Any feedback?
Please rate this page
(ligand.php)
(0/150)

BRENDA support

Ligand Ba2+

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

Basic Ligand Information

Molecular Structure
Picture of Ba2+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Ba
Ba2+
XDFCIPNJCBUZJN-UHFFFAOYSA-N
Synonyms:
barium ion

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (10 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
2.5 to 3.5fold activation
-
10 mM, activation to 112% of control
-
1 mM, 108% of inital activity
-
1.7fold activation of xylan-inducible enzyme, 1.1fold of xylose-inducible enzyme, at 0.25 mM
-
slight activation at 1 mM
-

Inhibitor in Enzyme-catalyzed Reactions (412 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
92.24% residual activity at 1 mM
-
0.5 mM, 35% inhibition
-
85.8% residual activity at 1 mM
-
70% residual activity at 1 mM
-
5 mM, partial inhibition of activity
-
5 mM, partial inhibition; 5 mM, partial inhibition of activity
-
competitive to Mg2+, wild-type enzyme
-
moderately inhibits PPO
-
partial inhibition of catalase activity
-
partial inhibition at 2 mM
-
1 mM, moderate inhibition
-
complete inhibition at 1 mM
-
weak inhibition
-
slightly inhibiting
-
weak inhibitor
-
1.17% residual activity at 1.0 mM
-
30% inhibition at 1 mM
-
19% inhibition in the presence of 1 mM
-
50% inhibition at 1 mM
-
inhibits NahF activity by 62%; inhibits NahV activity by 52%
-
0.11 mM, 10% inhibition
-
less than 60% residual activity at 3 mM
-
2 mM, 10% loss of activity
-
0.1 mM, 86% inhibition
-
46.47% residual activity at 5 mM
-
5 mM, 60% inhibition
-
1 mM, 25% inhibition
-
relative activity 70% of control
-
weak
-
complete inhibition at 5 mM
-
10 mM, 38% inhibition; 38% inhibition at 10 mM
-
30% of maximal activity
-
10 mM, 61% inhibition
-
1.0 mM, 12% inhibition
-
10 mM, complete inhibition
-
1 mM, 38.1% inhibition
-
10 mM BaCl2, 12% inhibition
-
weak
-
weak
-
1 mM, 93% decrease of activity
-
70.70% residual activity at 5 mM
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
in decreasing order of inhibitory efficiency: Ni2+, Zn2+, Cu2+, Ca2+, Ba2+
-
2 mM
-
20 mM, less than 30% inhibition
-
2 mM, 10% inhibition
-
low inhibition at 1 mM
-
low inhibition at 1 mM
-
inhibits isozyme Tfu 0882 7%
-
5 mM, 32% loss of activity
-
10 mM, 40% loss of activity
-
slight inhibition of intracellular and extracellular enzymes at 5 mM
-
85% of maximal activity at 1 mM BaCl2
-
C-1
-
2 mM, 54% of initial activtiy
-
90% residual activity at 2 mM
-
98% residual activity at 1 mM
-
63.52% residual activity at 1 mM
-
1 mM, complete inhibition
-
strong inhibition at 25 mM
-
40-50% inhibition at 2 mM
-
more than 50% of residual enzymatic activity at 20 mM
-
85% residual activity at 1 mM
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
-
1 mM, 5% inhibition of 2-nitrophenyl beta-D-galactopyranoside hydrolysis, 6% inhibition of 4-nitrophenyl beta-D-glucopyranoside hydrolysis
-
slight inhibition
-
partial
-
48% residual activity at 10 mM
-
some inhibition at 10 mM
-
1 mM, 82% of initial activity
-
addition leads to inhibition of free actinidin whereas immobilized actinidin shows a much weaker inhibition
-
slight inhibition
-
about 64 residual activity at 10 mM
-
5 mM, 85% residual activity
-
54% residual activity at 5 mM
-
1 mM, weak, caseinolytic activity
-
5 mM, slightly decreases activity
-
88% inhibition at 10 mM
-
79.86% residual activity at 10 mM
-
0.01 mM, 17% inhibition
-
5 mM, inhibition from 10-40%
-
slight inhibition at 1 mM
-
slight inhibition
-
1 mM: 5% inhibition
-
strong inhibition at 1 mM
-
26% inhibition at 1 mM
-
44% inhibition at 5 mM
-
1 mM, about 20% decrease in activity
-
8% inhibition at 5 mM
-
slight inhibition at 1 mM
-
0.8 mM, 50% inhibition
-
50 mM, 6% loss of activity
-
inhibited activation by K+ or NH4+
-
36% inhibition at 100 mM, formation of substrate/product precipitate
-
slight inhibition
-
slight inhibition
-
2 mM, 98% inhibition
-
1 mM
-
1 mM, 64% residual activity
-
about 30% inhibition at 0.5 mM
-
about 50% residual activity at 1 mM
-
10 mM, 43% inhibition in presence of 10 mM Mg2+, no activation in absence of Mg2+
-
-
-
27% residual activity
-
inhibits activation by Mn2+
-
1 mM
-
1 mM, 90% loss of activity
-

