Ligand potassium chloride

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Basic Ligand Information

Molecular Structure
Picture of potassium chloride (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
HClK
potassium chloride
WCUXLLCKKVVCTQ-UHFFFAOYSA-M
Synonyms:
KCl

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (7 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
styrene + KCl + H2O2 = 2-chloro-1-phenylethan-1-ol + 2 H2O
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (86 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
increase in activity about 2fold
-
an optimum concentration of about 150 mM KCl produces a more than 400% increase in activity compared with an absence of KCl; the optimum concentration of about 150 mM KCl produces more than 400% increase in activity
-
5-6fold increasing activity for NADPH-dependent activity at 0.2 M
-
80 mM, 9fold increase in hydroxypyruvate reductase activity
-
0.8 M activate F420-linked activity more than 10fold, slight inhibition of methyl viologen linked activity
-
2 M, more than 2fold stimulation
-
activation
-
or NaCl, required. Optimum concentration 100 mM
-
strong activation at 50 mM
-
adding 5 mM NAD+ in 0.2 M KCl improves the FDH elution and increases the specific FDH activity by 1.38fold as compared to elution with 1 M KCl
-
or NaCl, maximum activity at 0.25 M
-
maximum activity at 0.5 M
-
3.5fold activation at 200 mM
-
can repace for NaCl
-
activates at 5°C and 37°C
-
4°C: activates the enzyme at concentrations below 1 M
-
enzyme prefers high ionic strength, activation
-
110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration
-
maximal activity at 4.5 M
-
at 0.6 M stimulation
-
stimulates ATP-PRT activity in crude extracts, adding KCl to a final concentration of 0.13 M in reaction mixture increases the reaction rate by about 40%
-
below 50 mM
-
weak stimulation
-
50-100 mM, about 80% increase in activity; 50-100 mM, about 80% increase in activity
-
activation
-
in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis
-
major poly(A) polymerase, optimal at 250 mM, minor poly(A) polymerase, optimal at 125 mM, inhibition of both above 250 mM
-
activates
-
2fold activation
-
highest activity in 1 M KCl
-
stimulates at 20 mM
-
maximal enzyme activity at 0-20 mM
-
slightly increases activity by 20%
-
below 50 mM
-
136.2% activity at 400 mM
-
in organ culture
-
highest catalytic activity in presence of 25 mM KCl
-
17% activation at 300 mM
-
stimulation, optimal at 50 mM
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
-
1 mM, 116% of initial activity
-
preflagellin peptidase activity is optimal in the presence of 0.4 M KCl with 0.25% (v/v) Triton X-100
-
2fold increase within 0-0.5 M, beyond 0.5 M smaller extend of increase
-
higher activity in buffers containing 50 mM
-
150-300 mM
-
activates
-
1 mM, 1.4fold activation
-
ionic strength, and not the salt identity, is important for PI-PLC activation towards phosphatidylinositol in micelles. Added salt has a synergistic effect with zwitterionic phospholipids, leading to high specific activities for phosphatidylinositol cleavage with only moderate dilution of the anionic substrate in the interface. This kinetic activation correlates with weakening of strong PI-PLC hydrophobic interactions with the interface. PI-PLC cleavage of phosphatidylinositol presented in small unilamellar vesicles is activated by salt
-
200 mM, twofold stimualtion
-
3.5fold increase at 50 mM
-

Inhibitor in Enzyme-catalyzed Reactions (409 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
at 40°C, half-life in 0.5 M KCl is 86 h for wild-type, and 114 h for mutant D172K/D216K/D344K, 95 h for mutant D172K, 117 h for mutant D216K, 114 h for mutant D344K. At 25°C, half-life in 0.5 M KCl is 506 h for wild-type, and 613 h for mutant D172K/D216K/D344K, 630 h for mutant D172K, 660 h for mutant D216K, 537 h for mutant D344K
-
