.1 mM, the enzyme loses activity, and at 2 mM Cd2+ most of the activity has disappeared. Chelation of Cd2+ by dithiothreitol cannot recover the lost enzyme activity. Inactivation of the enzyme by Cd2+ is less effective when the enzyme is activated with Cd2+ than Mg2+, More than 50% of the activity of the enzyme activated with 0.05 mM Cd2+ remains in the presence of 1 mM GSH
binds to C379 of enzyme, resulting in loss of activity and structural alterations. Loss of glutaredoxin activity in cells treated with Cd2+ is more pronounced when cells are transfected with enzyme antisense cDNA
coadministration with oxalomalate results in inhibition of enzyme and glutaredoxin and enhanced susceptibility to apoptosis
inhibits the purified enzyme and the enzyme in cells, NADP+ does not protect. No inhibition of IDPc mutant S269S. DNA fragmentation is enhanced in IDPc siRNA-transfected HEK293 cells compared to control cells upon exposure to cadmium
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
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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+
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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
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after 48 h of exposure to 0.1 mM Cd2+, germination is unaltered, but root length and catalase activity are significantly reduced. 24 h post exposure, catalase activity is restored or even enhanced. The mechanism of catalse inactivation by Cd2+ involves oxidation of the protein structure. Cd2+ induces overexpression of catalase isoforms CatA1 and CatA2 in cotyledon and root
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complete inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
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minimal inhibitory concentrations cadmium to Variovorax sp. 12S strain in different media, overview
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the binding of Cd2+ induces a conformational change in the enzyme structure compared to the wild-type enzyme, overview
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at 0.001-0.005 mM, cadmium induces histone H3 lysine methylation by inhibiting histone demethylase activity on H3K4 and H3K9. 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
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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 induces histone H3 lysine methylation by inhibiting histone demethylase activity on H3K4 and H3K9. 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
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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
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inhibition by interaction with a cysteine residue of the protein that is important for the enzyme activity
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inhibition by interaction with a cysteine residue of the protein that is important for the enzyme activity, inhibition by cadmium ions is reversible by Zn2+ ions
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no effect: 0.05 mM CdCl2 or Cd-EDTA in assay medium, pretreatment of 30-60 min, significant decrease of activity
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70% inhibition, uncompetitive to dibromothymoquinone, noncompetitive inhibition of NADPH oxidation, Zn2+ diminishes the inhibitory effect for dibromothymoquinone reduction, but enhances inhibition of ferricyanide reduction, inhibitory effect on ferricyanide reduction, but on dibromothymoquinone reduction, is abolished by addition of 2-mercaptoethanol or histidine, inhibition mechnanism, overview
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noncompetitive type of inhibition, effect of cadmium binding is significant disturbance in the electron transfer process from FAD to dibromothymoqinone, but less interference with the reduction of ferricyanide. It causes a strong inhibition of ferredoxin reduction, indicating that Cd-induced changes in the FNR structure disrupt ferredoxin binding. Iodoacetamide blocks the sensitivity to Cd2+ inhibition. pH-Dependent inhibition: to interact with cadmium in a mode which leads to inhibition, the cysteine residues of FNR have to be charged. Almost no inhibition in pH lower than pH 7.7, while in pH higher than pH 8.1 the reduction of activity caused by cadmium ions increases, FNR cysteine-peptide mapping, overview. Triticum aestivum FNR is more sensitive to lower cadmium concentrations than the Spinacia oleracea enzyme
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inactivation due to dissociation of FAD from the enzyme molecule and denaturation of the apoenzyme
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0.5 mM, isozyme E I: insensitive, isozyme E II: 44% inhibition; 44% reduced activity of isozyme E-II, no inhibition of isozyme E-I
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2.85 mM, 82% inhibition of pyridoxamine 5'-phosphate oxidation, 27% inhibition of pyridoxine oxidation
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0.05 mM, 66% inhibition. IC50: 0.024 mM, noncompetitive inhibition; 0.05 mM, 66% inhibition, noncompetitive
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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
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in presence of NADH, inhibition is reversed by dithiols and less effectively by monothiols
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the enzyme also possesses a second Cd2+ binding site where Cd2+ binds to induce an inhibitory effect
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inhibits the free enzyme by about 75% and the immobilized enzyme by about 20% at 5 mM
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the ion interacts directly with the catalytic domain of the enzyme and induce unfolding/denaturation of the domain
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binds in the GSH-binding site by coordination with Asp and Gln residues, molecular modeling, overview
the degree of cadmium inhibition, when aniline is the cosubstrate, shows obvious differences between pI isozymes
