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Ligand CaCl2

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Basic Ligand Information

Molecular Structure
Picture of CaCl2 (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
H2CaCl2
CaCl2
UXVMQQNJUSDDNG-UHFFFAOYSA-L
Synonyms:
CaCl, calcium chloride

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (31 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
immobilized enzyme, activating factor, considerable increase in activity
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at 10 mM 25fold increase in activity
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0.1 mM
-
1 mM, 7% activation
-
373.5% relative activity at 5 mM
-
2 mM, 50% activation
-
100 mM, 151% increase in activity
-
7 mM, 2fold increase in activity
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5 mM, 2.5 fold stimulation of interior sulfotransferase activity, 1.9 fold stimulation of terminal sulfotransferase activity
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14 mM, 30°C, pH 7.5, relative activity 126% with glycogen synthase D as substrate and 232% with histone as substrate compared to no addition
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0.01 mM, significant enhancement of activity
-
100 mM activates
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40 mmol/l, 225.53% relative enzyme activity in midgut, 190.24% relative enzyme activity in salivary glands
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40 mmol/l, 233.33% relative enzyme activity in midgut, 193.31% relative enzyme activity in salivary glands
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in presence of, increase in optimum temperature and thermostability
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stimulation
-
473% residual activity at a concentration of 1 mM
-
0.5 mM, pH 5.6, 45% increase in activity
-
1 mM, 1.4fold activation
-

