Ligand Li+

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Basic Ligand Information

Molecular Structure
Picture of Li+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Li
Li+
HBBGRARXTFLTSG-UHFFFAOYSA-N
Synonyms:
Li+[side 1], Li+[side 2], lithium, lithium ion

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Li+/in = ADP + phosphate + Li+/out
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + Li+/in = ADP + phosphate + Li+/out
show the reaction diagram
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Activator in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
less than 1% of the activity with K+
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at 67 mM, 1.3fold activity
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1 mM, activation to 187% of control
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stimulates activity with increasing amounts from 5 mM (25%) to 20 mM (38%)
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can partly replace Na+, less efficient
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Inhibitor in Enzyme-catalyzed Reactions (270 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
24.4% inhibition at 50 mM of the reverse reaction
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strong inhibition
-
complete inhibition at 1 mM
-
about 92.32% residual activity at 1 mM
-
slight inhibition
-
slight inhibition
-
competitive, forward reaction
-
inhibits 17% at 10 mM
-
8% inhibition at 0.1 mM
-
87% residual activity at 5 mM
-
22% inhibition at 5 mM, at 37°C
-
slight inhibition
-
20% inhibition at 1 mM
-
72.5% residual activity at 1 mM
-
weak inhibitor
-
inhibits NahF activity by 50%; inhibits NahV activity by 57%
-
0.1 mM, 26% residual activity
-
slight, in presence of K+
-
1 mM, 32% inhibition
-
18.5% inhibition at 1 mM
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
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110 mM
-
10 mM, complete inhibition
-
36.45% residual activity at 12.5 mM
-
95.9% residual activity at 5 mM
-
above 20 mM
-
5 mM, 15% loss of activity
-
400 mM, 72% inhibition, slight activation at 50 mM
-
1 mM LiCl, 30% inhibition
-
81.40% residual activity at 5 mM
-
strong, dilution, Co2+ or Zn2+ protects, not Ca2+, Mg2+ or Mn2+
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weak
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at high concentrations
-
antagonizes stimulation by K+
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polymerase alpha
-
in presence of K+
-
inhibits at 0.5-5 mM
-
3.07% residual activity at 20 mM
-
24.7% residual activity at 1 mM
-
1 mM, 30% inhibition
-
inhibitory at 5 mM
-
65.8% residual activity at 10 mM
-
1 mM, slight inhibition
-
slight inhibition
-
inhibits isozyme alpha from leaf
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0.1 mM to 10 mM, the lithium inhibition profile is uncompetitive type
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5 mM, 37% loss of activity
-
slight inhibition at 1-5 mM
-
9% inhibition at 10 mM
-
10 mM, slight inhibition
-
40% inhibition
-
88% inhibition at 20 mM
-
12% residual activity at 20 mM
-
10 mM, 8% loss of activity
-
high concentration, 300 mM Li+, pH dependent inhibition, complete at pH 8
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relative activity 75.5%
-
slight inhibition at 1 mM
-
the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
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73.0% residual activity at 0.1 mM
-
10 mM, 19% inhibition
-
1 mM, 89% of initial activity
-
inhibits at 1 mM
-
10 mM, 17% residual activity
-
complete inhibition at 0.2 mM
-
0.01 mM, 51% inhibition
-
11% inhibition at 5 mM
-
0.01 mM 30% inhibition
-
inactivates subunit B
-
50 mM, 68% residual activity
-
10 mM, 40% inhibition
-
1 mM, 65% of initial activity
-
26-29% reduced activity at 1 mM
-
5% activation at 1 mM, 62% inhibition at 5 mM
-
1 mM, 65% of initial activity
-
about 90% residual activity at 1 mM
-
complete inhibition at 5 mM
-
slight inhibition at 3 mM
-
6 mM, 72% inhibition
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0.6 M, 50% inhibition of ATP-diphosphate exchange, 0.11 M, 50% inhibition of aminoacylation
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0.7 M, 50% inhibition of ATP-diphosphate exchange
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-
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inhibits the activity of the wild-type enzyme at 1 mM
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competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview
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indirect inhibition
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Metals and Ions (229 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
Ca2+, Li+, Mg2+, Mn2+ and NH4+ at 10 mM decrease activity by 10-50%
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1 mM, slight activation
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activates to 127% activity compared to the control activity at 1 mM and to 178% at 100 mM
-
activates to 127% activity compared to the control activity at 1 mM and to 178% at 100 mM
-
activates slightly at 1 mM
-
activates
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the enzyme activity is increased 13.8% over the control by 1 mM Li+
-
activating effect
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required for activity
-
benzaldehyde dehydrogenase I
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119% activity at 20 mM
-
monovalent cation required. K+ , Rb+ , Na+, Li+, NH4+ and Cs+ activate in this order
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500 mM, 107% of the activity compared to activity without metal ions
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stimulate
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stimulates activity
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activation of mutant type enzyme at 0.2 mM, decrease of wild type enzyme activity above 0.1 mM
-
monovalent cations stimulate in the order K+ less than Cs+ less than Na+ less than NH4+ less than Li+
-
not clear whether this reflects a general salt effect or a Li+ specific effect
-
slight stimulation
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
-
50 mM, weak stimulation
-
about 118% activity at 10 mM
-
below 20 mM, slight activation, concentrations higher than 20 mM abolish activation by K+ and Rb+
-
2 mM or 20 mM Li+ induces slightly enhanced activity
-
activates by 15.8% at 2 mM
-
11% of the activation with Mn2+
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activates
