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BRENDA support

Ligand K+

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Basic Ligand Information

Molecular Structure
Picture of K+ (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
K
K+
NPYPAHLBTDXSSS-UHFFFAOYSA-N
Synonyms:
K+in, K+out, K+[side 1], K+[side 2], potassium

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (24 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + K+[side 1] = ADP + phosphate + K+[side 2]
show the reaction diagram
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In Vivo Product in Enzyme-catalyzed Reactions (24 results)

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EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ATP + H2O + K+[side 1] = ADP + phosphate + K+[side 2]
show the reaction diagram
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Substrate in Enzyme-catalyzed Reactions (51 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Product in Enzyme-catalyzed Reactions (53 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (125 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates NADH production
1 mM, 106% of initial activity
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efficient coupling of decarboxylation and hydroxylation, stimulation
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125 mM KCl, 1.5 fold increase in activity
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slight activation
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K+-activated type II enzyme: binding of K+ is required to enhance activity through induced conformational change
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allosteric activator of PARN and its truncated forms, optimal concentration is around 100 mM, with the increase of the K+ concentration, the enzyme reaches its Vmax at a much lower substrate concentration
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1 mM, activation to 193 % of control
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5 mM, 116% of initial activity
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50 mM, 112% of initial activtiy
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5 mM, 113% of initial activity
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slight activation
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mechanism of activation
activates, 100-250 mM
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enhances the phosphorylation of enzyme during hydrolysis
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stimulates activity
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extracellular

Inhibitor in Enzyme-catalyzed Reactions (1184 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, 70.3% residual activity; 1 mM, 82.3% residual activity
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slight inhibitory effect at 5 mM
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absolute requirement, inhibitory above 0.4 M
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about 92.11% residual activity at 1 mM
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weak inhibition at 2.5 mM
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about 30% inhibition at 1 mM, about 20% inhibition at 10 mM
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73.6% residual activity at 5 mM
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reduction of dihydroxyacetone
slight inhibition
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97% residual activity at 1 mM
38% residual activity at 50 mM
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10 mM, 6% inhibition
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16.7% residual activity at 1 mM
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about 90 % residual activity at 10 mM
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strong inhibition at 50 mM
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95.3% residual activity at 1 mM
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above 1 M
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K+, NH4+, and Rb+ at 0.2 M activate up to 20fold. Inhibitory at higher concentrations
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about 70% residual activity at 5 mM
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94% residual activity at 1 mM
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potassium ion in phosphate buffer may be inhibitory
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2 mM, 17% loss of activity
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200 mM, 50% inhibition at pH 7.9, 300 mM, 40% inhibition at pH 5.5, 95% at pH 8.5
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5 mM, weak inhibition
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inhibitory in presence of Mg2+
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Dnmt3b
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72% inhibition at 200 mM
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0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
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slight inhibition
at increased concentrations
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1 mM, 41% inhibition
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at high concentrations, stimulation at lower concentrations
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91.7% residual activity at 0.1 mM
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10 mM, 14% inhibition
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weak
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1 mM, 14% inhibition of hydrolysis reaction, transfer reaction to 435% of initial value, respectively
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slight inhibition at 0.1 M
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500 mM, 63% inhibition in the presence of MgCl2
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inhibitory at 50-400 mM
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at high concentrations
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weak
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inhibition by increasing concentrations
300 mM, activates at 30 mM
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1 mM
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weak, only at high concentrations
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complete inhibition at 4 mM K+
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200 mM, 50% inhibition
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complete inhibition at 10 mM
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about 70% residual activity at 10 mM
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73% residual activity at 100 mM
1 mM, 88% of initial activity
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1 mM, 55.8% residual activity
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AChEA and AChEB lose 80% actiivty at 1 mM of K+
1 mM, 42% residual acivity
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slight inhibition at 5 mM of intracellular enzyme
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no inhibition at 50 mM, 50% inhibition at 200 mM
above 100 mM, significant inhibition
90% residual activity at 4 mM
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at high concentrations
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1.0 mM, 18% inhibition of isoenzyme PI, slight activation (1.1fold) of isoenzyme PII
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80.2% residual activity at 1 mM
slight inhibition
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84.6% residual activity at 10 mg/ml
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1 mM, 1% loss of activity
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10% residual activity at 1 mM
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about 77% residual activity at 5 mM
10 mM, 5% loss of activity
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slight inhibition at 5 mM
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78% residual activity at 10 mM
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94.9% residual activity at 100 mM
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90.66% residual activity at 5 mM
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97.26% residual activity at 5 mM
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the inhibition exerted by the cations varies according to the following order: K+, Na+, Li+, Ba2+, Ca2+, Mg2+
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FtmPT1 shows 86.5% relative activity at 5 mM K+
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17.7% inhibition at 1 mM; 82.3% residual activity in the presence of 1 mM
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activating up to 0.1, inhibitory above
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1 mM, 4% inhibition
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linear competitive
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36% inhibition at 1 mM, 53% inhibition at 4 mM
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1 mM, 79% of initial activity
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inhibits hK6 at pH 7.5 or 9.0
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inhibited by 100 mM
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inhibits 19% at 5 mM
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97.4% residual activity at 10 mM
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85% residual activity at 10 mM
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about 56% residual activity at 10 mM
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0.01 mM, 24% inhibition
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significant inactivation by 100 mM
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2 mM, specific activity 0.56, relative activity 84%
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