Inhibitor in Enzyme-catalyzed Reactions (197 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
100 mM, 30% inhibition
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2.5 mM, in presence of 50 mM substrate, 12% decrease in activity
-
1 mM, 28% inhibition
-
1 mM, 29.1% inhibition
-
1 mM, 21% residual activity
-
15% inhibition at 0.5 mM
-
1 mM, 72.8% of the activity without metal ion
-
5 mM, about 20% inhibition
-
irreversible loss of activity at 2 M
-
10 mM, 81% residual activity
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0.001 mM, 56% inhibition
-
0.1 mM, 9% inhibition
-
little or no effect
-
16% inhibition at 1 mM
-
98% of initial activity at 0.005 mM
-
10 mM
-
1 mM, 30°C, 11% loss of aminating activity
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0.09 mM, 50% inhibition
-
1 mM, slightly inhibited,less than 24%
-
3 mM, 28% loss of activity
-
8 mM, 50% inhibition, competitive vs. cytochrome b5
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10 mM, slightly increases activity
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reactivation by washing
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0.25 mM, 9.1% loss of activity
-
0.1 M, 72% inhibition
-
1 mM, 30-50% inhibition
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1 mM CaCl2 inhibits 73% and 24% activity of subcellular fractions P3B and P3D respectively
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1 mM, 3% inhibition
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33% inhibition of isozyme mtGPAT1, 70% inhibition of isozyme mtGPAT2
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1 mM, 20% inhibition
-
12.5 mM, 20-30% inhibition
-
1 mM, 17% inhibition
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1 microM, 60% inhibition. Addition of EDTA restores activity
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5 mM, 30% inhibition
-
20 mM, 35% inhibition
-
2 mM, 18% inhibition
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0.8 mM, 35% inhibition
-
1 mM: 29% inhibition, 10 mM: 53% inhibition
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weak
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inhibits at 0.1 mM by 64%
-
69% residual activity at 10 mM
-
43% residual activity at 10 mM
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above 100 mM
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45 mM, 50% inhibition
-
80% remaining activity at 1 mM, 7% remaining activity at 10 mM
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10 mM, 98% inhibition
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remaining activity 3%
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0.02 M, 35% inhibition
-
90% inhibition at 5 mM
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5 mM, 5% inhibition
-
noncompetitive
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21% inhibition at 1 mM
-
no effect at a concentration of 3.3 mM
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1 mM, residual activity 82.1%
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10 mM, 22% inhibition of phospholipase B activity, slight activation of lysophospholipase activity
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at 10 mM 39% inhibition
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50 mM, 47% inhibition
-
1 mM, 27% inhibition
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above 200 mM
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1 mM, 32% inhibition
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14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 50% remaining activity
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the enzyme binds to Ca2+, the inhibition is recovered by addition of EGTA and MgCl2
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above 0.4 mM, pH 7.0
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reduces adenosine binding
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1 mM, 94% activity compared to control without any metal ion
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at 17 mM inhibition
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10 mM, 48% inhibition
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1 mM, 27% inhibition of activity with 4-methylumbelliferyl-N,N',N''-triacetylchitotriose, no inhibition of activity with 4-methylumbelliferyl-(GlcNAc)2
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probably by calcium chelation of polygalacturonic acid
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1 mM, partial
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10 mM, 19.9% inhibition
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inhibits at 5%, the netrapped complexed enzyme is less sensitive, overview
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72.27% residual activity at 0.5 mM
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over 90% inhibition at 10 mM
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5 mM, 15.3% inhibition
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2 mM, 14.8% inhibition
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5 mM, 52% residual activity
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1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity
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1 mM, 60% inhibition
-
10 mM, 33% inhibition
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partially
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at 1 mM causes 21% inhibition of PGI, at 5 mM causes 35% inhibition of PGI
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1 mM, 50.7% inhibition
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at 1 mM, inhibition less than 10%
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50 mM, 5-10% inhibition, no inhibition up to 1 mM
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100 mM, 52% inhibition
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43% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
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strongly inhibits
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0.1 M, 11% activity
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91% inhibition at about 40 mM
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the maximal enzymatic activity is obtained at 110°C in the presence of CaCl2. In the absence of CaCl2, the maximal activity observed is obtained at 100°C. Below 100°C the enzyme activity does not show significant differences either with or without CaCl2. Concentrations higher than 1 mM CaCl2 show an inhibitory effect on enzymatic activity
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inhibition to a variable extent
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relative activity 91.7%, incubated for 10 min
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10% inhibition at 0.5 mM
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1 mM: 6.2% inhibition
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1 mM, 32% inhibition
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1 mM, dextran-conjugated enzyme and native enzyme retain 45.9% and 51.9% of their initial activities
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5 mM, 34% inhibition
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1 mM, 35% inhibition
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3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
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in presence of Mn2+, 10 mM MgCl2 inhibits 20%
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1 mM, 40% decrease of activity in HEPES and a 15% decrease in Tris/HCl buffer
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slight inhibition
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0.1 mM, 87% inhibition
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5 mM, about 10% residual activity
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18% inhibition at 5 mM; 5 mM, 18% inhibition
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10 mM, 50°C, 77% loss of activity, dehydration of D-gluconate
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slight inhibition at 100 mM
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1 mM reduces activity to less than that without addition of CaCl2
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2 mM, 28% inhibition
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mild
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1 mM, 77% inhibition
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1 mM, more than 50% inhibition
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50 mM or greater
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inhibitory form is the Ca2+diphosphate complex
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Metals and Ions (165 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation
-
activation
-
2.5 mM, in presence of 5 mM substrate, 40% increase in activity
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1 mM, stimulates
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10 mM, activates to 173% of control
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10 mM, 7.7fold activation
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the enzyme shows highest activity at 64°C and with 2 M CaCl2
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5 mM, activation to 164% of control
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68% activation at 0.1 mM, 97% activation at 1 mM
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0.1 mM, slight activation of microsomal enzyme
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30 mM, 3.8fold stimulation of activity of ALDH1
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divalent cations stimulate activity, highest stimulation observed with CaCl2 is twofold. Activity increased linearly with increasing CaCl2 concentration and reaches saturation at 40 mM
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10 mM, 1.3fold increase in activity
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with 1 mM 84.5% activity
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enhances activity
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activates slightly
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1 mM, 15% increase of activity
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0.1 mM are included in assay medium