half Vmax/Km at less than 0.1 M due to general ionic strength effect
-
0.1 M, inactivation
-
inhibition above 100 mM
-
17% inhibition at 1 mM
-
80-100 mM, 50% inhibition
-
1 M, 44% inhibition
-
inactivation
-
oxidized truncated enzyme
-
100 mM, 47% inhibition
-
10 mM, 21% inhibition
-
50% inhibition at 20 mM
-
over 80% inhibition at 500 mM
-
50 mM, 50% inhibition
-
high salt concentration inhibits, 0.05 M: 40%, 0.1 M: 50%, 0.2 M: 70%
-
higher salt concentration (500 mM KCl) results in sixfold lower activity suggesting that the interaction of the protein components is affected by high salt concentration
-
high concentration
-
200 mM, 39% loss of activity. 500 mM, 69% loss of activity
-
total inactivation
-
sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above
-
1 mM causes 5% inhibition at 30°C
-
14% inhibition at 1 mM concentration
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
-
10–20% inhibition is observed with 50 mM KCl, while with higher concentrations (maximum, 0.6 M), 46–65% activation is reached, and further increased concentrations of KCl are inhibitory, enzyme Ape1473/1472
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited
-
increase in Km-value for D-xylose and NADP+
-
70% inhibition at 1 M
-
50 mM, 40% inhibition
-
32% inhibition at 100 mM
-
3 M, 75% inhibition
-
0.5 M, specific activity 133 U/mg
-
80% inhibition at 75 mM
-
100 mM, 88% inhibition of dimeric and tetrameric enzyme
-
about 30% residual activity at 250 mM KCl
-
inhibition of glycine-CO2 exchange reaction
-
200 mM, 33% inhibition
-
recombinant enzyme, concentration above 0.1 M
-
reactivation by washing
-
inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
-
slight inhibition
-
0.5 M
-
500 mM, inhibits purified enzyme
-
activates, optimally at 50 mM, 80% inhibition at 500 mM
-
400 mM KCl, pH 8.2, 20% inhibition
-
80 mM, 50% loss of activity, 200 mM, 90% loss of activity
-
30.81% inhibition of transferase activity at 100 mM; 33.33% inhibition of transferase activity at 100 mM; 35.13% inhibition of transferase activity at 100 mM
-
40% residual activity at 10 mM
-
reversible
-
28% residual activity at 100 mM
-
above 0.4 M
-
IC50: 0.33 M for homodimeric enzyme, IC50: 0.18 M for heterodimeric enzyme
-
50% inhibition at 100 mM
-
0.4 M, more than 90% inhibition
-
1.3 M
-
80 mM, 50% inhibition
-
500 mM, 16% inhibition
-
weak
-
200 mM KCl decreases the polyphosphate-dependent activity to 75%
-
40 mM, 50-60% decrease in activity of recombinant enzyme
-
above 10 mM
-
slight inhibition
-
at 10 mM
-
complete inhibition in the forward reaction, slightly inhibitory in the reverse reaction
-
high concentrations
-
activity linearly decreases from 100% (at 0 mM added KCl) to 71% at 500 mM added KCl
-
0.5 M, 10% inhibition
-
activation at 0.4 M, inhibition at higher concentration
-
in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis
-
stimulation at low concentrations, at 300 mM, 15% inhibition, major poly(A) polymerase, 52% inhibition, minor poly(A) polymerase
-
inhibits GlgC/GlgD complex, no effect on subunit GlgC alone
-
enzyme works optimally at 50 mM KCl, inhibition at 200 mM
-
above 10 mM
-
25 mM, slight decrease in activity
-
125 mM, about 50% of maximal activity
-
KCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
-
50 mM, 60% inhibition of isoenzyme A, slight activation of isoenzyme B
-
activates below 0.1 M, inhibits at higher concentrations
-
500 mM
-
2 M, inactivation of the soluble enzyme, no inactivation of the membrane-bound enzyme
-
100 mM, 75% inhibition
-
FEN-1 retains up to approximately 70.0% of its endonuclease at 0-50.0 mM, between 75 and 100 mM FEN-1 displays a significant reduction in activity and at the highest salt concentrations between 125-200 mM almost a complete ablation of activity occurres
-
above 15 mM
-
above 25 mM
-
above 100 mM, strong inhibition
-
above 300 mM
-
reduces activity 10fold at a concentration of 200 mM
-
Py-Py correndonuclease II loses 75% of activity in presence of 100 mM
