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Ligand diethyldicarbonate

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Basic Ligand Information

Molecular Structure
Picture of diethyldicarbonate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
Molfile
C6H10O5
diethyldicarbonate
FFYPMLJYZAEMQB-UHFFFAOYSA-N
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Synonyms:
DEPC, dicarbonic acid diethyl ester, diethyl dicarbonate, diethylpyrocarbonate, ethoxy-formic anhydride, ethoxyformic anhydride, ethoxy formic anhydride

Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (9 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
isoform A shows 111% activity at 2.5 mM
-
170% activity at 0.4 mM
-
37% activation at 1 mM
-
1 mM, 86% inhibition. Protected by N-acetyl-D Glu or 2-oxo-ketoglutarate
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63% increase of activity at 0.1 mM for IsoI and 38% increase of activity at 1 mM for IsoII
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1.0 mM, relative activity 102%
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1 mM, 114% of initial activity
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Inhibitor in Enzyme-catalyzed Reactions (441 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
100% inactivation
-
complete
-
60% inhibition at 1 mM
-
inactivation
-
1mM, 32.8% residual activity
-
60% inhibition at 1 mM
-
kidney aldehyde reductase
-
complete inhibition at 0.1 mM
-
I80 of less than 17 mM
-
80% inactivation after treatment with 5 mM diethyldicarbonate for 25 min, biphasic inactivation, 40-50% inactivation in first phase, 1-2 histidine residues are acylated by diethyldicarbonate, 250 mM malate provides complete protection, 50% protection with 50 mM MgSO4, 55% enzyme activity is restored with 0.5 M hydroxylamine
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1 mM, 33% inhibition, incubation for 1 min
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inactivation follows pseudo-first-order reaction kinetics, partial protection by NADP+, complete protection in presence of NADP+, 0.25 M hydroxylamine causes total reversal of inhibition
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2 mM, 30% residual activity
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competitive inhibition, 10% inhibition
-
inactivation in simple linear pseudo-first order kinetics, recovery by 0.5 M hydroxylamine
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the covalent modification of His105 inhibits the epoxidation and peroxide dismutations catalyzed by CPO
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less than 50% inhibition at 50 mM
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chemical modification of active site His residues results in reduced enzymatic hydrogenase and diaphorase activities, pH-dependence and kinetics of modifications/inactivation
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65% loss of activity 6 mM
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modifies histidine residues of catechol dioxygenases, 1 mM, 70% inhibition
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modifies one histidyl residue per flavin
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6fold molar excess with respect to enzyme-bound FMN results in 92% inactivation after 13 min, substrate and competitive inhibitors decrease the maximum extent of inactivation to a 50%, modification of histidines
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98% inhibition at 1 mM
-
isozyme CS2, rapid inactivation at pH 6.0, 25°C, t1/2: 1.1 min
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2 mM, no residual activity
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complete inhibition. Inactivation can be partially prevented by the inclusion of L-proline and 2-oxoglutarate in the preincubation mixture
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complete inhibition
-
31% inhibition at 2 mM
-
complete inactivation at 1.5 mM, pH 6.8, after 20 min
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0.5 mM, 33% loss of activity
-
2 mM, 16% inhibition
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at 2.5 mM
-
90% loss of NAD+ dependent activity at 1 mM, retains more than 90% of oxygen-dependent and 3-acetylpyridine adenine dinucleotide+-dependent NADH oxidation activity
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NAD+, NADP+ prevent inhibition
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44% residual activity at 3 mM with feruloyl-CoA as substrate
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2% residual activity at 2.5 mM
-
1 mM, 5% residual activity
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tested at 1.0 mM, 54% inhibition
-
concentration-dependent inhibition, complete inactivation at 50 mM
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reduces PcyA activity to less than 20% of mock-treated enzyme within 10 min, diethylpyrocarbonate-inactivation can be prevented by the presence of biliverdin IXa substrate
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1 mM, 83% residual activity
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rapid inactivation
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inactivation follows pseudo-first-order kinetics
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20 mM, 60% loss of activity
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1.2 mM, complete inactivation after 10 min, activity decrease of 60% can be restored by a 20 min incubation with 900 mM hydroxylamine, pyridoxal 5'-phosphate oxime protects from inactivation, inactivation is due to modification of histidine residues
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reversal of the inhibition by hydroxylamine
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20 mM NADP+ and 20 mM NAD+ partially protected the enzyme against inactivation whereas 20 mM nicotinamide gives complete protection
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the enzyme rapidly loses its activity on incubation with 0.5 mM diethyldicarbonate