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monovalent cation required, K+, Li+ or NH4+ markedly stimulate
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less effective than Na+ in meeting the monovalent ion requirement
-
123.1% activity at 100 mM
-
slight stimulation
-
1 mM, 5-10% stimulation
-
supports activity to a small degree
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absolute requirement for both monovalent and divalent cations, when Mg2+ fills the requirement for divalent cation, K+ and Rb+ are the most active monovalent cations, NH4+, Na+, Cs+ and Li+ are decreasingly active
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stimulates
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results in 34.5% activity compard to Mg2+
-
poor activator which seems to modify the enzymatic mechanism from a random to an ordered sequential pattern with ATP bound before pyridoxal. Km: 37 mM
-
the enzyme is slightly activated by Li+ +(65.87% relative activity at 10 mM)
partial activity
-
activity reduced about 20% in 50 mM LiCl
-
activation at 0.2 M LiCl, inhibitions at higher concentrations, only with acetoacetate or acetoacetyl-CoA as substrate
-
14% activation at 1 mM
-
112.8% activity at 2 mM
-
addition of 50 mM increases the initial activity by 10-20%
-
115.4% activity at 1 mM
-
can substitute for K+ to a small extend
-
activation
-
less effective in activation than K+
-
0.05-0.2 M, 20% activation in presence of 10 mM Mg2+
activates
-
slight activation at 1 mM
-
activates
-
inhibits activity
-
slightly enhances activity
-
about 166.5% activity at 1 mM
-
5 mM, 1.2fold increase in activity
-
1 mM LiCl2, activates
-
about 110% activity at 1 mM
-
105% activity at 2 mM
-
110% activity at 1 mM
-
5 mM, 132% of initial activity
-
102.6-128.4% activity at 2.5 mM
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activates the acid trehalase
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10 mM, 147% of initial activity
-
stimulation at 25 mM
-
low concentration: activation
-
activates 20% at 1 mM
-
109% activity at 5 mM
-
activates
-
115% activity at 1 mM
-
1 mM, 35% activation
-
103.25% activity at 1 mM
-
1 mM, 112% of initial activity
-
82% of control activity at 2 mM
-
about 118% activity at 5 mM
-
moderate activation
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maximal activation near 0.2 M LiCl with Micrococcus luteus cell walls as substrate, sharp optimal activation at 0.1 M with Bacillus subtilis cell walls as substrate
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activates, alters the enzyme kinetics
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0.4 M activates the activity by 45%
-
activates slightly
-
0.06 mM, activation to 111% of control
-
Na+, K+, Li+, Rb+ or Ca2+ required for activation
-
binds to complement component C2A
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activates, can partially substitute for Na+, binding to Asp189
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activates, preference of monovalent cations in descending order: Na+, K+, Li+
-
activates 20% at 10 mM
-
5% activation at 1 mM
-
rapid and reversible activation
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activates
-
activating at 1 mM to 133%, slightly inhibitory at 5 mM
-
Li+ can substitute for Na+ as activator. In the presence of K+, Li+ iss a less potent activator than Na+
-
weak activator
-
0.8 M KCl optimal, can be replaced by NaCl, CsCl, RbCl, NH4Cl, LiCl
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activation, no significant influence on the rate-limiting step. Km value 0.219 mM
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activates to a lesser extent than K+
activates
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has an effect on the conformational equilibrium
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stimulates
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slight activation
-
0.2 M, 1880% of initial activity
-
10 mM, 192% of initial activity
-
1 mM, enhances activity 4.4fold
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activates
-
partially stabilizes the enzyme during storage, but less effective than Mn2+
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5fold activation of R69D mutant, slight activation of wild-type PI-PLC
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enzyme activity is 43.7 U/mg protein at a metal concentration of 1 mM
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activity of enzyme towards UDP-xylose is 18.1 U/mg protein at a metal concentration of 1 mM
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1 mM, activates to 106% of control
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1 mM, slightly enhances the activity (6.7%)
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1 mM, 74% of K+ activation
-
slightly stimulates in presence of Mg2+
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activation at 5-8 mM, absolute requirement for certain monovalent cations, inhibition above 10 mM
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0.4 M, required
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can replace K+
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specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
-
relative activation by monovalent cations in decreasing order: K+/ NH4+, Na+, Li+
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the Na,K pump is activated by the combined effect of Na+ on the cytoplasmic side and of K+ on the extracellular side of the membrane. K+ can be replaced by the following monovalent cations in the order of decreasing activation: K+, Rb+, NH4+, Cs+, Li, Na+
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Km: 25 mM
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activates, Km: 100 mM
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3D Structure of Enzyme-Ligand-Complex (PDB) (166 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (5 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (8 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.06
-
wild type enzyme, pH and temperature not specified in the publication

Ki Value (9 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.14
-
pH 7.7, 30°C
6000
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ATP-diphosphate exchange

IC50 Value (16 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
5.5
-
pH 8.4, 22°C
0.2
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30°C, pH 7.5, 2 mM Mg2+, 0.2 mM adenosine 3',5'-bisphosphate as substrate

References & Links

Links to other databases for Li+

ChEBI
PubChem
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PubChem