-
total inhibition at chloride ion concentration of 600 mM
-
at high concentrations
-
moderate salt concentrations
-
50% inhibition at 2 mM
-
weak inhibition up to 200 mM
-
at 10 mM
-
slight
-
60 mM, the activity increases 1.3-fold, 100 mM KCl result in significant inhibition of activity
-
40% inhibition by 1 M
-
1 mM, 91% activity compared to control without any metal ion
-
50 mM: 50% inhibition
-
1 mM, 22% inhibition
-
10-30% decrease in activity
-
2.0 M, 41.3% inhibition; 2.0 M, 74.6% inhibition, alpha-galactosidase 3; 2.0 M, 8.8% inhibition, alpha-galactosidase 1
-
70% residual activity at 0.5 mM
-
with 1 mM 80% of activity remains, with 2 mM 50% of activity remains
-
25% of enzyme inhibition at 0.5 mM, at 37ºC, pH 6.5
-
50% inhibition at 0.1 M
-
slight inhibition
-
2fold inhibited
-
20 mM, 79% residual activity
-
with ATP-Mg acetate
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
-
92% inhibition at 0.2 M
-
weak, above 0.2 M
-
0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity
-
minimal activity at 0.5-0.8 M, depending on substrate concentration. Minimal activity is 50-70% of the acitivity in absence of salt, with increase in KM-value and decrease in kcat-value. Slight reactivation above 0.8 M
-
100 mM
-
25.9% inhibition at 5 mM
-
at a concentration of 200 mM
-
concentrations of KCl higher than 20 mM weaken slightly the hydrolytic ability of VIM-12
-
high salt concentrations (above 100 mM KCl) inhibit the reaction
-
0.2 M, complete inhibition
-
abover 150 mM
-
slight inhibition at high concentrations
-
0.4 mM, 29% loss of activity
-
200 mM, 63% inhibition
-
5.8% inhibition at 5 mM; 94.2% remaining activity at 5 mM
-
50% inhibition at 1.5 M
-
0.05-1.0 M, 60% inhibition at 0.25 M, 27% inhibition at 0.1 M
-
at pH 6.5
-
67 mM, slight
-
100 mM, 67% inhibition
-
decreases mDSD enzyme activity during purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside
-
high salt concentrations (NaCl, KCl, or MgCl2 at a concentration of 220 mM) inhibit the enzyme activity completely
-
1 mM, 11% inhibition
-
weak inhibition at 1 mM
-
400 mM, 32% inhibition
-
stimulates up to maximum concentration of 80 mM, inhibition at higher concentration
-
150 mM
-
1 M, 35% inactivation, 2 M, 55% inactivation
-
10 mM, 11% loss of activity
-
0.5 mM, about 25% inhibition
-
above 10 mM
-
0.125 M
-
stimulates, maximal effect at 0.1 M, inhibition at higher concentrations
-
above 300 mM, inhibits activity of recombinant AtUGlcAE1DELTA1-64
-
0.2 M
-
the complex of Pus1 with tRNA is sensitive to high ionic strength. The optimal concentration of KCl for Pus1 binding is 100 mM. Above 400 mM KCl, no complex is detected
-
50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M)
-
inhibits enzyme forms PC-1 and PC-2, PC-3 is stimulated (optimal concentration 75 mM)
-
inhibits acylation of yeast tRNA, little effect on acylation of homologous tRNAGly
-
the enzyme loses half of its activity at KCl concentrations below 2 M
-
-
-
approx. 50% inhibition at 500 mM
-
in the presence of 0.1 M or 0.2 M KCl, activities are 40% and 15% relative to reactions without KCl
-
inhibition above 100 mM
-
5-10 mM, strong inhibitory effect on the glutamylation reaction. 80 mM, 90% inhibition
-
75 mM
-
activates at lower concentrations, inhibits at higher concentrations
-
1.2fold stimulation in presence of 20 mM KCl. Inhibition at concentrations higher than 50 mM
-
inhibition by KCl occurs at greater than 30 mM (NH4)2SO
-
no ATPase activity above 300 mM
-

Metals and Ions (380 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
-
activation
-
maximal activity at 1.5 M
-
optimal activity is observed in the presence of 500 mM NaCl or KCl
-
highest activity at about 1 M KCl
-
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
-
highest activity at about 3 M KCl
-
activates at 2 mM
-
