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

BRENDA support

Ligand sodium chloride

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 sodium chloride (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
HClNa
sodium chloride
FAPWRFPIFSIZLT-UHFFFAOYSA-M
 Download
Synonyms:
NaCl, Salt

Roles as Enzyme Ligand

Product in Enzyme-catalyzed Reactions (1 result)

top print hide
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
3-chloro-D-alanine + NaHS = D-cysteine + NaCl
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (279 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
triple mutant D172K/D216K/D344K shows its maximum activity in a buffer with 0.50-0.75 M NaCl while the wild type protein has its maximum activity with 1.5 M NaCl
-
activation at 1-1.3 M, optimal pH shifts to 9-9.5
-
stimulates prostaglandin D2 11-ketoreductase activity
-
activation up to 0.1 M
-
increased concentration
-
5-6fold increasing activity for NADPH-dependent activity at 0.2 M
-
isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
-
maximum activity at 1.5 M, strong stimulation
-
The presence of 1 M NaCl results in a significant increase in activity in the wild-type strain.
-
80 mM, 8fold increase in hydroxypyruvate reductase activity, reaction rate increases with an increase in NaCl concentration up to 200 mM, but diminishes if the salt concentration is greater
-
gradually activates the enzyme with increasing concentrations of 0.1-1.0 M
-
PGDH activity increase about 1.5-2.3fold upon the increase of salinity from 0.5 to 2.5 M NaCl
-
up to 8%
-
20 mM, 1.4fold increase in activity
-
highest activity for catalase at 2 M, for peroxidase at 1 M
-
maximal activity in the presence of 200 mM NaCl
-
up to 0.5 M, activation of methyl or benzyl viologen mediated hydrogen oxidation
-
activation
-
maximum activity at 1.0-1.5 M, a high NaCl concentration enhances luciferase stability to thermal denaturation
-
or KCl, required. Optimum concentration 100 mM
-
isoform K09H is activated by NaCl, reaching its maximum activity at 2.0 M NaCl, an 1.8fold increase relative to its activity in the absence of NaCl
-
nearly 2fold activation at 100 mM
-
or KCl, maximum activity at 0.25 M
-
enzyme shows partial substrate inhibition, inhibition is alleviated completely by a 1M NaCl resulting in increased enzyme activity at high substrate concentrations
-
required for full activity, about 10fold activation at 150 mM
-
optimal oionic strength 0.62 mM
-
maximum activity at a ionic strength of 60 mM, independent of salt type
-
high NaCl induces the formation of reactive oxygen species, which in turn induces the synthesis of the alpha-subunit of GDH
-
2 h in 3 M NaCl at 60 °C, the residual activity is 1.8fold higher than that of the control without NaCl
-
activates at 37°C only
-
highest enzyme activity is obtained by incubation with 1.6 M NaCl, which is approximately 1.5fold higher than that of the untreated enzyme
-
in comparison to cultivar Jinchun no. 2, cultivar Changchun mici shows an increase in diamine oxidase activity as well as free spermidine and spermine, soluble conjugated and insoluble bound putrescine, spermidine and spermine contents in the roots during exposure to salinity (50 mM NaCl).
-
a significant increase in the P5C reductase activity is observed with increasing severity of NaCl stress (0-200 mM)
-
salt stress results in activiation of plasma membrane NAD(P)H oxidase. NaCl-induced increase in total Ca2+ is partially abolished by the addition of NAD(P)H oxidase inhibitor diphenyleneiodinium
-
the enzyme exhibits the highest activity (136.4%) at 1.0M NaCl
-
4°C: activates the enzyme at concentrations below 1 M
-
enzyme prefers high ionic strength, activation
-
APR activity of all three isoforms increases 3fold in roots after 5 h of treatment with 150 mM NaCl
-
activation, 0.4 M
-
30 mM, 1730% activation
-
increased expression in media containing 5% NaCl
-
required for maximal activity
-
maximal activity at 4.5 M
-
700 mM, 15fold activation
-
100 mM, 105% increase in activity
-
concentration of 0.5 - 1 M NaCl
-
stimulation
-
enzyme shows its maximum hydrolysis activity in a buffer with 1.5 M NaCl and retains up to 65% of its activity at 0.5 M NaCl
-
stress treatment induces higher levels of OGT protein expression
-
weak stimulation
-
ManNAc kinase activity is increased by presence of 200 mM
-
at 0.2-0.4 M, stimulation of 2’-deoxycytidine and 2-chlorodeoxyadenosine phosphorylation, but inhibition of 2’-deoxyguanosine phosphorylation
-
100 mM, increase in activity to 150% of control, inhibitory above 150 mM
-
activation at concentration up to 0.1 M
-
leads to a greater activation of the cDNA-expressed DHEA ST when assayed with dehydroepiandrosterone
-
2fold activation
-
activity of liver EST transiently expressed in COS-1 cells increases 86% in presence of 150 mM
-
activity is increased at least 4fold by salinization with 40% v/v artificial sea water
-
at high salinity levels, the enzyme activity increases; the highest activity is detected at 5 M NaCl
-
addition of NaCl increases the reaction rate with EnzChek lipase substrate dramatically with the highest rate, 46% higher than that without salt, occurring at 0.15 M
-
82% stimulation up to 70 mM
-
ATP molecules hydrolyzed per base pair unwound slightly increased
-
optimum activity at around 50 mM NaCl
-
350% activity at 20 mM
-
small increase of activity at 50 mM NaCl
-
optimal activity at 100 mM
-
maximum activity of SNR140 and SNR141 SNAse R N-terminal fragments which extends from residues 6 to 140 and 6 to 141 respectively, 0.3 M, studies performed to explore the mechanism of nascent peptide folding
-
salt treatment
-
the activities of isoforms Amy a, Amy c, and Amy h improved by about 47, 12, and 32%, respectively, after incubation in 3 M NaCl
-
160.5% activity at 4 M
-
0.1 M, required for optimal activity
-
maximum activity at 200 mM. The activity of the enzyme is strictly depended on the NaCl concentration
-
the optimum NaCl concentration for the enzyme is 250 mM
-
the enzyme is activated by high concentrations of NaCl (124% activity at 1 M)
-
highest activity in the presence of 200 mM NaCl
-
about 135% activity at 0.1 mM
-
40 mmol/l, 223.25% relative enzyme activity in midgut, 193.54% relative enzyme activity in salivary glands
-
40 mmol/l, 198.57% relative enzyme activity in midgut, 163.63% relative enzyme activity in salivary glands
-
123.47% relative activity at 50 mM
-
120% activity at 1 mM
-
small positive effect
-
the enzyme activity is significantly stimulated in the presence of 5-20% (w/v) NaCl (140% activity at 15% (w/v))
-
0.3 M
-
activation
-
the enzyme requires a physiological concentration of NaCl (150 mM) for optimal activity
-
highest activity at 20-100 mM
-
slight activation
-
enzymatic activity is markedly enhanced by high NaCl concentration, NaCl affects the P1 preference of OpdB synergistically in a substrate-dependent manner
-
300 mM NaCl stimulates enzyme activity
-
activation of rCPB2.8 and rCPB3 in acidic pH
-
1-2.5 M, up to 5fold increase in activity
-
assay at 3 M, no activity at salt concentrations of 0.2-0.4 M Na. In vitro dimerization of the protease domain is inducible at high salt concentrations. This effect might be caused by a hydrophobic dimerization interface, which under high ionic strength disfavors the monomeric state
-
activates at 2 M
-
up to 40fold increase in activity in presence of 4 M NaCl, substrate MOCAc-PLGL(Dpa)AR. Degree of activation depends on substrate
-
the optimum NaCl concentration for aggrecan degradation is between 12.5 and 50 mM
-
the highest lytic activity is observed in the presences of 250 mM NaCl
-
higher activity in buffers containing 150 mM
-
maximal activity at 20 mM, ionic strength affects activity below 10 mM
-
up to 3fold increase in activity at pH 5.4
-
highest activity with 1-1.4 mM
-
20% increase in activity at 1 M
-
maximum activity at 125 mM
-
best at 0.5 M
-
highest activity at 300 mM NaCl
-
the highest AP endonuclease activity is observed at NaCl concentrations of 100-150 mM
-
maximal activity at 200 mM, inhibition above
-
NaCl considerably enhances the reaction rate at pH 6.8
-
Rv1647 is slightly activated at 500 mM
-
all PLC1-6 are activated in salt/ethanol extractions
-
optimum activity at 100 mM NaCl
-
exposure to 150 mM NaCl for 48 h causes increased expression of MTSase
-
leaf L-myo-inositol 1-phosphate concentration increases 40fold during the first 6 h of salt stress (exposure to 300 mM NaCl)
-
low concentrations of NaCl (50 mM) stimulate the ATPase activity of the enzyme
-
highest activity at 200 mM
-
high saline conditions increase enzyme activity in root tonoplast
-
highest activity at about 400 mM NaCl
-