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inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
inhibition of metal-independent wild type and mutant enzymes D247E, P249A at 2 microM and above, inhibition of mutant 247E/P249A at 8 microM and above
slightly inhibites both O-acetyl-L-serine sulfhydrylation and O-phospho-L-serine sulfhydrylation
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order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
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0.2 mM, 39% inhibition of alanine aminotransferase activity measured in soft body and gills, 0.6 mM, 46% inhibition
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78% inhibition at 1 mM, effect is completely reversed by increasing concentrations of Zn2+, protection by glutathione and dithiothreitol
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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
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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
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isozyme Lip-1 shows 38% relative activity in the presence of 5 mM Cd2+; isozyme Lip-2 shows 28% relative activity in the presence of 5 mM Cd2+
chronic cadmium exposure (32.5 ppm Cd2+ in purified water over 3 months) leads to noncompetitive inhibition of serum and hepatic enzyme activity. The addition of 5 mM of Zn2+ shows almost 58% reactivation of the enzyme
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0.2 mM, 30% inhibition of hydrolysis of di-p-nitrophenyl phosphate, 20% inhibition of 3'-AMP hydrolysis
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noncompetitive inhibition of isoenzyme Q192 and uncompetitive inhibition of isoenzyme R192
noncompetitive inhibition of isoenzyme Q192 and uncompetitive inhibition of isoenzyme R192
noncompetitive inhibition of isoenzyme Q192 and uncompetitive inhibition of isoenzyme R192
1 mM, 33% inhibition of wild-type enzyme, 48% inhibition of mutant enzyme L134R/S320A
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complete inhibition of isozyme AII, high inhibition of isozymes AI-1 and moderate of AI-2, at 5 mM
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inhibits activity at 1 mM, 7.7% relative activity compared with activity without any addition of effector
inhibits activity at 1 mM, 7.7% relative activity compared with activity without any addition of effector
inhibits activity at 1 mM, 7.7% relative activity compared with activity without any addition of effector
inhibits activity at 1 mM, 7.7% relative activity compared with activity without any addition of effector
inhibits activity at 1 mM, 7.7% relative activity compared with activity without any addition of effector
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
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with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 41%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 38%
with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 41%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 38%
with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 41%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 38%
with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 41%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 38%
with 2 mM hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside is reduced to 41%, hydrolysis of p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside to 38%
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
2 mM, 10% residual activity; 2 mM, 21% residual activity; 2 mM, 25% residual activity
no inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 12% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
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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
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at concentration of 1 mM, the enzyme is strongly inactivated by Cd2+ (38.2% residual activity)
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decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
partially inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 76.8% and 49.7% residual activity for chymotrypsin A and B, respectively
partially inactivates both chymotrypsin A and B at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 76.8% and 49.7% residual activity for chymotrypsin A and B, respectively
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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0.5 mM, complete inhibition , characteristic of enzymes with essential vicinal sulfhydryl groups
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inhibitory effect of heavy metals over immobilized enzyme decreases in the order Cu2+, Cd2+, Zn2+, Ni2+, Pb2+
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noncompetitive, binds at the alpha1 subsite ligated by His67, His69 and Asp366
mixed competitive inhibitor. Kidney enzyme is more sensitive to inhibition than liver enzyme. Cd2+ enhances substrate activation of kidney enzyme while still being inhibitory. Cd2+ is also inhibitory to kidney enzyme in presence of Mn2+
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0.1 mM Cd2+ totally inhibits enzyme activity. Dithiothreitol (0.003 mM) is able to restore the inhibition of enzyme activity caused by Cd2+ (0.02 mM)
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enzyme inhibition in excised etiolated leaf segments during greening. Cd2+ inhibits ALAD activity by affecting the ALA binding to the enzyme and/or disrupting thiol interaction. Inhibition of ALAD activity by Cd2+ is decreased in the presence of nitrogenous compounds, glutamine and NH4NO3, overview. Supply of some essential metal ions, such as Mg2+, Zn2+, and Mn2+, also reduces the inhibition of enzyme activity by Cd2+
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inhibition at low concentration of substrate and stimulation at high levels of substrate
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inhibits delta-ALA-D activity. Chelating and antioxidant agents potentiated the inhibition