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0.1 mM, 62% inhibition
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the quinol-dependent, but not the viologen dye dependent, activity is inhibited irreversibly by exposure to diethyl pyrocarbonate
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modifies ten His per enzyme molecule
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96% inhibition
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decreases ThyX deprotonation activity at least 20fold, is partially reversible with hydroxylamine treatment
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the inactivation of the enzyme by diethyl dicarbonate is specific for histidine residues, pre-incubating the methylase with DNA is able to protect the enzyme from diethyl dicarbonate inactivation, hydroxylamine is unable to reverse the effect caused by diethyl dicarbonate
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90% loss of activity after 5 min at 0.5 mM, preincubation with feruloyl-CoA protects
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80% reversion after treatment with hydroxylamine
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0.3 mM, approx. 67% inhibition of microsomal acyltransferase, approx. 40% inhibition of mitochondrial acyltransferase, approx. 60% inhibition of recombinant mitochondrial acyltransferase, activity is restored to approx 50% by hydroxylamine
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complete inhibition
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1 mM, 45% inhibition
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1 mM, 51% inhibition, 20 min, 20°C
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CPT II, strong, linear pseudo-first order kinetic, modification of a histidine residue, reversible by hydroxylamine, decanoyl-CoA and L-carnitine
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0.04 mM, 50% inhibition, 0.05 mM palmitate partly protects, completely reversible by 50 mM hydroxylamine, enzyme from intestine is less sensitive than enzyme from liver
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69% residual activity at 0.1 mM
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2 distinct tissue types with difference in reactivity, DEP-sensitive subtype typified by aortic ACTAT, DEP-resistant subtype typified by liver ACAT, irreversible inhibition, the inhibitor appear to modify a histidine residue
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88% inhibition at 1 mM
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inhibits MCT1 but not MCT2 at 1 mM
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inactivation, pH dependence, overview
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reversible by incubation with hydroxylamine, binds a histidine residue at the active site
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reversion after treatment with hydroxylamine
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not without Ca2+
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rapid inactivation by modification of three essential His residues, at neutral pH, partial reactivation with hydroxylamine
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the addition of 0.5 mM ATP in the preincubation reaction mixture provided complete protection of enzyme activity from inactivation by diethyldicarbonate
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inhibition prevented by preincubation with acetyl-CoA
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0.84 mM, 50% inhibition
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0.2 mM, 74% inhibition
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protected against inactivation upon pre-incubation with stigmast-5-en-3beta-ol or UDP-glucose
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5 mM, 98% inhibition with quercetin or gossypetin as substrate
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10 mM, 16% activity retains
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0.1 mM, 31% inhibition
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20% inhibition at 2 mM
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0.2 mM 31% inhibition
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binds to His; hydroxylamine partiallly protects, UDP-GalNAc protects
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0.5 mM, activity is decreased to 11%; 0.5 mM, activity is decreased to 13%
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10 mM, about 90% inhibition
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i.e. DEPC; reversible by hydroxylamine, UDP-glucose protects, inhibitor acts on histidine residues, including His193, within or near UDP-glucose binding site
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35% inhibition at 0.1 mM
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alkylation of Arg155, complete inactivation at pH 9.0, pH dependent
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inactivation with a second-order rate constant of 220/M/min, subtstrates protect from inactivation, enzyme activity is recovered by treatment with hydroxylamine
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Phe-sensitive isozyme, pH-dependent, phosphoenolpyruvate protects wild-type and mutants H64G, H207G, H304G
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80% loss of activity at 5 mM
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deoxyguanosine slightly protects
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27% residual activity at 0.04 mM
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complete inactivation at 1 mM
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in the presence or absence of ATP-sulfurylase
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2.5 mM, 10% residual activity
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inactivates the enzyme by combination with histidyl residues, inhibition is reversed by hydroxylamine
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His108 is critical for activity
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50% inhibition at 0.28 mM