Inhibitor in Enzyme-catalyzed Reactions (943 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
half Vmax/Km at less than 0.1 M due to general ionic strength effect
-
activity is strictly salt dependent, with highest stimulation at 600 mM NaCl and 24% of maximum activity at 1.5 M
-
uncompetitive inhibition with respect to NADH, competitive inhibition with respect to indole-3-acetaldehyde
-
200 mM cause about 65% inhibition of the enzyme activity
-
VNG1048G loses much of its activity when salinity drops below 3 M NaCl
-
47% reduction by 100 mM
-
100 mM, 87% residual activity
-
2 M, 36% loss of activity
-
80-100 mM, 50% inhibition
-
50 mM, 25% inhibition
-
isoform ICD-2, increase in activity in up to 200 mM NaCl. Isoform ICD-1, no influence of NaCl. Above 200 mM, NaCl is inhibitory
-
almost no activity at 10% (w/v)
-
complete inhibition at 0.5 M
-
250 mM, 48% inhibition
-
100 mM, 47% inhibition
-
about 60% inhibition at 300 mM
-
slightly inhibits at concentrations higher than 8%
-
50% inhibition at a concentration of 4%
-
80% residual activity with 20% NaCl (3.42 M) and 83% relative activity with 12% NaCl (2.05 M) concentration
-
inhibitory (20-70% residual activity) between 5 and 300 mM
-
5 mM, 90% of initial activity
-
1 mM, 95.3% of the activity without metal ion
-
complete inhibition at 300 mM
-
44% inhibition at 1 mM
-
above 0.5 M, considerable inhibition of H2 evolution
-
increasing NaCl concentration gradually reduce activity. In 0.7 M NaCl quaternary structur changes to a dimeric arrangement and causes a 51% decrease in specific activity on catechol substrate
-
0.001 mM, 63% inhibition
-
half-maximal inhibition was at 600 mM
-
reduces the activity of the isozymes LH1, LH2a, LH2b, and LH3 with most of the synthetic nonpeptide substrates tested, in some cases the isozyme is activated or completely inhibited, overview
-
0.2 M, 50% loss of activity
-
0.1 M, 20fold increase in Km for NADPH
-
0.1 mM, 48% inhibition
-
10 mM, 36% inhibition. 100 mM, 89% inhibition
-
54% residual activity at 250 mM
-
a salt concentration of 162 mM results in half of the maximum inhibitory effect
-
above 100 mM
-
decrease in activity might be due to reduced enzyme solubility with increasing NaCl concentrations
-
enzyme activity is decreased by NaCl
-
sufficient NaCl inhibits enzyme activity significantly
-
70 mM, 50% inhibition
-
sharp decrease in activity in presence of up to 50 mM KCl, smaller increase in inhibition above
-
half-maximal inhibition at 100 mM
-
about 40% inhibition at 0.7 mM
-
about 50% residual activity at 0.5 M, complete inhibition at 2 M
-
at 2 M, 50% residual activity of enzyme expressed in Escherichia coli
-
the addition of 0.3 M NaCl causes a significant inhibition (up to 80%) of the activity
-
complete inhibition above 200 mM
-
IC50: 0.01 mM
-
0.2 M, 55% inhibition
-
purified recombinant VbANR almost loses its catalytic activity at 500 mM
-
about 50% residual activity in the presence of 1 M NaCl, about 30% residual activity in the presence of 2 M NaCl, about 10% residual activity in the presence of 4 M NaCl, about 3.5% residual activity in the presence of 6 M NaCl
-
60% inhibition at 1 M
-
inhibits recombinant wild-type enzyme and mutant V311M
-
NaCl does not inhibit PvRA activity up to 1 M, but inhibition is observed at 2.5 M. The activities of ALD and GxRA are significantly increased in the presence of NaCl at concentrations of 0.1-0.25 M
-
3 M, 89% inhibition
-
8 mM, 50% inhibition
-
0.5 M, specific activity 152 U/mg
-
80% inhibition at 75 mM
-
100 mM, 88% inhibition of dimeric and tetrameric enzyme
-
200 mM, approx. 50% inhibition, almost complete inhibition of the purified enzyme with 1 M NaCl
-
direct inhibition by NaCl is due to FAD dissociation
-
200 mM, 38% inhibition
-
up to 20% increase in activity up to 0.2 M, activity declines above and falls to zero at 0.8 M
-
the specific activity of DMGO decreased when cells are grown in the medium with high NaCl concentration. High osmolarity inhibits the activity of the enzyme, but not in the case of the medium with glycine betaine as the sole carbon source
-
reactivation by washing
-
slight
-
15 mM, 50% inhibition of activity with horse heart cytochrome, activity with pseudoazurin or cytochrome c550 is inhibited only above 100 mM
-
more than 80% inhibition above 200 mM, inhibition of nitrate reductase-ferredoxin complex formation at high ionic strength
-
below 5% remaining activity at 1 M
-
inhibition at concentration below 200 mM, original activity is recovered at 200 mM
-
sodium chloride strongly inhibits the activity of the human enzyme. Half maximal activity is seen at about 25 mM with a peptide substrate based on histone H2B and about 200 mM for the GST-GAR protein substrate
-
enzyme activity is abolished at NaCl concentrations above 125 mM
-
inhibits about 50% at concentration of 1.5 M
-
100% inhibition above 200 mM
-
reduces activity at 25 mM by about 30%
-
above 0.05 M
-
mutant trmC1: 100 mM, mutant trmC2: 200 mM
-
1 M, 97% inhibition
-
50 mM, 25% inhibition
-
200 mM NaCl inhibits the activity by about 22%
-
20% activity at 0.5 M
-
0.5 M
-
100 mM, 30% inhibition
-
above 150 mM
-
fetal rat liver enzyme
-
50% inhibition at 50 mM
-
above 200 mM
-
above 50 mM
-
slight
-
ubiquitination of substrate FAF1 is reduced by high-salt treatment
-
weak
-
10% of activity remaining above 0.2 M
-
slight inhibition at 0.1 M
-
40% inhibition at 300 mM
-
more than 0.2 M, decrease in enzyme acitivty; more than 50 mM, decrease in enzyme acitivty
-
0.2 mM: 50% inhibition of glucosyltransferase I, 0.25 mM: 50% inhibition of glucosyltransferase II
-
0.5 M, 86% inhibition of Chs1 and 29% inhibition of Chs2
-
concetration of 2-4 M NaCl
-
1 mM, 28% inhibition
-
1 M, about 50% inhibition
-
0.4 M, 40% inhibition
-
50% inhibition at 250 mM, complete inhibition at 500 mM and above
-
competitive with respect to phosphate
-
80% inhibition of starch transglycosylation activity at 0.5-4 M NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10-30%
-
slight activation up to 0.2 M, about 60% inhibition at 0.8 M, almost complete inhibition at 1.2 M
-
400 mM, 49% inhibition
-
complete inhibition at 300 mM
-
81.2% and 77.4% of its original total activity at NaCl concentrations of 3.5 M and 4.0 M, respectively
-
only the hydrolytic activity of the dextransuccrase is influenced by sodium ions, whereas there is no effect on glucosyltransferase activity. 0.5 mM, 65% inhibition of hydrolytic activity, 20 mM, 90% inhibition of hydrolytic activity. The enzyme shows biphasic effects in response to Na+ ions. The enzyme activity is restored by 86% after dialysis compared to the control enzyme preparation. No effect on in presence of other monovalent cations (Rb+, Cs+, and K+). The effects of sodium ions on dextransuccrase activity are specific, thus it can be useful to block its catalytic activity, and reducing the cariogenic potential of Streptococcus mutans
