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:
calcium chloride

Show all pahtways known for Show all pathways known for CaCl2

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (28 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
immobilized enzyme, activating factor, considerable increase in activity
-
at 10 mM 25fold increase in activity
-
0.1 mM
-
1 mM, 7% activation
-
373.5% relative activity at 5 mM
-
2 mM, 50% activation
-
7 mM, 2fold increase in activity
-
5 mM, 2.5 fold stimulation of interior sulfotransferase activity, 1.9 fold stimulation of terminal sulfotransferase activity
-
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
-
0.01 mM, significant enhancement of activity
-
100 mM activates
-
40 mmol/l, 225.53% relative enzyme activity in midgut, 190.24% relative enzyme activity in salivary glands
-
40 mmol/l, 233.33% relative enzyme activity in midgut, 193.31% relative enzyme activity in salivary glands
-
in presence of, increase in optimum temperature and thermostability
-
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 (181 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
100 mM, 30% inhibition
-
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
-
10 mM, 31% inhibition
-
5 mM, about 20% inhibition
-
irreversible loss of activity at 2 M
-
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
-
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
-
10 mM, slightly increases activity
-
reactivation by washing
-
0.1 M, 72% inhibition
-
1 mM, 30-50% inhibition
-
1 mM CaCl2 inhibits 73% and 24% activity of subcellular fractions P3B and P3D respectively
-
1 mM, 3% inhibition
-
33% inhibition of isozyme mtGPAT1, 70% inhibition of isozyme mtGPAT2
-
1 mM, 20% inhibition
-
12.5 mM, 20-30% inhibition
-
1 mM, 17% inhibition
-
1 microM, 60% inhibition. Addition of EDTA restores activity
-
5 mM, 30% inhibition
-
20 mM, 35% inhibition
-
2 mM, 18% inhibition
-
0.8 mM, 35% inhibition
-
1 mM: 29% inhibition, 10 mM: 53% inhibition
-
weak
-
inhibits at 0.1 mM by 64%
-
69% residual activity at 10 mM
-
43% residual activity at 10 mM
-
above 100 mM
-
45 mM, 50% inhibition
-
80% remaining activity at 1 mM, 7% remaining activity at 10 mM
-
10 mM, 98% inhibition
-
remaining activity 3%
-
0.02 M, 35% inhibition
-
90% inhibition at 5 mM
-
noncompetitive
-
21% inhibition at 1 mM
-
no effect at a concentration of 3.3 mM
-
1 mM, residual activity 82.1%
-
10 mM, 22% inhibition of phospholipase B activity, slight activation of lysophospholipase activity
-
at 10 mM 39% inhibition
-
50 mM, 47% inhibition
-
1 mM, 27% inhibition
-
above 200 mM
-
1 mM, 32% inhibition
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 50% remaining activity
-
the enzyme binds to Ca2+, the inhibition is recovered by addition of EGTA and MgCl2
-
above 0.4 mM, pH 7.0
-
1 mM, 94% activity compared to control without any metal ion
-
at 17 mM inhibition
-
10 mM, 48% inhibition
-
1 mM, 27% inhibition of activity with 4-methylumbelliferyl-N,N',N''-triacetylchitotriose, no inhibition of activity with 4-methylumbelliferyl-(GlcNAc)2
-
probably by calcium chelation of polygalacturonic acid
-
1 mM, partial
-
10 mM, 19.9% inhibition
-
inhibits at 5%, the netrapped complexed enzyme is less sensitive, overview
-
72.27% residual activity at 0.5 mM
-
over 90% inhibition at 10 mM
-
5 mM, 15.3% inhibition
-
2 mM, 14.8% inhibition
-
5 mM, 52% residual activity
-
1 mM, 60% inhibition
-
10 mM, 33% inhibition
-
partially
-
at 1 mM causes 21% inhibition of PGI, at 5 mM causes 35% inhibition of PGI
-
1 mM, 50.7% inhibition
-
at 1 mM, inhibition less than 10%
-
reduces adenosine binding
-
50 mM, 5-10% inhibition, no inhibition up to 1 mM
-
100 mM, 52% inhibition
-
43% inhibition at 1 mM, with t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide as substrate
-
strongly inhibits
-
0.1 M, 11% activity
-
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
-
inhibition to a variable extent
-
relative activity 91.7%, incubated for 10 min
-
10% inhibition at 0.5 mM
-
1 mM: 6.2% inhibition
-
1 mM, 32% inhibition
-
inhibition at 50 mM
-
1 mM, 35% inhibition
-
3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
-
in presence of Mn2+, 10 mM MgCl2 inhibits 20%
-
in presence of Mn2+, 10 mM MgCl2 inhibits 20%
-
1 mM, 31% inhibition
-
slight inhibition
-
10 mM, 50°C, 77% loss of activity, dehydration of D-gluconate
-
slight inhibition at 100 mM
-
1 mM reduces activity to less than that without addition of CaCl2
-
2 mM, 28% inhibition
-
mild
-
1 mM, 77% inhibition
-
1 mM, more than 50% inhibition
-
50 mM or greater
-
inhibitory form is the Ca2+diphosphate complex
-