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activates 1.44fold at 10 mM
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activity is stimulated by thiol reducing agents
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5 mM, stimulation
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the ability of cold-water-extractable, heat-stable polymers (CHPs) to solubilize XTHs from Arabidopsis cell walls is mimicked by NaCl and CaCl2. The effect plateaues above about 30 mM CaCl2, while the CHP effect does not plateau even at the highest concentration tested (1.8 mg/ml). The relative effect of CHP is greatest (34fold promotion) in the absence of CaCl2, but strong CHP effects (4.6 to 9.1fold promotion) and much higher absolute XET activities are still detected in the presence of 15 mM CaCl2, indicating synergy between CHP and the inorganic salt
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10 mM, 82% activity retains
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no activity in absence of divalent cations, 20% of the activation with MgCl2
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absolute requirement for the addition of a divalent cation, optimal concentration: 0.01 M
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stimulation at 20 mM, inhibition above 100 mM
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1 mM relative activity: 115.5%
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approx. 4fold increase in activity at pH 6.4
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2 mM ADP and 2 mM D-fructose 6-phosphate, CaCl2 show the lowest activity with 75% of the activity measured in the presence of MgCl2, activity does not change with the cation concentration in the range of 2.5 to 7 mM
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MnCl2 yields 9% of the activity observed when MgCl2 is included in the assay
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activity 107%
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30 mM, 3fold stimulation
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activates with increasing temperature to a maximal value
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1 mM, 1.3fold activation
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added to assay
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10 mM, 22% inhibition of phospholipase B activity, slight activation of lysophospholipase activity, to 8% at pH 5.0 and 4% at pH 7.0
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more pronounced stimulation
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8% of the activity found compared to optimal Mg2+ concentration
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1 mM, 1.6fold increase in activity
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relative activity in presence of CaCl2 10mM 123%
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activation, e.g. chlorides of Ca2+, Mg2+, K+, Na+, (NH4)2SO4 or NaHCO3, non-specific effect, activity depends on ionic strength with maximum sensitivity between 0.05 and 0.1 and saturation at 0.2
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enzyme has 17% as much activity with 1 mM CaCl2 than with MgCl2
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CaCl2 is required for activity, and the optimal concentration of CaCl2 for the full-length enzyme is 4 mM, the isolated C-terminal domain is most active at 3 mM
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stimulates at pH 5.5, pH dependent
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entirely dependent on the presence of divalent cations, activity with 0.2 mM CaCl2 is 15.9% of maximal activity obtained with 2 mM MgCl2
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greatly stimulates, optimum concentration: 2 mM
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added to optimized fluorescence assay
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1 mM, 94% activity compared to control without any metal ion
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5 mM: slight stimulation, at 17 mM inhibition
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1 mM, 1.2fold activation
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slight activation
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maximal activity at 0.15 mM
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1 mM, activates
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5 mM, 1.1fold activation
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more effective activation than with NaCl
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1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity
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the hydrolytic activity displays a maximum increase of 138% in the presence of 1.1 M NaCl. The hydrolytic activity is higher when using CaCl2 compared to NaCl. In the synthesis of fucosylated oligosaccharides using 4-nitrophenyl-fucose as donor substrate and lactose as acceptor, the presence of 1.1 M CaCl2 favors the rate of transfucosylation, and improves the yield of synthesis duplicating and triplicating it with lactose concentrations of 58 mM and 146 mM, respectively. CaCl2 does not significatively affect hydrolysis rate in these reactions. The combination of the activating effect of CaCl2, the decrement in water activity and lactose concentration has a synergistic effect favoring the synthesis of fucosylated oligosaccharides
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5 mM, activation to 116%
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slight activation
-
5 mM, 120% of activity
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extracellular enzyme, slight activation
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slight activation
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activates in absence of Cl-, maximal activity at 0.3 mM
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optimal activity at 0.01 mM
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1 mM, 18% inhibition, isoenzyme MpiCP-1
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0.1 mM and 1 mM, 108.9% and 105.5% compared to a control without additives
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1 mM, weak activation
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activation
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stimulates at 5 mM
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recombinant S1P-1 activity can be stimulated by Ca2+, but is not dependent on Ca2+. Increases activity of recombinant S1P-1 60% at 4 mM, higher concentrations of CaCl2 lowers the activity
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tryptase free from trypstatin is activated by 10 mM CaCl2, but tryptase associated with trypstatin is not
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50 mM, enhances Nalpha-tert-butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl esterase activity
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5 mM, 31% inhibition
-
5 mM, 1.39fold activation
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5 mM, 1.13fold activation
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enhances milk clotting activity
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required
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the maximal enzymatic activity is obtained at 110°C in the presence of CaCl2. In the absence of CaCl2, the maximal activity observed is obtained at 100°C. Below 100°C the enzyme activity does not show significant differences either with or without CaCl2. Concentrations higher than 1 mM CaCl2 show an inhibitory effect on enzymatic activity
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allows some peptidase and caseinase activity in the absence of any nucleotide, however Ca2+ abolishes ATP hydrolysis and prevents further activation by ATP and 5'-adenylyl beta,gamma-imidodiphosphate
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5 mM: high activation
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2-5 mM restores activity of EDTA-inhibited enzyme
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10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
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activity is dependent on various salts, such as CaCl2, NaCl, KCl, and NaBr, with an optimum concentration of 400 mM
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maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
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activity is dependent on various salts, such as CaCl2, NaCl, KCl, and NaBr, with an optimum concentration of 400 mM
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2.5 mM, 99% stimulation of activity
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requirement of alkaline earth metal ion for activity. 10 mM, around 2fold increase in activity
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no significant activity with 5-oxo-D-proline, stimulates activity with D-glutamate
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1 mM, relative activity: 102.0%
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activates the purified enzyme by 50% at 1-100 mM, activates at 0.005% in the culture medium, activation is lowered in presence of MgSO4
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activates
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optimal activity at 0.05-0.5 mM
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activity declines to 82%, concentration of metal ion not given in the text
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activates to 120% activity at 1 mM
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5-10 mM optimal for activity
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Enzyme Kinetic Parameters

Ki Value (5 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.6
-
pH 9.0, 37°C
0.59
-
-
1.5
-
-
1.15
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with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
1
-
-

IC50 Value (5 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.164
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pH 7.4, temperature not specified in the publication

References & Links

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Links to other databases for CaCl2

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ChEBI
PubChem
ChEBI
PubChem