Metals and Ions (363 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 113% of initial activity
-
up to 200 mM, 2fold increase in activity
-
37% activation at 5 mM only in D-mannitol oxidation
-
activates
-
increase of activity at 10 mM
-
activates
-
up to 200 mM, 2fold increase in activity
-
about 300% activity at 1 mM
-
113% activity at 1 mM
-
activates
-
activates slightly at 1 mM
-
1 mM, 62% of initial activity
-
mutants D354N, N355D, and D354N/N355D
-
136.4% activity at 2 mM
-
activates
-
activates the activity of APX from kiwano at 1-10 mM
-
15% activation at 10 mM
-
activates
-
2 mM, 147% of initial activity
-
1 mmol/l, 30°C, 15 min, 106% remaining activity
-
45% of the activation with Ca2+
-
reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective
-
the activity is elevated to 2-3fold in the presence of 2 mM Ba2+
-
activates
-
5 mM chloride salt, 123.3% activity compared to untreated control
-
5 mM, 26.5% increase in activity
-
129.02% activity compared to no addition 100%
-
activates slightly
-
very low activity
-
metal-free enzyme preparation has no activity, addition of Ba2+ restores 27% of the original activity
-
activates
-
stimulates
-
activation, can replace Ca2+ to a lesser extent
-
about 30% of the activation with Mg2+
-
107% activity at 5 mM
-
activation
-
10 mM, 23fold stimulation
-
slight activation
-
stimulates to a smaller extent than Mn2+
-
requires divalent cation, in decreasing order of effectiveness: Mg2+, Ba2+, Ca2+, Co2+, relative activities: Mg2+: 1.0, Ba2+: 0.77, Ca2+: 0.65, Co2+: 0.31
-
stimulates
-
activates
-
slight activation
-
enhances activity
-
1 mM, less effective than Mg2+ in meeting the divalent ion requirement
-
presence of Ba2+ stimulates the activity by more than 300%
-
slight activation
-
can partially replace Mg2+ in activation
-
10 mM, slight activation
-
2 mM, activity with AMP and deoxythymidine is enhanced about 50%, no absolute requirement
-
slight stimulation, about 14% of activity compared to Mg2+
-
slight inhibition
-
cation requirement is relatively nonspecific, Mg2+, Ba2+ or Ca2+ provides maximal activation in the 10 mM range, Mn2+ or Co2+ stimulates at lower concentration, inhibition at higher concentration
-
markedly activated by 5 mM divalent cations
-
stimulates chondroitin 6-sulfotransferase activity and keratan sulfate sulfotransferase activity
-
activates
-
stimulates
-
117.94% activity at 1 mM
-
divalent cation required
-
stimulation
-
activates isozyme Tfu 0883 7% at 1 mM
-
activates
-
activation
-
strong stimulation of enzyme activity
-
enhances activity
-
53% activation at 1 mM, 46% activation at 20 mM. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified
-
activates
-
40% stimulation at 0.25 mM
-
restores activity after EDTA treatment
-
slight stimulatory effect
-
about 120% activity at 1 mM
-
activation is stronger in presence of 1 mM ascorbate
-
reduces the activity in the range of 10-50%
-
stimulates the activity of the enzyme
-
stimulates
-
0.25 M, activates
-
5 mM, 87% residual activity
-
1 mM, minor stimulation
-
10 mM, activation to 104.65% of control
-
1 mM, activity increases to 104% of control
-
increases activity
-
activates 22% at 1 mM
-
relative activity 101.5%
-
128% activity at 1 mM
-
10 mM, increased the enzyme activity by 96%
-
122% activity at 5 mM
-
116.5% activity at 10 mM
-
120% activity at 1 mM
-
113% activity at 1 mM
-
activation
-
activation
-
0.06 mM, activation to 119% of control
-
activates 8% at 1 mM, 15% at 5 mM
-
about 170% activity at 2 mM
-
10 mM, 1.37fold activity enhancement after 1 h at 55°C
-
3 mM, activity is increased by a factor of two
-
better activator than Mg2+
-
10% activation at 10 mM
-
activity enhanced
-
slight activation of Cda2
-
very slight activation
-
10 mM, slight activation
-
stabilizes partially at 1 mM
-
Ba2+ activates isozymes PAD 1 and 3 to about 15% and 2.5%, respectively, of the level of Ca2+
-
50% of the activation with Ca2+
-
0.01-1 mM, activation
-
5 mM, unable to stimulate enzyme activity
-
7.3% of the activation with Mg2+
-
weak activator
-
sligthly activates
-
4 mM, activates at 17% of the activity of Mg2+
-
gives 10fold lower activity compared to monovalent alkali cations of similar ionic radius, increases association of pyridoxal 5'-phosphate and decreases dissociation rate constant of pyridoxal 5'-phosphate
-
247% stimulation at 15 mM
-
less effective than Mg2+ or Mn2+ or Ca2+
-
about 170% activity at 5 mM and pH 7.5 for N-acetylneuraminate synthesis
-
activation
-
0.45 mM, slight stimulation
-
2 mM, 1.32fold activation
-
1 mM: 109% activity
-
stimulates
-
stimulatory effect, 5 mM greatly accelerates activity
-
1 mM, weak enhancement of activity
-
slight stimulation
-
improves the activity to some extent
-
enzyme activity is 54.6 U/mg protein at a metal concentration of 1 mM
-
activity of enzyme towards UDP-xylose is 23.0 U/mg protein at a metal concentration of 1 mM
-
stimulates activity
-
activates
-
increase in activity
-
slightly activating above 5 mM
-
Ba2+ can replace Mg2+ in activity enhancement
-
Mg2+, Mn2+, Ca2+ and Ba2+ similarly effective, optimal concentration: 0.1 mM
-
increases the activity of wild-type and mutant enzymes at 1 mM
-
stimulates
-
PMCA of neurons is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded
-
activates
-
high affinity Na+ uptake is not inhibited by this cation
-
bivalent cations more effective activators than monovalent cations
-

3D Structure of Enzyme-Ligand-Complex (PDB) (32 results)

top print hide

Enzyme Kinetic Parameters

Ki Value (5 results)

top print hide
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.49
-
40°C
0.8
-
-

IC50 Value (1 result)

top print hide
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
2
-
at pH 6.5 and 70°C

References & Links

top