-
74% residual activity at 10 mM
-
25% residual activity at 100 mM
-
activity is reduced by about 50% in the presence of 150 mM NaCl compared with the activity without added NaCl
-
above 0.2 M
-
50% inhibition at 0.6 M
-
increasing concentrations in the presence of 5 mM Mg2+ result in inhibition
-
50% inhibition at 100 mM
-
1.3 M
-
200 mM, 25% residual activity
-
75 mM, 50% inhibition
-
activates slightly at up to 350 mM, inhibits by 50% at 1.25 M
-
more than 50% inhibition at above 200 mM
-
In ten-day-old seedlings grown on MS medium, AtIpk2b transcript level decreases in response to salt
-
200 mM NaCl decreases the polyphosphate-dependent activity to 75%
-
8.7-35 mM: slight activation, 70 mM: inactivation
-
50–500 mM, the enzymatic activity decreases approximately 40%–60%, respectively; 50–500 mM, the enzymatic activity decreases approximately 40%–60%, respectively
-
above 100 mM
-
250 mM, 50% inhibition
-
at 0.2-0.4 M, stimulation of 2’-deoxycytidine and 2-chlorodeoxyadenosine phosphorylation, but inhibition of 2’-deoxyguanosine phosphorylation
-
above 0.1 M
-
increased NaCl concentrations convert the active hexamer into an inactive tetramer. The action of NaCl appears to be confined to the Hik2 kinase domain
-
strong inhibition and destabilization at 2 M
-
0.1 M, 25% inhibition
-
activation at 0.2 M, inhibition at higher concentration
-
reverse reaction
-
inhibitory above 200 mM, 39% inhibition at 300 mM, 67% inhibition at 500 mM
-
inhibits GlgC/GlgD complex, no effect on subunit GlgC alone
-
IC50: 40-50 mM
-
slight inhibition
-
90% inhibition at 0.3 M
-
activity decreases with increasing concentrations of NaCl
-
0.1 M, 36% inhibition. 0.5 M, 91% inhibition
-
200 mM, about 50% of maximal activity
-
NaCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
-
inhibition at concentration above 0.1 M
-
activates below 0.1 M, inhibits at higher concentrations
-
kinetics, 24% inhibition at 10 mM
-
the enzyme retains approximately 90% activity at 3 M NaCl and 40% activity at 4 M NaCl
-
2 M, 80% residual activity
-
inhibits hydrolysis of triglycerides, e.g. triolein
-
150 mM, 15% inhibition
-
a salt concentration of 0.05 M inhibits 50% of the activity, salt optimum: 0.01 M
-
robust hydrolytic activity is observed in the presence of up to 250 mM NaCl with 7mer RNA as substrate. With substrate 5'-p-nitrophenyl-TMP, little effect on nuclease activity is observed even at 2 M NaCl
-
inhibition at 0.2 M ionic strength; inhibits at 150-200 mM
-
100 mM, 50% inhibition, fully reversible by dialysis or dilution
-
above 15 mM
-
0.05 M
-
above 50 mM
-
inhibitory above 0.6 M
-
inhibits substrate binding by the enzyme, in the samples that are pretreated with DTT, the addition of salt strongly inhibits the reaction and completely eliminates off-register cleavage
-
inhibition of the reconstituted mini-enzyme at 0.4 M NaCl
-
in vivo: The presence of 100 mM NaCl in the growth medium only marginally alters the cytosolic and chloroplastic enzyme activities of salt-tolerant varieties whereas both the activities decline appreciably in salt-sensitive varieties tested. in vitro: comparison of inhibition of chloroplastic enzyme in a salt-sensitive and a salt-tolerant enzyme, protection against inhibition in salt-sensitve rice by mannitol, inositol, pinitol, sorbitol, trehalose, sucrose and proline
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 83% remaining activity
-
0.1-0.3 M, 40-96% inhibition
-
1 M, shift in oligomeric state of the protein from dimer towards monomer
-
low resistance against increased salt concentrations
-
50 mM, inhibitory
-
0.1 M, 10% loss of activity, 0.5 M, 50% loss of activity
-
SBPase activity decreases at 100 mM NaCl and above
-
synergistic with ouabain
-
inhibits reactivation
-
100 mM, 37% inhibition
-
PyapApase shows higher activity below 100 mM NaCl, and more than 100 mM NaCl inhibits its activity. The enzyme activity at 50 mM NaCl is 5fold higher than that at 500 mM NaCl
-
enzyme PHY US573 is extremely salt-tolerant preserving 80% and 95% of activity in the presence of 20 g/l of NaCl and LiCl, respectively
-
inhibits phosphatidylinositol hydrolysis of low molecular weight PLC. Conversely, PIP2 hydrolysis is stimulated by increasing concentrations of NaCl
-
inhibition of binding to single or double stranded DNA
-
0.16 M 50% inhibition
-
at 10 mM
-
slight
-
slight inhibition at high concentrations
-
76% residual activity in the presence of 2 M NaCl, after 60 min at 70°C
-
50% inhibition by 500 mM
-
0.8 mM 62% inhibition
-
50 mM: 40% inhibition
-
0.3 M, complete inactivation
-
activates at 0.1 M, inhibitory at over 0.3 M
-
high salt, 1.0 M NaCl, inhibits enzyme activity by 50% compared with activity without any addition of effector
-
1 mM, 22% inhibition
-
increasing concentration up to 0.5 M gradually inhibits the enzyme activity to about 50%
-
activity remains relatively constant over the range 50-250 mM NaCl (pH 7.0), but decreases significantly below and above these concentrations
-
optimum activity in presence of 0.1-0.2 M, inhibitory above 0.2 M
-
the activity of both soluble beta-Gal and encapsulated beta-Gal decrease with salt addition. While in the case of soluble beta-Gal at 150 mM NaCl the reaction rate has decreased to half of the control value, in the case of encapsulated bet-Gal the same inhibition level is reached at 300 mM NaCl
-
0.1 M, partial, intracellular enzyme
-
strong inhibition at 10 mM, treatment of cells leads to accumulation of trehalose
-
between 0.075 and 0.25 M, the activity is decreased with increasing NaCl concentration. Above 0.25 M, the enzyme shows no activity. The activity of beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide is decreased with increasing NaCl concentrations, and 0.4 M NaCl produces 50% inhibition
-
loss of 70% activity at 4.5 N NaCl
-
30% inhibition of the tartaric acid-stimulated phlorizin hydrolase at 20 mM
-
5 mM, 79.17% relative activity
-
1.3 M
-
1 mM, inhibition to 104.48% of control, rTRE_P2
-
70% inhibited by addition of 0.1 M NaCl
-
inhibition with 200 mM
-
20 mM, 90% residual activity
-
96% cleavage activity at 200 mM, 13% cleavage activity at 400 mM
-
NaCl completely inhibits the thymine removal at 0.4 M
-
more than 18%
-
hydrolysis of Ala-4-nitropanilide, competitive inhibition at pH 6.6, inhibition is noncompetitive at pH 5.8, inhibition is mixed type at pH 6.2
-
1 M, 40% residual activity
-
about 30% of activity is retained in 20% (w/v) NaCl; about 30% of activity is retained in 20% (w/v) NaCl