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exposure of isolated mitochondria to 0.05 mM Cd2+ results in 20-25% inhibition of mitochondrial aconitase activity. Exposure of whole oysters to Cd2+ for 3-6 weeks has no effect on aconitase activity
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the crystallographic data indicate that the inhibition of ferrochelatase by Cd2+ occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation
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the enzyme is maximally inhibited by 25 nM free Cd2+ in the assay medium, with a K(50%) inhibition of 11.3 nM Cd2+. The decreased activity of the sperm ATPases might have a critical importance in the biochemical mechanisms underlying the decreased sperm motility of individuals exposed to Cd2+
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wild-type cells are not able to grow on cadmium chloride containing substrate, but the recombinant strain is able to survive at 1 mM cadmium chloride concentration, the wild-type can grow on 1 mM Cd2+ in presence of 20 mM GSH
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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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98% inhibition at 0.1 M, addition of 0.1 M of Cd2+ to the reaction medium results in almost complete inhibition of dNADH:K3 oxidoreductase activity of membrane vesicles from the wild-type strain
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enzyme activity shows a gradual decrease in post larvae on exposure to 0.12 and 0.24 ppm cadmium
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Metals and Ions (596 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
preincubation with 0.07 or 5 mM leads to 3fold increase of C38D mutant enzyme activity, 0.5 mM, 6.5fold increase of wild-type enzyme activity, substrate L-threonine
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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
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enzyme is stimulated in presence of 3 mg and 5 mg of Cd on the first day of experiment in gill, liver and kidney tissues. The stimulation effect of the 5 mg/l dose of Cd on G6PD and 6PGD enzyme activities is significantly diminished after seven days. The G6PDenzyme activity levels are stimulated by approximately 60% in gills, 68% in liver, and 67% in kidneys
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divalent cation required, Mn2+ and Cd2+ are about equally effective at 0.5 mM
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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
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maximum activity at a ratio of 2 mol M2+/mol of enzyme. Inhibitory above a ratio of 4 mol M2+/mol of enzyme
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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
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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
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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
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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
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0.2 mM, induction of enzyme and 4.5fold enhancement of activity, biliverdin partly prevents
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crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC)
crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC)
the first cadmium ion, Cd1 is coordinated in a trigonal-bipyramidal manner, in which the triangle is formed by the side chains of His25, Asp52, and a water molecule bridging two cadmium ions, and the corner of the pyramid is formed by the side chain of Glu56 and another water molecule. The second cadmium ion, Cd2 is coordinated in a distorted octahedral manner to the side chain of His37 and three water molecules, with two sites remaining unoccupied. Zinc ions are more likely to coordinate in a tetrahedral arrangement. Cadmium ions are also more likely to coordinate in both tetrahedral and octahedral arrangements, but also exhibit a versatile coordination geometry. Cadmium ions are found to be coordinated in a trigonal-bipyramidal manner
the first cadmium ion, Cd1 is coordinated in a trigonal-bipyramidal manner, in which the triangle is formed by the side chains of His25, Asp52, and a water molecule bridging two cadmium ions, and the corner of the pyramid is formed by the side chain of Glu56 and another water molecule. The second cadmium ion, Cd2 is coordinated in a distorted octahedral manner to the side chain of His37 and three water molecules, with two sites remaining unoccupied. Zinc ions are more likely to coordinate in a tetrahedral arrangement. Cadmium ions are also more likely to coordinate in both tetrahedral and octahedral arrangements, but also exhibit a versatile coordination geometry. Cadmium ions are found to be coordinated in a trigonal-bipyramidal manner
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
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induction of enzyme together with heme oxygenase-1 and glutathione S-transferase Ya
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a cadmium ion is found within the active site of each monomer, crystallization data
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activates the enzyme at 0.036-0.36 mM about 4-9fold. PCS activation is self-regulated, because its product poly(4-glutamyl-cysteinyl)glycine chelates Cd2+, and the reaction stops when free Cd2+ ions are no longer available. Cd2+ also activates the enzymes peptidase activity. Presence of PC2, PC3, and PC4 oligomers is evident in extracts from gametophytes exposed to Cd2+ for 7 days, determined by HPLC-ESI-MS-MS analysis
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activation
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Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
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the enzyme is stimulated by more than 2fold by free Cd2+ concentrations of 0.00035-0.001 mM