Metals and Ions (145 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation
-
activation
-
2.5 mM, in presence of 5 mM substrate, 40% increase in activity
-
1 mM, stimulates
-
10 mM, activates to 173% of control
-
10 mM, 7.7fold activation
-
5 mM, activation to 164% of control
-
68% activation at 0.1 mM, 97% activation at 1 mM
-
0.1 mM, slight activation of microsomal enzyme
-
30 mM, 3.8fold stimulation of activity of ALDH1
-
divalent cations stimulate activity, highest stimulation observed with CaCl2 is twofold. Activity increased linearly with increasing CaCl2 concentration and reaches saturation at 40 mM
-
10 mM, 1.3fold increase in activity
-
with 1 mM 84.5% activity
-
enhances activity
-
activates slightly
-
1 mM, 15% increase of activity
-
0.1 mM are included in assay medium
-
activates 1.44fold at 10 mM; activates 1.44fold at 10 mM
-
activity is stimulated by thiol reducing agents
-
5 mM, stimulation
-
10 mM, 82% activity retains
-
no activity in absence of divalent cations, 20% of the activation with MgCl2
-
absolute requirement for the addition of a divalent cation, optimal concentration: 0.01 M
-
stimulation at 20 mM, inhibition above 100 mM
-
1 mM relative activity: 115.5%
-
approx. 4fold increase in activity at pH 6.4
-
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
-
activity 107%
-
30 mM, 3fold stimulation
-
activates with increasing temperature to a maximal value
-
added to assay
-
1.24fold stimulation at 1 mM
-
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
-
more pronounced stimulation
-
8% of the activity found compared to optimal Mg2+ concentration
-
1 mM, 1.6fold increase in activity
-
relative activity in presence of CaCl2 10mM 123%
-
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
-
enzyme has 17% as much activity with 1 mM CaCl2 than with MgCl2
-
stimulates at pH 5.5, pH dependent
-
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
-
greatly stimulates, optimum concentration: 2 mM
-
added to optimized fluorescence assay
-
1 mM, 94% activity compared to control without any metal ion
-
5 mM: slight stimulation, at 17 mM inhibition
-
1 mM C-terminal truncated enzyme ApuADELTA: amylase activity: 105%, pullulanase activity: 94%; 1 mM full length enzyme: amylase activity: 111%, pullulanase activity: 101%
-
slight activation
-
maximal activity at 0.15 mM
-
1 mM, activates
-
more effective activation than with NaCl
-
5 mM, activation to 116%
-
slight activation
-
5 mM, 120% of activity
-
5 mM, 107.3% 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, 92.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-glucopyranoside as substrate, pH 4.6, 42°C
-
extracellular enzyme, slight activation
-
IFO 3134, slight activation
-
slight activation
-
activates in absence of Cl-, maximal activity at 0.3 mM
-
optimal activity at 0.01 mM
-
1 mM, 18% inhibition, isoenzyme MpiCP-1
-
0.1 mM and 1 mM, 108.9% and 105.5% compared to a control without additives
-
1 mM, weak activation
-
activation
-
stimulates at 5 mM
-
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
-
tryptase free from trypstatin is activated by 10 mM CaCl2, but tryptase associated with trypstatin is not
-
50 mM, enhances Nalpha-tert-butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl esterase activity
-
5 mM, 1.39fold activation
-
5 mM, 1.13fold activation
-
enhances milk clotting activity
-
required
-
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
-
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
-
5 mM: high activation
-
2-5 mM restores activity of EDTA-inhibited enzyme
-
10 mM, highest stimulation by BaCl2 (8fold), followed by SrCl2, MgCl2, MnCl2, CaCl2 and CoCl2 in a decreasing order of effectiveness
-
activity is dependent on various salts, such as CaCl2, NaCl, KCl, and NaBr, with an optimum concentration of 400 mM
-
maximal activity is observed only in the presence of high concentrations of various salts: KCl, NaCl, NaBr, K2SO4, CaCl2 or MgCl2
-
activity is dependent on various salts, such as CaCl2, NaCl, KCl, and NaBr, with an optimum concentration of 400 mM
-
2.5 mM, 99% stimulation of activity
-
requirement of alkaline earth metal ion for activity. 10 mM, around 2fold increase in activity
-
1 mM, relative activity: 102.0%
-
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
-
activates
-
optimal activity at 0.05-0.5 mM
-
activity: 82%, crude: 100%
-
5-10 mM optimal for activity
-

Enzyme Kinetic Parameters

Ki Value (5 results)

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

IC50 Value (4 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE

References & Links

Links to other databases for CaCl2

ChEBI
PubChem
ChEBI
PubChem