-
retained maximum activity up to 50 mM NaCl, but further increase was accompanied with decreased enzyme activity
-
the enzyme activity is maximal in the absence of NaCl
-
1 mM, 78% loss of activity
-
continuous decrease in activity with increasing NaCl concentration, showing 95, 91, 85, 74, 68, and 63% residual activity at 5, 10, 15, 20, 25, and 30% of NaCl, respectively
-
1 mM, 80% inhibition of isoform -1S-SprE
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
-
1.0 M, 50% inhibition
-
above 200 mM
-
inhibits activation of prethrombin 2, no effect on reaction with meizothrombin
-
inhibits by 53.1% at 2.5 M
-
high concentrations inhibit the binding of beta2-glycoprotein I to tPA
-
600 mM
-
loss of almost 50 and 70% of its activity in the presence of 0.2 and 1.0 M NaCl, respectively. Presence of NaCl does not disrupt the dimeric structure
-
above 160 mM
-
at 100 and 250 mM, Gly-Asp-Asp-Asp-Asp-Lys-?-naphthylamide as substrate
-
maximum activity is observed in a basal minimal defined medium, whereas in the presence of NaCl 0.25%-1% (w, u) CEP activity is inhibited 1.4fold
-
activity is reduced by approximately 30% in the presence of 0.8 M NaCl
-
0.2-0.45 M: no effect. 0.1 M: 30-40% decrease in activity
-
0.1 M, 90% loss of activity
-
minimal activity at 0.5-1.2 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 1.2 M
-
12-21% inhibition, respectively
-
inhibition by displacement of viral DNA from complexes with enzyme
-
mu-calpain is more active at 165 mM NaCl than at 295 mM NaCl
-
m-calpain is more active at 165 mM NaCl than at 295 mM NaCl
-
500 mM reduces cleavage to 60%, 1 M reduces cleavage to 30%
-
80% of enzyme activity inhibited in the presence of 100 mM NaCl
-
1 M, 70% loss of activity
-
4% down-regulates the enzyme by more than 50% in the kidney and heart but not in the aorta
-
inhibition of rCPB2.8 and rCPB3 at pH higher than 5
-
30%, activity of pepsin A decreases by 60-65%
-
30%, activity of pepsin B decreases by 60-65%
-
optimal activity in absence of NaCl, 80% inhibition by 0.15 M NaCl
-
40% inhibition at 0.3 M
-
inhibits at 200-500 mM
-
binding to heparin and fibronectin can be disrupted by 0.3 M NaCl
-
50% reduction of activity at 0.3 M for protease I and 0.5 M for protease II
-
2 M, about 40% residual activity
-
100 mM
-
dramatic inhibitory effect on the activity of TACE
-
the activity is very low at or below 50 mM NaCl or above 500 mM NaCl
-
2fold lower kcat/Km, but required for stability
-
0.001 mM decreases enzyme activity by 25%
-
500 mM, 12% inhibition
-
27.7% inhibition at 5 mM
-
the enzyme is halotolerant, 16-19% activation at 1 M, but 13-14% inhibition at 2 M
-
slight inhibition
-
1.0 M and higher: inhibition, 100 mM: activation
-
inhibitory in sodium phosphate/citric acid buffer, 50% inhibition at 100 mM
-
1 mM, dextran-conjugated enzyme and native enzyme retain 13% and 11% of their initial activities
-
0.2 M, complete inhibition
-
MD calculations, discussion of effects
-
5 mM, 26% inhibition
-
100 mM, inhibits ATP hydrolysis by 30%
-
the decapping reaction is significantly inhibited by increasing salt concentration, with KCl being a more potent inhibitor than NaCl
-
is inhibitory at 200 mM NaCl and above
-
basal activity is independent of NaCl, microtubule-activated enzyme shows 50% inhibition at around 40 mM
-
inhibitory above 50 mM due to binding of the chloride anion in close neighborhood to the thiamine diphosphate cofactor
-
100 mM, 30-60% decrease in activity. 50 mM, reductions of 10-25% of activity. 10 mM, 5-15% reduction of activity
-
about 98% residual activity at 50 mM
-
decarboxylation of substrate phenylalanine is inhibited increasing concentrations of NaCl, no inhibition for substrate tyrosine
-
at pH 6.5
-
enzyme from infected cells is unaffected up to 0.8 M, 50% inhibition of the enzyme from uninfected cells at 0.45 M
-
800 mM, 50% inactivation
-
100 mM, 76% inhibition
-
38% inhibition at 20 mM
-
in cells cultivated with 200 mM NaCl, the inhibition produced in fumarase is 90%
-
slight inhibition, wild-type and mutant enzymes
-
1 mM, 10% inhibition
-
5 mM, 13.3% inhibition
-
optimal concentration 62.5 mM for substrate chondroitin 6-sulfate, 50% inhibition at 125 mM, optimal concentration 125 mM for substrate dermatan sulfate, 50% inhibition at 250 mM
-
the enzyme loses 54% of its activity after the addition of 100 mM NaCl, and 2% of activity remain at 500 mM NaCl
-
400 mM, 34% inhibition
-
150 mM
-
0.4% wt/vol, 78% residual activity
-
0.5 mM, about 25% inhibition
-
0.125 M
-
80% inhibition at 0.2 mM, affects C-type NP 1-53 stimulation of the enzyme
-
stimulates, maximal effect at 0.05 M, inhibition at higher concentrations
-
additions up to 0.1 M do not reduce the activity much, at 0.5 M NaCl less than 10% of the activity is retained
-
0.2 M
-
both the enzyme's phosphoglucomutase and phosphomannomutase activities decrease at increased NaCl concentrations, with phosphomannomutase displaying slightly higher levels of relative activity (55% relative activity at 0.2 M NaCl) than phosphoglucomutase (43% relative activity at 0.2 M); but as NaCl concentrations increase, similar decreases in relative phosphoglucomutase and phosphomannomutase activities are evident
-
inhibition is cooperative, NaCl also increases the sensitivity of the enzyme to inhibition by Phe
-
at high concentrations
-
approx. 50% inhibition at 100 mM, approx. 90% inhibition at 600 mM
-
30% ATPase inhibition at 200 mM
-
150 mM NaCl, 3 h, most of the JcDHX candidates are repressed
-
inhibits enzyme forms PC-1 and PC-2 much more than PC-3
-
100 mM, 40% inhibition of ATP-diphosphate exchange, 500 mM, 91% inhibition
-
50% inhibition at 100 mM, recombinant HIS-/thioredoxin-tagged enzyme
-
no activity of isoform LeuRS1 is detected in NaCl solutions
-
concentration of 5-20 mM decrease the activity 20-25%
-
2-3 M, 40% loss of activity
-
almost complete inhibition at 250 mM
-
the polyglutamylase activity of the recombinant enzyme is inhibited by NaCl in proportion to the concentrations of NaCl: 100 mM NaCl suppresses the enzyme activity at 40%, and 200 mM NaCl suppressed it at 90%
-
inhibition above 100 mM
-
inhibits the purified enzyme at 0.1 M, but not the immobilized enzyme in crude extract of recombinant yeast cells
-
slight inhibition at 20 mM
-
30% inhibition at 100 mM
-
at 300 mM or 450 mM NaCl, the activity of the H+-ATPase significantly increases. At 600 mM NaCl, the activity decrease and reaches a level below control in shoots and roots
-
inhibits ATPase activity
-
increase in salinity reduces the nitrate transport into wild-type cells
-
no ATPase activity above 300 mM
-
about 78% reduced activity at 500 mM NaCl
-
0.5 M, inhibits
-