the activity of the enzyme is markedly dependent on the concentration of NaCl or KC1 in the Tris/EDTA/Mg2+ buffer, being maximal in 0.5 M NaCl or KCl. The stimulatory effect of KCl is greater than that of NaCl
-
activates the enzyme at high concentrations
-
NAD+, NADH, NADP+, NADPH, AMP, ADP, ATP, dipicolinic acid, (NH4)2SO4, Na2SO4, NaCl and KCl reactivate partially purified enzyme inactivated by storage at 4°C, optimal reactivation at 30°C and pH 7.0, enzyme may be regulated by monomer-dimer interconversion
-
10 mM, activates to 127% of control
-
0.1-0.3 M, chloride salts become strongly inhibitory at higher concentrations, replacing K+ with Na+ or NH4+yields similar results
-
50 mM, 63% of the activity with Mn2+
-
slight activation
-
optimal salt concentration is 350-400 mM
-
100 mM, 5.8fold activation
-
activation
-
activity is optimal at 200 mM salt, with 1.5fold greater activity in KCl than in NaCl, and the enzyme displays reduced activity after the removal of salt by dialysis
-
5 mM, activation to 146% of control
-
increases activity, maximal activity at 250 mM
-
the enzyme requires the presence of salts, 50% of maximal activity is reached at 100 mM potassium phosphate, KCl or NaCl
-
optimal salt concentration is 2 M KCl or NaCl
-
stimulation, optimum at 0.5 M
-
13% activation at 0.1 mM, 20% activation at 10 mM
-
activation at high concentration
-
exhibits its highest activity in 2 mol/l KCl at 45°C
-
120 mM: 40fold increase of activity of ALDH5 with NAD+. 16 mM: 20fold increase of activity of enzyme ALDH5 with NADP+. No stimulation of the activity of enzyme form ALDH1
-
required for optimal activity
-
activity with KCl slightly higher than with NaCl
-
3 mM, activates to 144% of control
-
enzyme shows maximal activity in presence of more than 3 M salt
-
the rate of transfer of the first electron from methylamine-reduced MADH to amicyanin is increased by monovalent cations
-
highly activating, best monovalent cation, amino acid sequences of putative K+-binding sites of TbGMPR, overview
-
maximal enzymatic activity at 2 to 3 M KCl
-
IC50: 0.51 M
-
enzyme prefers high ionic strength, activation
-
slightly stimulated up to 0.2 M
-
TRM5 enzyme is stimulated 4fold by 100 mM KCl. TRM5 tends to lose all activity in 600 mM KCl
-
the optimal ionic strength for both enzymes requires 100 mM KCl, with DHFR displaying 2.5fold activation and TS 4.5fold activation
-
activation, 140-180 mM, cap I-methyltransferase
-
weak stimulation by low concentrations
-
maximal activity required KCl concentrations of greater than 3.5 M
-
slight activation at 0.25 M
-
2fold enzyme activity at 0.05 - 0.1 M
-
activates, optimally at 50 mM for the solubilized enzyme and at 70 mM for the membrane-bound enzyme, 80% inhibition at 500 mM; optimum activity at 50 mM
-
stimulates; stimulates enzyme activity 2.5-fold
-
optimal activity at 100 mM
-
about 8fold activation, maximum activation at 0.6-0.8 M
-
optimal concentration
-
100 mM, activity is increased 1.5fold
-
salt optimum: 3.0 M KCl
-
activation in presence of glucose 6-phosphate
-
upon an increase in the KCl concentration from 0 to 100 mM, the OtsA activity decreases by more than 40%, whereas it is not significantly affected when UDP or GDP-glucose is used as the substrate
-
0.3 M: stimulation
-
activates at 50 mM, slightly more effective than NaCl
-
or NaCl required for optimal activity
-
upon an increase in the KCl concentration from 0 to 100 mM, the OtsA activity decreases by more than 40%, whereas it is not significantly affected when UDP or GDP-glucose is used as the substrate
-
lower activity compared to NaCl, best at 50 mM
-
0.4 M activates
-
activates at 50 mM
-
removal of KCl from the reaction mixture results in a decrease of activity
-
optimal activity between 50 and 100 mM. 85% of maximal activity when the KCl concentration is 500 mM
-
required at 0.5 M for full enzyme activity
-
at 20 mM
-
at 20 mM
-
300 mM, 3.6fold increase of activity
-
