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BRENDA support

Ligand ammonium sulfate

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Basic Ligand Information

Molecular Structure
Picture of ammonium sulfate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
H8N2O4S
ammonium sulfate
BFNBIHQBYMNNAN-UHFFFAOYSA-N
Synonyms:
(NH4)2SO4, ammoniumsulfate, diammonium sulfate

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
FLEEL + CO2 + O2 + ammonium sulfate = ? + vitamin K epoxide + H2O
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (1 result)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
mesoporphyrin IX + ferrous ammonium sulfate = mesoheme + ammonium sulfate
show the reaction diagram
-
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Activator in Enzyme-catalyzed Reactions (70 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activity of the purified recombinant enzyme is stimulated about 4fold by 1.5 M
-
about 100% activation at 10 mM
-
enhancing effect on NAD-dependent 3-phospho-D-glycerate oxidation and 3-phosphohydroxypyruvate reduction but inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
-
additions of ammonium sulfate even at weak concentrations (10 to 70 mM) stimulate catalatic activity measured in the presence of 1.5 M NaC1 by about 30%
-
improves reactivation of enzyme with FAD after FAD depletion
-
activates, optimal concentration is 1.25 mM
-
the enzyme activity is increased about 10fold in the presence of 0.045 M (NH4)2SO4
-
stimulates activity
-
short incubation activates isozyme E-II, not E-I
-
stimulates
-
250 mM, 10fold activation
-
less effective than Na2SO4
-
10 mM, relative activity 108%
-
45 mM, 10% increase in activity
-
45 mM, 10% increase in activtiy
-
activates at 0.5 mM
-
maximum of activity: about 45% (NH4)2SO4 and decrease in activity at higher concentrations
-
10 mM, activates
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stimulation
-
activates
-
high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
-
inhibition at high concentration, acceleration of activity at low concentrations
-
inhibitory above 30 mM, activates below
-
stimulates
-
optimal concentration of 20 mM, inhibition below and above 20 mM
-
500 mM, activates
-
with FeSO4, when used as nitrogen source, 1.7fold increase in activity
-
10 mM, 127% of initial activity, 50 mM, no residual activity
-
xylanase activity is 9.7 U/ml with 0.1% urea
-
20% activation at 0.15 M
-
0.4 M, enhances activity of unpurified enzyme by 55%, but no effect with purified enzyme
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substrate dCMP-Hg-S-CH2-CH2-OH, 0.2 M ammonium sulfate: activation, reversed by cCTP
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50 mM, stimulates
-
1 mM, 203% of initial activity
-
20% stimulation at concentrations above 25mM
-
with 30 mM (NH4)2SO4, the activity is maximal
-

Inhibitor in Enzyme-catalyzed Reactions (149 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.05 mM: slight inhibition, 400 mM: activation
-
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
-
at high concentrations
-
1 M, 71% inhibition
-
100 mM, 68% inhibition, 10 mM, 8% inhibition
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
-
slightly inhibits
-
10 mM
-
more than 50% inhibition at 25 mM
-
mutant enzyme is less sensitive to inhibition than wild-type enzyme
-
enzyme activity is inhibited by ammonium sulfate ; however, this inhibition is overcome by addition of 10 mM guanidine
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1.9 M, E II: activation at short incubation time, E I: complete inactivation after 10 h incubation; inactivation of isozyme E-I after 10 h
-
200 mM, 16% inhibition
-
1 mM, 71% inhibition
-
0.15M-0.2M (NH4)2SO4 stimulates by a factor of 1.3. Higher concentrations are inhibitory
-
slightly inhibitory
-
20% activity at 0.5 M
-
strong inhibitor at 1 mM
-
competitive against both acetyl-CoA and histones
-
50-300 mM, weak inhibition
-
20% inactivation at 20 mM
-
1 mM
-
1 M, about 50% inhibition
-
inhibits the activity of the partially purified enzyme
-
weak
-
at high concentration
-
0.05 mM, 45% inhibition, 5 mM, complete inhibition
-
slightly inhibitory
-
50% inhibition at 200 mM
-
high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
-
inhibits at high concentrations
-
5 mM, 29% inhibition
-
above 0.2 M, stimulates at 0.05-0.1 M
-
above 30 mM, activates below
-
slightly inhibitory at 50 mM
-
0.35 M, 50% inhibition
-
inhibits both subunit GlgC and GlgC/GlgD complex
-
1.0 M, 83% inhibition, reversible by desalting
-
above 60 mM
-
optimal concentration of 20 mM, inhibition below and above 20 mM
-
5 mM, 71% of initial activity
-
0.06 M, 55% inhibition
-
0.05 M
-
50% inhibition at 25 mM, inhibition of formation of acid-soluble products
-
0.05 M, 70% inhibition
-
10 mM, 127% of initial activity, 50 mM, no residual activity
-
complete inactivation with higher concentrations
-
30% inhibition at 10 mM
-
slight
-
0.5 M, 40% inhibition
-
intracellular enzyme
-
0.5 mM, 36% residual activity
-
0.5 M, 30% residual activity
-
76% inhibition at about 40 mM
-
inhibition above 10 mM
-
75% residual activity at 800 mM
-
92% inhibition at 2 mM
-
10 mM, slight
-
62% inhibition at 80.6 mM, complete inhibition at 806 mM
-
recovery after restoration of lower ionic strength shows hysteresis effect
-
50% inactivation at 400 mM
-
66% inhibition at 4 mM
-
100 mM, 47% inhibition
-
-
-
-
-
weak, gamma-glutamyl transferase activity
-
almost complete inhibition at 500 mM
-
25 mM
-
10 mM, 60% inhibition
-
(NH4)2SO4 concentrations higher than 30 mM are inhibitory. At 100 mM KCl, concentrations of (NH4)2SO4 above 12 mM are inhibitory
-

Metals and Ions (41 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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
-
4fold activation
-
1.5 M, stimulates about 4fold
-
activity increases with increasing salt concentration up to 2 M
-
the most effective salt, the optimal concentration is 0.035 M
-
0.045 M, 10fold activation
-
enhances enzymatic activity up to a concentration of 0.0014 mM
-
activates
-
the activity of the recombinant methylase in 0.5 M and 1.0 M ammonium sulfate is about 1.25fold higher than in the absence of ammonium sulfate
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activates at at least 0.5 mM
-
0.3-0.5 M: stimulation
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activates
-
activation, 0.05-0.1 M, inhibits above 0.2 M
-
slightly stimulating
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activates
-
activates optimally at 0.2 M
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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
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0.166 M, enhances activity
-
slight activation
-
high salt concentration, (NH4)2SO4, 2 M, dissociates the high molecular weight form yielding the low molecular form and increasing the specific activity
-
1 M, 4fold increase in activity
-
activation is stronger in presence of 1 mM ascorbate
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activation to 105.5% at 5 mM
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(NH4)2SO4 enhances autoconversion of the enzyme, it increases formation of the mature (M) form, after 2 h incubation all molecules are converted to the M-form
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optimal activity in presence of 2.0 M, 48% of the activation with NaCl
-
relative activity: 409%
-
0.4 M, 1.5fold enhancement of activity
-
optimal up to 50 mM
-
stimulation by 5-25 mM
-
2-3fold activation at 1 M
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Enzyme Kinetic Parameters

Ki Value (5 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.05
-
pH 6.7, 85°C
0.85
-
-
2.5
-
pH 7.5, 30°C

IC50 Value (2 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE

References & Links

Links to other databases for ammonium sulfate

EXTERNAL LINKS