Metals and Ions (720 results)

top print hide
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
most active at 5 M NaCl or 4 M KCl
-
the activity is dependent on the concentration of NaCl or KCl in the activity buffer, being optimal at 1.3 M
-
activity is increased by nearly 120% when NaCl concentration is 2 M. Transgenic Arabidopsis thaliana ectopic expressing the enzyme (HmS6PDH) accumulates more sorbitol under salt stress
-
forward reaction highest activity at 4.5 M, reverse reaction at 3.5 M
-
activation
-
maximal activity at 1.5 M
-
optimal activity is observed in the presence of 500 mM NaCl or KCl
-
activation
-
activates 15% at 100 mM
-
activity at 2 M NaCl is more than 4fold higher than that in the absence of salt
-
activates, best at 0.4 M
-
specific HMGR activity is responsive to changes in NaCl concentrations. Minimal activity under optimal conditions and an increase in HMGR activities and protein levels under hyposaline and hypersaline conditions. HMGR activity is crucial for halotolerance as well as for the changes in protein prenylation in response to changing salinity
-
maximum activity in the presence of 4 M NaCl
-
activation of the enzyme was obtained by increasing the salt concentration to 3 M NaCl
-
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
-
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
-
at 400 mM regains 63% activity on refolding
-
addition of a neutral electrolyte, such as NaCl, shields repulsion interactions in the highly positively charged enzyme at pH 2.0, effects on the secondary structure by increasing NaCl concentrations at pH 2.0 and 25°C, overview
-
when Dunaliella salina is cultured chronically at various salinities, the accumulation of single cell glycerol increases with increased salinity, Dunaliella salina also can rapidly decrease or increase single cell glycerol contents to adapt to hypoosmotic or hyperosmotic shock
-
50 mM, 19% of the activity with Mn2+
-
activation
-
50 mM KCl, 19% of the activation with 50 mM NH4Cl
-
optimal salt concentration is 350-400 mM
-
100 mM, 3.8fold activation
-
induces the ascorbate oxidase activity
-
high concentration of NaCl (over 200 mM to 1200 mM) can enhance the activity of isozyme MGMnP1
-
activates 2 fold at 1 M, pH 5.0, 25°C
-
activates 2 fold at 1 M, pH 5.0, 25°C
-
there is a stimulation of catalase by addition of NaCl 10 mM (176%)
-
5 mM, activation to 144% of control
-
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
-
has no significant effect on enzyme activity up to 3.5 g/l
-
stimulation, optimum at 0.5 M
-
reduces the activity of the isozymes LH1, LH2a, LH2b, and LH3 with most of the synthetic nonpeptide substrates tested, in some cases the isozyme is activated or completely inhibited, overview
-
activates at an ionic strength of 0.222
-
as a true halotolerant enzyme, MmoC still shows 50% of its specific activity at 2 M NaCl. Evaluation of salt tolerance for NADH-mediated reduction of benzyl viologen by MmoC at non-optima conditions, 23°C and pH 7.0
-
the enzyme is optimally active at 250 mM NaCl, with an activity increase of more than 25% compared to the enzyme in the absence of NaCl
-
stabilizes
-
10% is optimal NaCl concentration for Chromohalobacter sp. strain HS-2
-
activates
-
activation at high concentration
-
0.1 mM, slight activation of microsomal enzyme
-
the maize enzyme is greatly stabilized in presence of NaCl
-
the intracellular VvAHGD shows weak salt tolerance
-
3 M, 67fold activation
-
optimally active under high-salt conditions (3.5-5 M NaCl)
-
maximal activity at salt concentrations from 3 to 4 M NaCl
-
stimulation of NADPH-dependent reaction, 70% stimulation at 100 mM
-
enzyme activity increases eightfold by the addition of 500 mM NaCl at pH 6.0, fourfold by 250 mM at pH 8.0, and becomes independent of salt concentration at pH 10.0
-
salt increases PAO activity
-
optimum concentration 0.4-0.6 M, about 4fold activation for substrate ferricytochrome c
-
100 mM NaCl increases enzyme activity in leaves from plants grown on 0.1 or 1 mM nitrate about 3fold
-
activating
-
optimum salt concentration: 2 M
-
enhances activity
-
completely inactive in absence of NaCl
-
up to a concentration of 100 mM, up to 2fold activation
-
enzyme prefers high ionic strength, activation
-
all three APR isoforms increased 3fold in roots after 5 h of treatment with 150 mM NaCl, regulation of salt stress by plant hormone signalling, overview
-
at 40-70 mM NaCl in 50 mM Tris/HCl buffer, close to the physiological conditions in plant chloroplasts, delicate interprotein regulation optimizes SiR activity. At NaCl concentrations above several hundred millimolar, collision and diffusion may limit the formation of the stable electron-transfer competent complex
-
activates VhoGAC activity, highest activity at 1 M
-
activates FdhGHI activity, best at 2 M, formate oxidation is slightly lower with 2 M KCl instead of NaCl
-
the maximum specific chlorate reductase activity is detected in the presence of low NaCl concentrations at 35 °C. At salt concentrations higher than 0.4 M, the maximum specific activity can be detected at higher temperatures (between 40°C and 45°C)
-
activation, 0.4 M
-
enzyme mutant N4CMT79-324 shows sensitivity to ionic strength above 200 mM, ionic strength has opposing effects on solubility/stability and activity, overview
-
slightly stimulated up to 0.2 M
-
incubation of native calf thymus DNA in presence of 40 mM NaCl results in 50% inhibition, more than 90% inhibition at 200 mM. With denatured calf thymus DNA, low concentrations of NaCl, up to 90 mM stimulate, 50% inhibition at 175 mM
-
maximum activity in presence of 150 mM NaCl
-
optimal concentration: 100 mM
-
activity is optimal at an NaCl concentration of 200 to 500 mM
-
while raising the NaCl concentration from 1.5 to 3.5 M leads to an increase in enzyme activity, this increase is 3fold lower than that detected in the presence of optimal KCl levels
-
1 M increases the activity 20fold
-
slight activation at 0.25 M
-
activation at 200 mM
-
stimulates
-
synthesis of unsaturated fatty acid and double bond index (DBI) of phosphatidylglycerol of plants are inhibited by salt stress
-
1.4fold stimulation at 0.5 M
-
optimum concentration in assay 100 mM
-
SpNaa50 maintains the ability to co-migrate with SpNatA in sizing buffer with NaCl concentration as high as 1 M
-
optimal activity at 0.5 M
-
100 mM, activity is increased 1.5fold
-
activation in presence of glucose 6-phosphate
-
0.1 M NaCl stimulates more than 2fold
-
the transcript level and protein abundance of CsSUS3 hardly change during salinity treatment, but the enzyme activity increased slightly, especially on the first and ninth days, compared with control
-
activates, best at 2%
-
activation, 0.2 M
-
activates at 50 mM, slightly less effective than KCl
-
or KCl, required for optimal activity
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10-30%
-
preferred salt, best at 50 mM
-
