Ligand ammonium sulfate

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Basic Ligand Information

Molecular Structure
Picture of ammonium sulfate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
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
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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 (68 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activity of the purified recombinant enzyme is stimulated about 4fold by 1.5 M
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about 100% activation at 10 mM
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enhancing effect on NAD-dependent 3-phospho-D-glycerate oxidation and 3-phosphohydroxypyruvate reduction but inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
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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%
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improves reactivation of enzyme with FAD after FAD depletion
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activates, optimal concentration is 1.25 mM
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stimulates activity
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short incubation activates isozyme E-II, not E-I
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stimulates
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250 mM, 10fold activation
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less effective than Na2SO4
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10 mM, relative activity 108%
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45 mM, 10% increase in activity
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45 mM, 10% increase in activtiy
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activates at 0.5 mM
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maximum of activity: about 45% (NH4)2SO4 and decrease in activity at higher concentrations
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10 mM, activates
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stimulation
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activates
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high salt activates at high adenosine 5'-phosphosulfate concentrations but inhibits at low adenosine 5'-phosphosulfate concentrations
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inhibition at high concentration, acceleration of activity at low concentrations
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inhibitory above 30 mM, activates below
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stimulates
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optimal concentration of 20 mM, inhibition below and above 20 mM
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500 mM, activates
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with FeSO4, when used as nitrogen source, 1.7fold increase in activity
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10 mM, 127% of initial activity, 50 mM, no residual activity
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xylanase activity is 9.7 U/ml with 0.1% urea
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20% activation at 0.15 M
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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
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1 mM, 203% of initial activity
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optimal functionality of MmGroEL/GroES and its ability to encapsulate larger proteins, such as malate dehydrogenase, requires the presence of ammonium sulfate in vitro
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20% stimulation at concentrations above 25mM
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with 30 mM (NH4)2SO4, the activity is maximal
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Inhibitor in Enzyme-catalyzed Reactions (145 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.05 mM: slight inhibition, 400 mM: activation
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reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
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at high concentrations
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1 M, 71% inhibition
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100 mM, 68% inhibition, 10 mM, 8% inhibition
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inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
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slightly inhibits
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more than 50% inhibition at 25 mM
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mutant enzyme is less sensitive to inhibition than wild-type enzyme
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enzyme activity is inhibited by ammonium sulfatehowever, 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
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200 mM, 16% inhibition
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1 mM, 71% inhibition
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0.15M-0.2M (NH4)2SO4 stimulates by a factor of 1.3. Higher concentrations are inhibitory
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slightly inhibitory
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10 mM
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20% activity at 0.5 M
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strong inhibitor at 1 mM
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competitive against both acetyl-CoA and histones
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50-300 mM, weak inhibition
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20% inactivation at 20 mM
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1 mM
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1 M, about 50% inhibition
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inhibits the activity of the partially purified enzyme
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weak
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at high concentration
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0.05 mM, 45% inhibition, 5 mM, complete inhibition
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slightly inhibitory
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50% inhibition at 200 mM
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high salt inhibits at low adenosine 5'-phosphosulfate concentrations, but activates at high adenosine 5'-phosphosulfate concentrations
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inhibits at high concentrations
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5 mM, 29% inhibition
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above 0.2 M, stimulates at 0.05-0.1 M
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above 30 mM, activates below
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0.35 M, 50% inhibition
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slightly inhibitory at 50 mM
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inhibits both subunit GlgC and GlgC/GlgD complex
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1.0 M, 83% inhibition, reversible by desalting
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above 60 mM
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optimal concentration of 20 mM, inhibition below and above 20 mM
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0.06 M, 55% inhibition
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0.05 M
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50% inhibition at 25 mM, inhibition of formation of acid-soluble products
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0.05 M, 70% inhibition
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10 mM, 127% of initial activity, 50 mM, no residual activity
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complete inactivation with higher concentrations
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30% inhibition at 10 mM
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slight
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0.5 M, 40% inhibition
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intracellular enzyme
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0.5 mM, 36% residual activity
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0.5 M, 30% residual activity
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inhibition above 10 mM
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75% residual activity at 800 mM
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92% inhibition at 2 mM
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10 mM, slight
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62% inhibition at 80.6 mM, complete inhibition at 806 mM
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recovery after restoration of lower ionic strength shows hysteresis effect
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50% inactivation at 400 mM
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66% inhibition at 4 mM
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100 mM, 47% inhibition
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weak, gamma-glutamyl transferase activity
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almost complete inhibition at 500 mM
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25 mM
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10 mM, 60% inhibition
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(NH4)2SO4 concentrations higher than 30 mM are inhibitory. At 100 mM KCl, concentrations of (NH4)2SO4 above 12 mM are inhibitory
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Metals and Ions (38 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
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4fold activation
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1.5 M, stimulates about 4fold
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activity increases with increasing salt concentration up to 2 M
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the most effective salt, the optimal concentration is 0.035 M
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0.045 M, 10fold activation
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enhances enzymatic activity up to a concentration of 0.0014 mM
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activates
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500 mM, stimulates; highly activating
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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
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0.3-0.5 M: stimulation
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activates
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activation, 0.05-0.1 M, inhibits above 0.2 M
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slightly stimulating
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activates
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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
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slight activation
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high salt concentration, (NH4)2SO4, 2 M, dissociates the high molecular weight form yielding the low molecular form and increasing the specific activity
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activation is stronger in presence of 1 mM ascorbate
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activation to 105.5% at 5 mM
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optimal activity in presence of 2.0 M, 48% of the activation with NaCl
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the enzyme requires NaCl for maximal activity but Na2SO4 and (NH4)2SO4 can substitute. Five times more activity than in the presence of NaCl is observed when 1 M (NH4)2SO4 is present
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relative activity: 409%
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0.4 M, 1.5fold enhancement of activity
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optimal up to 50 mM
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stimulation by 5-25 mM
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Enzyme Kinetic Parameters

KM Value (1 result)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
5.4
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37°C, pH 8.5

Ki Value (5 results)

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

References & Links

Links to other databases for ammonium sulfate

ChEBI
PubChem
ChEBI
PubChem