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the enzyme possesses two Cd2+ binding sites, Cd2+ binds to one of these sites to activate the enzyme. In the presence of 0.01 mM Cd2+, activity increases and reaches the maximum rate with an increase in GSH concentration up to 15 mM
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under 0.085 mM CdCl2 stress for 3d, 1.3- to 2.1-fold increase when compared with wild-type
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4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
substitution of the active site zinc with cadmium increases the affinity of the peptide substrate and decreases the rate constant for the chemical step
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Cd-substituted enzyme has altered specificities with regard to utilization of both peptide and isoprenoid substrates
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can replace Mg2+ in activation, optimal concentration: 5 mM, 68% of the activity with Mg2+
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0.42 and 1.1 mM, maximal activation of forward reaction in the presence of 0.42 and 1.1 mM ATP respectively
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multiphasical activation, at pH below physiological value, inhibits at physiological pH
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causes delayed but strong activation of SIMK, MMK2, MMK3, and SAMK, activation profiles, overview
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a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP
a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
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catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
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the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
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the enzyme activity is increased by 23% and 53% at 0.25 and 0.5 mM Cd2+, respectively
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the enzyme requires a divalent metal ion for activity. The highest activity is observed with Cu2+, followed by Mn2+, Ni2+, Mg2+, Cd2+and Co2+, in the presence of EGTA. When EGTA is replaced by EDTA, activity can be observed. In the absence of divalent metal ions the enzyme is inactive
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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
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Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
the Mn2+-containing enzyme is about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower
the Mn2+-containing enzyme is about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower
the Mn2+-containing enzyme is about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower
a low concentration of 0.05 mM Cd2+ is able to activate alpha-glucosidase activity (enhancing it up to 10%)
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in the wild-type enzyme Cd2+ stimulates hydrolysis of 4-nitrophenyl alpha-D-mannoside to a 4fold lesser extent than Co2+. The side chains at positions 228 and 533 are involved in binding the activating metal ion as their primary function
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maximal activity of 56 U/mg is reached at 1 mM CoCl2. Inactive in absence of metal ion
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potent activator at concentration of 1 mM, 12.5fold activation compared to the apoenzyme
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with alpha-1,2-, alpha-1,3-, alpha-1,4-, or alpha-1,6-mannobiose as a substrate, Co2+ is the only metal ion promoting hydrolysis of all substrates. Mn2+, Cd2+, and Zn2+ can substitute to a varying extent
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inhibitory above 0.05 mM. Reduced catalytic activity in presence of Zn2+ is not due to altered binding of substrate
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metal binding modelling using titration, kinetic, and thermodynamic data, dinuclear metal enzyme, sequential binding to two metal binding sites, affected by Ca2+
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CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations
CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations
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, cadmium chloride pre-treatment of cells significantly inhibits caspase-9 activation in a dose dependent manner, 40% and 52% inhibition at 10 and 20 microM cadmium chloride, respectively
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induces activation of caspase-9, decreases expression of the inactive form pro-caspase-9
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conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI
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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)
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the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
the metal ion is bound in the active site, metalloprotease, metal binding and coordination structure of enzyme XoPDF
apoenzyme reconstituted with Co2+ has 15.8fold lower activity than the native Zn-containing enzyme
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chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
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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
no activity in the presence of 1.0 mM Cd2+, weak enzyme activation at 5 mM (4.% compared to 1.5 mM Mn2+)
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enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
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Cd2+ can partially replace Mn2+, 16%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Cd2+, 38%
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transcripts of ADC in peach leaves are quickly induced in response to treatment with 0.15 mM CdCl2
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0.5 mM chloride salt, 4% relative activity, with 4-hydroxy-2-oxopentanoate as substrate
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5 mM, 90% inhibition of Mg2+-activated enzyme, interaction with catalytic domain induces partial unfolding (revealed by thermal denaturation, far-UV circular dichroism, fluorescence