addition of NaCl stimulates the total activity of the enzyme in the concentration range of 0.5 M to 3.0 M, and the maximum activity (142.6%) is achieved at 1.5 M NaCl
-
activates 11% at 0.1 mM
-
HmcIsc activity increases with increasing NaCl concentration reaching an optimum at 3.5 M NaCl. The Na+ ion, being the most abundant in Tuz Lake, is one of the most essential factors to preserve the enzyme stability and function. Replacement of Na+ by Mg2+ in the chlorine salt leads to a drastic decrease in HmcIsc activity, but replacing Cl- by SO4 2+ restores this inhibition to a great extent. Although extracellular HmcIsc is still enzymatically active at 4.5 M NaCl, the free water at such concentrations becomes extremely scarce. Indeed, although the water binding capacities of fructans and NaCl are very similar, extreme salt levels will remove the water from the carbohydrates, promoting carbohydrate:carbohydrate interactions
-
1 mM: activation to 118% of control. 10 mM: activation to 121% of control tagged enzyme
-
activates AT2 transferase
-
the activity of AvNRT increases up to 2fold in 4 M NaCl aqueous solution
-
optimum concentration is 114 mM
-
alpha2,6-sialyltransferase activity is increased approximately 40% in the presence of 300-800 mM
-
in presence of 500-700 mM NaCl 2fold increase in activity
-
0.2 M activates
-
the enzyme shows tolerance to high salt concentrations up to 2 M NaCl. Addition of up to 400 mM NaCl results in a slight increase in the activity of enzyme Hoch3033
-
activates slightly at up to 350 mM, inhibits by 50% at 1.25 M
-
at 50 mM
-
Induced gene expression in rice by 200 mM. Level of relative germination in the two T3 transgenic tobacco lines overexpressing the OsITL1 gene is approximately 20-30% lower than that in the wild-type lines in the presence of 100 mM NaCl. In presence of 150 or 200 mM NaCl, seedling development is more significantly inhibited in transgenic tobacco plants than in wild-type plants. Transgenic plants that overexpress OsITL1 are more sensitive to NaCl stress during seed germination and early seedling development. The leaves of the transgenic seedlings show complete bleaching or extensive chlorosis after 7 days of exposure to 200 Mm NaCl
-
addition of 50 mM NaCl markedly enhances Mak stability
-
increased activity at high salt conditions, 100 mM
-
stimulates, yields 50% of the activity observed in equimolar KCl
-
50% of the stimulation compared to KCl
-
0.5 M, stimulates about 2-fold
-
enhances activity up to about 1.3fold at 1 M
-
mitogen-activated protein kinase kinase 5, MKK5, is activated in response to salt stress
-
250 mM, stimulates
-
from 0-0.5 M does not affect activity
-
activation at 0.2 M, inhibition at higher concentration
-
optimal activity at 50 mM NaCl2
-
optimal activity at 300-500 mM NaCl
-
stimulates
-
activates
-
activation, sulfation of tert-butoxycarbonylcholecystokinin
-
induces aggregation of the purified enzyme at 0.5 M
-
activates
-
activates below 0.1 M, inhibits at higher concentrations
-
150 mM, inhibitory at 500 mM when pH below pH 8
-
in the presence of 3 M activity of the enzyme increases by 28%
-
a high ionic strength of 0.5 M NaCl in the reaction mixture is required for optimal activity
-
25%, the enzyme retains 60% of its activity
-
MtbXthA exhibits an increase in AP site incision activity in a salt-dependent manner
-
enzyme is active in NaCl, but the cleavage efficiency is 10times lower when compared to its activity in KCl
-
optimal concentration: 20-40 mM
-
optimally active at NaCl concentrations ranging from 100-200 mM
-
the enzyme is active in NaCl concentrations ranging from 100 to 200 mM
-
activates at 50 mM, inhibits at concentrations above 100 mM
-
0.5-4.5 M extracellular NaCl activates intracellular glycerol production
-
stimulates
-
activates the 4-nitrophenyl phosphatase activity of the Na+/K+-ATPase, increases stimulation by other agents, e.g. KCl, oligomycin, and ATP, stimulation mechanism and kinetics, is also required for ATPase activity of the enzyme
-
at 0.1 M, purified enzyme, 58% reduced activity after 30 min at 37°C
-
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
-
PyapApase shows higher activity below 100 mM NaCl, and more than 100 mM NaCl inhibits its activity. The enzyme activity at 50 mM NaCl is 5fold higher than that at 500 mM NaCl
-
0.5 M, activates
-
activates at 1 mM by 58%, inhibits at 5 mM by 18%
-
the enzyme is capable to hydrolyze DNA in the presence of 0.9% NaCl containing 0.002 M calcium cations
-
200 mM, 37% increase of activity
-
when rice suspension-cultured cells are treated with 100 mM NaCl, PLDalpha activity in cell extracts show a transient activation with a threefold increase at 1 h. The amount of OsPLDalpha protein decreases slightly in the cytosolic fractions, whereas it increases significantly in the tonoplast after NaCl treatment. Knockdown of OsPLD-1 prevents the NaCl-induced increase in the transcript level of OsVHA-A, encodes TP H+-ATPase, and OSA2, encodes PM H+-ATPase, as well as OsNHX1, encodes TP Na+/H+ antiporter
-
in vivo: activity decreases (mIMCD-3 cell), measuring choline by chemiluminescence, substrate sn-glycero-3-phosphocholine. in vitro: no direct decrease in GDPD5 activity, GPC-PDE in vitro activity is reduced by over 60% in immuno-precipitates from HEK293 cells exposed to high NaCl concentration.
-
stimulates
-
stimulation, over pH-range 4.2-4.8, glucuronic acid 2-sulfate-2,5-anhydro-D-mannitol 6-sulfate as substrate, inhibits at pH 3
-
1 M, 2.5fold increase in activity
-
1 mM, 94% activity compared to control without any metal ion
-
3 mM: stimulation, above 10 mM: inhibition
-
activates
-
maximal activity in presence of 0.4 M NaCl
-
5 mM, activation to 125% of control
-
0.2-1 mM, 110% of initial activity
-
0.2-1 mM, 110% of initial activity
-
activity remains relatively constant over the range 50-250 mM NaCl (pH 7.0), but decreases significantly below and above these concentrations
-
maximal activation at 8% (w/v)
-
optimum activity in presence of 0.1-0.2 M, inhibitory above 0.2 M
-
highest activity at 1.0 M
-
activation
-
optimally active at 4 M NaCl
-
the hydrolytic activity displays a maximum increase of 67% in the presence of 0.8 M NaCl
-
5% (w/v) activates rAglST1, 5-10% (w/v) activates rAglST2
-
12.5% activation at 10 mM
-
slight activation at 75 mM
-
required, optimal in 5% sodium chloride
-
enzyme is active in salt concentrations up to 5 M NaCl. The tolerances to heat, alkali and ionic liquids are salt-dependent. At 37°C, the optimal salt concentration is 0.25 M NaCl, at 80°C, the optimal salt concentration is 5 M NaCl
-
effects on kinetics, overview
-
optimal concentration: 200 mM
-
activates
-
a salt-tolerant aspartyl aminopeptidase, the relative activity of the enzyme remains 85% in 3 M NaCl solution for 15 days, Km and Vmax are slightly affected in 3 M NaCl solution. Enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase
-
absolutely required for activity
-
highest PepA activity is observed at 12% NaCl concentration
-
stimulates, optimal cobcentration
-