the enzyme is maximally active in the presence of 1.2 M KCl. Activity in the presence of RbCl and CsCl is similar to that observed in the presence of KCl
-
stimulates, optimal concentration: 1.2 M
-
at 80 mM
-
activates
-
KCl-induced cell depolarization stimulates Dp71d phosphorylation
-
activates
-
maximal activation at 100 mM
-
concentration of 3 M required for activity
-
activation at 0.4 M, inhibition at higher concentration
-
activation, 25 mM, NAD+-synthesis, not deamido-NAD+-synthesis
-
stimulated by concentrations up to 50 mM
-
requires KCl concentration of about 0.4 M
-
0.02 M, 70% activation
-
0-0.5 M KCl gives optimal activities at around 55-60°C. When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
-
stimulates
-
activity 128%
-
activates below 0.1 M, inhibits at higher concentrations
-
the enzyme is dependent on the presence of KCl and shows highest activity at 4 M KCl
-
300 mM, 77fold activation; activates about 80fold, optimally at 300 mM
-
activates 12% at 1 mM
-
enhances activity
-
ExoVII activity is maximal at low salt concentrations (lower than 250 mM)
-
preferred concentration is 50 mM. Activity starts to decrease above 150 mM
-
activates
-
stimulating between 25 and 50 mM, inhibitory above 50 mM
-
the enzyme requires a low ionic strength; the enzyme requires high ionic strength, 200 mM KCl
-
optimal concentration in reaction buffer: 200 mM
-
optimum concentration 50 mM
-
at low salt concentrations less than 5 mM maximum of cleavage rate; at low salt concentrations of less than 5 mM the enzyme has its maximum cleavage rate
-
activates at chloride ion concentration up to 50 mM
-
in its absence activation by Mg2+ occurres at 2fold lower concentrations
-
0.1 M, stimulates
-
activates the 4-nitrophenyl phosphatase activity of the Na+/K+-ATPase only in presence of NaCl, gradually inhibits ATPase activity of the enzyme
-
activation
-
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
-
0.5 M, activates
-
required
-
in vitro: no direct decrease in GDPD5 activity, measuring choline by chemiluminescence, substrate sn-glycero-3-phosphocholine
-
stimulates
-
60 mM, the activity increases 1.3-fold, 100 mM KCl result in significant inhibition of activity
-
1 mM, 91% activity compared to control without any metal ion
-
can partially substitute for NaCl at higher concentrations
-
3 mM: stimulation, above 10 mM: inhibition
-
1 mM, 1.2fold activation
-
50 mM C-terminal truncated enzyme ApuADELTA: amylase activity: 106%, pullulanase activity: 93%; 50 mM full length enzyme: amylase activity: 112%, pullulanase activity: 99%
-
slightly activating at 1-2 mM
-
maximal activity in presence of 0.4 M NaCl. KCl is able to compensate for KCl
-
0.2-1 mM, 110% of initial activity
-
0.2-1 mM, 110% of initial activity
-
1 mM
-
the activity of the enzyme in 2.5 M and 4 M KCl relative to 4 M NaCl is 34% and 40%, respectively
-
5 mM, activation to 111%
-
activation to 110.4% at 5 mM
-
no activity in the presence of 0–0.3 M salt. The enzyme shows a salt requirement for activity, being active from 0.3 M NaCl, with maximal activity at 3.5 M NaCl. KCl supports similar activities as NaCl up to 3.5 M, and LiCl up to 2.5 M. The monovalent salts can not be substituted by 3.5 M divalent cations, CaCl2 or MgCl2
-
5 mM, 1.1fold activation
-
activity 4fold stimulated by 0.1 M KCl
-
slightly more stimulatory than NaCl
-
activates optimal at 25 mM, recombinant UDG
-
stimulates, optimal at 50 mM
-
the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl
-
addition of 0.5 M NaCl to the assay buffer does not significantly alter the activities of the wilde-type enzyme with 0.2 mM dansyl-Ala-Arg or the E260Q mutant enzyme but does substantially increase the activity of the E260A mutant, 219%. The enhancement of E260A is not specific for NaCl, as similar increases are detected with other salts such as NaNO3, 249%, KNO3, 256%, KCl, 256%, or Na2SO4, 297%
-
increases activity of recombinant S1P-1 25% dependent on the substrate used