optimal activity between 50 and 200mM NaCl for recombinant truncated cathepsin C. Variant's enzyme activity in the presence of 0.15 mM NaCl is about 55% of optimal activity
-
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%
-
optimal activity at NaCl concentrations of 0.7–2 M. Little to no activity at low concentrations of salt (150 mM NaCl)
-
140 mM
-
increases activity of recombinant S1P-1 25% at 50 mM dependent on the substrate used
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
-
best at 1 M
-
best at 0.15 M
-
elastase 1: slight inhibition above 150 mM, elastase 2: 25-250 mM, activation
-
required
-
50% activation at 600 mM
-
0.1-1.0 M, highest activity with Nalpha-tert-butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester
-
variation of the sodium chloride concentration from 25 mM to 1.5 M do not show any significant change in the autoproteolysis of MtLexA
-
kcat/Km values decrease by adding NaCl up to 100 mM. This results from the systematic increase in Km values with the increase in NaCl concentration in the range 1 to 10 mM
-
the maximal activity of the purified pernisine seen for 20 mM NaCl in the absence of 1 mM CaCl2 increases to more than 2fold after the addition of CaCl2, with even larger relative enhancement by CaCl2 at higher NaCl concentrations
-
highest proteolytic activity is at 150 mM NaCl
-
activation, 0.15-1.25 M
-
stimulates at 0.3 M
-
Km increases up to 400 mM, then decreases and remains constant at 50-60% up to 1 M, kcat maximum at 300 mM
-
activates at 50 mM, the enzyme is stable until 150 mM NaCl
-
100 mM, increases proteolytic activity by about 50%
-
required, at 100 mM
-
the protease works more efficiently at high salt concentrations, 2 M NaCl, than at lower salt concentrations
-
1 M, activates
-
activates optimally at 2.4 M
-
1 M NaCl, rate of substrate cleavage increases up to 4fold
-
enzyme assay in presence of 2 M NaCl
-
activates at 4 M
-
strong activation
-
strong activation
-
wild-type and Y219F mutant MMP-7 activity is enhanced with increasing concentration of NaCl, activation by 550% and 850% at 4 M NaCl, respectively
-
4-bladed beta-propeller protein in which the 4 blades are arranged around a channel-like opening in which Ca2+ and a Na+Cl- ion pair are bound
-
activates IDE at high concentration
-
when tested at different concentrations of NaCl ranging from 20 to 500 mM, lysostaphin retains almost the same level of protease activity
-
2 mM NaCl increases enzyme binding to the elastin fibres
-
at 150 mM NaCl, acer-1 seedlings dramatically loose vitality compared with the wild-type, the amiR-ACER-1 seedlings are the most sensitive to salt, showing obvious differences from the other genotypes after 100 mM NaCl treatment for 12 days
-
influences the oligomerization status of the enzyme. 60% octameric and 40% dimeric enzyme in absence of NaCl, 5% octameric and 95% dimeric enzyme at and above 150 mM NaCl, profile overview
-
maximum activity at 18-23% NaCl at 50°C, loses activity irreversibly in the absence of NaCl
-
150 mM NaCl treatments result in an upward trend in the expression of CsGGT2 before 12 h and then decreases rapidly within 96 h. The content of theanine increases significantly under the 150 mM NaCl treatments. The content of theanine is increased by 3.55fold after 96 h of exposure to 150mM NaCl compared with the treatment for 6 h
-
1 M: 1.69fold activation
-
the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increase, the activity of the enzyme is reduced to almost half of the maximal activity but the enzyme is still partially active
-
optimal activity in presence of 3.5 M
-
1.0 mM, relative activity 107%
-
maximum activity at 0.15 or 2 M
-
optimal activity of APOBEC1 without auxiliary factor at 80 mM ionic strength, optimal activity of APOBEC1 in presence of the auxiliary factor ACF at 90 mM
-
100-150 mM activates
-
large increase in the mobility of APOBEC3G cytidine deaminase on ssDNA at higher salt, Mg2+ or NaCl
-
1 mM, stimulation
-
50 and 200 mM, 46 and 42% activity enhancement, respectively
-
stimulates
-
maximal activity at 0.1 M
-
monovalent metal ions stimulate the enzyme activity
-
20 mM NaCl used in this mixture was found to be optimal for ATP hydrolysis
-
GTPase activity is measured in the presence of 3.6 M NaCl
-
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
-
activation between 25 and 200 mM to a maximum of 14% a at 75 mM
-
the enzyme activity is enhanced by increasing KCl and NaCl concentrations. Optimum activity is diaplayed in 2.5 M KCl, while that in equimolar NaCl is lower. However, aldolase is less active in NH4CI and LiCI
-
activates
-
maximal activity for the enzyme in whole cells: 0.4-0.5 M
-
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
-
0.1 mM, around 2fold increase in activity
-
ligand binding sites, effector on the action of activators or inhibitors, overview
-
1 mM, activation to 125% of control. 10 mM, activation to 142% of control
-
highest activity at 200 mM
-
2 mM, 1.1fold activation
-
does not affect the product specificity of Cop4 significantly at 1 M
-
does not affect the product specificity of Cop4 significantly at 1 M
-
up to 50 mM no influence on the dRP lyase acticity of beta-pol or 8-kDa domain occurs. Above 200 mM the activity is completely abolished
-
addition of increasing concentrations enhances the activity by 2fold
-
optimum is 200 mM
-
modest (about 30%) activation at 0.05 M, strongly inhibition (more than 50%) at higher concentrations (0.5 M)
-
optimal concentration: 150 mM
-
the transgenic and the untransformed plants are exposed to 100 mM NaCl. The transgenic plants survived whereas the untransformed control plants fail to survive
-
enhances activity
-
increases the activity
-
activates best at 300 mM
-
activates at 0.1-4.9 M, the enzyme works best at 0.5-1.0 M NaCl in the presence of 1 mM Mn2+
-
modulates enzyme expression increasing or decreasing it dependent on growth conditions, overview
-
50-500 mM, stimulates ATPase activity. The enzyme maintains full ATPase activity up to 2 M
-
required at 0.1-3 M, salt dependence profile, overview
-
stabilizes at 200 mM
-
requirement for high concentrations of salt, with the exception of Mg2+, the requirement for ion is nonspecific. Chaotrophic salts are effective at lower concentrations than less chaotrophic salts
-
stabilizes at 200 mM
-
theanine biosynthesis, derived from nitrogen metabolism in Camellia sinensis plants, can be influenced by salt treatment
-
optimal concentration between 20 mM and 50 mM
-
in plants grown with 100 mM NaCl supply, ATPase activity increases with salinity in a non-competitive way for 7 d and 21 d. In plants grown with 10 mM K2SO4 plus 100 mM NaCl supply, activity decreases competitively with Na+, after 21 d of salinity, with different effects on Km and Vmax
-
2-3fold activation at 1 M
-
ATPase activity increases with increasing salt concentration
-
5 mM, increases the activity by 20%, respectively
-
100 mosmol/kg osmolality, stimulates OpuA activity
-