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
-
increases enzymatic activity somewhat, while choline-Cl has a larger effect
-
strong activation
-
strong activation
-
the catalytic activity of YpA does not vary significantly as a function of ionic strength at 100-3000 mM KCl
-
1 M: 1.47fold activation
-
leads to dissociation of the dimer
-
1.0 mM, relative activity 116%
-
2.5 M, maximal 100fold stimulation; 2.5 M stimulates
-
the KCl optimum for A37–I37 conversion by Tad1p is 25 mM
-
brain enzyme, 15 mM: activation, substrate: Tris salt of acetyl phosphate
-
slight stimulation at 0.05-0.1 M, inhibition at 0.2 M
-
stimulates the ATPase activity in the absence of ssDNA as well as the strand-exchange activity in the presence of AMPPNP
-
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
-
activity is not strongly dependent on KCl over a 0 to 4 M range
-
activates
-
enzyme retains activity at salt concentrations ranging from low salt to at least 1.5 M NaCl or KCl for CO2 hydration, 2.0 M NaCl for esterase activity and 0.5 M for bicarbonate dehydration
-
facilitates mDQD enzyme purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside as a chaotropic agent
-
the enzyme is dependent on the presence of KCl and shows highest activity at 0.5 M KCl. With 82% of activity at 4 M KCl, whereas the activity dropps severely at 0.1 M KCl
-
optimal concentration is 100 mM, wild-type enzyme
-
relative activity: 521%
-
1 mM, 120% of initial activity
-
stimulates activity, relative activity: 109%
-
only weakly influences GDP conversion with the ag1 enzyme causing a 2fold activation at 100 mM KCl, but the monovalent cation has no effect with FDP as substrate
-
addition of increasing concentrations (higher than 10 mM) enhances the activity by 10fold
-
nonspecific requirement for a monovalent or bivalent cation. Half-maximal activity is produced with 22.5 mM KCl
-
modest (about 30%) activation at 0.05 M, strongly inhibition (more than 50%) at higher concentrations (0.5 M)
-
stimulates up to maximum concentration of 80 mM, inhibition at higher concentration
-
0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
-
enhances activity
-
enzyme is inactive in absence of KCl, stimulation at concentrations up to 0.35 M, at higher levels slight fall of activity
-
the complex of Pus1 with tRNA is sensitive to high ionic strength. The optimal concentration of KCl for Pus1 binding is 100 mM. Above 400 mM KCl, no complex is detected
-
50-500 mM, stimulates ATPase activity. ATPase activity decreases significantly at higher KCl concentrations (1-2 M)
-
maximal activity of wild-type enzyme at 150 mM, maximal activity of mutant enzyme N726D at 75-100 mM
-
50 mM, required for optimal activity
-
enzyme form PC-3 is stimulated, optimal concentration 75 mM, enzyme form PC-1 and enzyme form PC-2 are inhibited
-
required, optimal cocentration is 150 mM
-
optimal concentration: 50 mM
-
optimal concentration is 10 mM
-
optimal concentration is 45 mM in absence of KCl, 5 mM in presence of 160 mM KCl
-
optimum concentration: 50-100 mM
-
optimal activity at 1-1.5 M
-
0.4 M, 1.4fold enhancement of activity
-
optimal up to 50 mM
-
activates
-
activates
-
optimal concentration: 100 mM
-
optimum concentration: 5 mM
-
like ATP hydrolysis, ATP synthesis can be performed in 1.75 mol/l KCl instead of NaCl
-
ATPase activity increases with increasing salt concentration
-
100 mM, activates OpuA instantaneous and reversible
-

Enzyme Kinetic Parameters

Ki Value (10 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.62
-
competitive vs. L-dopa
0.1
-
pH 6.7, 85°C
18.04
-
-
0.1
-
-
0.35
-
25°C, pH 6.5
120
-
-

IC50 Value (13 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
20
-
catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
200
-
cofactor NADH, pH 7.8, 35°C
510
-
IC50: 0.51 M
50
-
about
250
-
-
200
-
IC50 200 mM
40
50
IC50: 40-50 mM
0.52
-
pH 7.5, 25°C
160
-
-

References & Links