Enzyme Kinetic Parameters

Ki Value (23 results)

top print hide
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
1.82
-
competitive vs. L-dopa
70
-
-
85
-
in 100 mM potassium phosphate buffer pH 8.0, at 30°C
4.5
-
-
67
-
30°C, pH 6.6
1
-
pH 6.7, 85°C
0.05
-
salt 0.01 M
10
-
fully reversible by dialysis or dilution
0.16
-
-
1831
-
pH 2.8, 37°C, enzyme from healthy individuals
0.1
-
-
500
-
-
22.4
-
with acetyl-KHYR-7-amido-4-carbamoylmethylcoumarin
0.43
-
25°C, pH 6.5
0.000329
-
37°C, pH 8.0
150
-
at pH 7.4 and 25°C
198
-
wild type enzyme, pH 6.9
200
-
-
115
-
-
50
-
-

IC50 Value (33 results)

top print hide
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
5
-
catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
0.01
-
IC50: 0.01 mM
300
-
in 100 mM potassium phosphate buffer pH 8.0, at 30°C
550
-
IC50: 0.55 M
4
-
about
200
-
IC50 200 mM
50
-
pH 7.5, 30°C
40
50
IC50: 40-50 mM
0.028
-
inhibits native M1Pase with an IC50 value of 0.028 mM, for recombinant enzymes between 0.054 mM and 0.044 mM
2000
-
IC50 above 2000 mM, at 25°C in 100 mM sodium phosphate (pH 7.0)
0.07
-
-

References & Links

top

Links to other databases for sodium chloride

top print hide
EXTERNAL LINKS
ChEBI
PubChem
UniChem