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almost complete inhibition
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complete inactivation at 2 mM
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20% residual activity at 1 mM
-
0.5 mM, 90% inactivation after 10 min, activity can be recovered to 41% of initial activity by treatment wit 200 mM hydroxylamine
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71% inhibition at 5 mM
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54% inhibition at 1 mM; 56% inhibition at 1 mM
-
40% inhibition at 5 mM, 90% at 20 mM
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100% inhibition at 0.8 mM
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1 mM, 97% inhibition
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at pH 6-8, due to histidine modification
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inactivation
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7% inhibition at 1 mM
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complete inhibition at 1-10 mM
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inactivation
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pH 6.5, 22°C, time-dependent inhibition, kinetics, completely reversed by 0.5 M hydroxylamine
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0.02-0.1 mM, complete inhibition, sphingomyelinase P1; 0.02-0.1 mM, complete inhibitionsphingomyelinase P2
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55% inhibition at 1 mM after 30 min
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24.5% residual activity at 10 mM
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1 mM, 98% residual activity
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complete inhibition at 2 mM, at pH 6.0
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the compound modifies a His residue that results in a less active enzyme. After 40 min with 40 mM diethylpyrocarbonate at 30°C pH 6.0, trehalase activity decreases to about 50% of the initial activity
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48% inhibition at 4 mM, 76% at 10 mM
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inactivation indicates a carbethoxylation of histidine residues
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complete loss of activity at 36 mM (pH 6.0)
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2 mM, 60% of original activity
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with 30 mM 1.1% of activity remains
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1 mM, 10-20% inhibition
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5 mM, inhibition to 70% of control
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inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation
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88.43% residual activity at 10 mM
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50% inhibition at 0.011 mM
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modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation
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10 mM, 92.8% inhibition
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inactivates
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modification of the Zn2+-complexing histidine residues in the active site, inactivation
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reversed by hydroxylamine
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partially reversed by hydroxylamine (not)
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93% inhibition by 93 mM, complete inhibition by 10 mM
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90% inhibition at 0.5 mM
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at 2 mM 95% and at 5 mM 80% residual enzyme acitvity
-
89% residual activity at 10 mM for IsoI and 90% residual activity at 10 mM for IsoII
-
1 mM, 49% inactivation after 30 min and 63% inactivation after 120 min in 100 mM potassium phosphate, pH 6.0
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2 mM, complete inhibition
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complete inactivation, 2-deoxy-2-amino-D-glucitol 6-phosphate protects
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inactivation
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inhibits GTP hydrolysis, but not the assembly reaction
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about 55% residual activity at 1% (w/v)
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60% inhibition at 0.5 mM
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significant inactivation
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1 mM, 66% of initial activity for decarboxylation reaction, 62% of initial activity for carboxylation reaction
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causes dissociation of the enzyme into dimers and monomers
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10 mM, complete inhibition
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1 mM, 37% inhibition of carboxylation activity, 21% inhibition of decarboxylation activity
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inactivates at 5 mM, rate is dependent on pH, glycerone phosphate protects
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3 MM, 93% inhibition
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not reversed by hydroxylamine, L-4-carboxy-4-hydroxy-2-oxoadipate strongly protects against inactivation
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strong inhibition at 5 mM
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0.5 mM, 69% inhibition
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complete inhibition at 5 mM
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10 mM, 41% residual activity
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inactivation is complete when about 1.2 His per subunit are derivatized
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1 mM, complete inactivation
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inactivation, 80% reversible by hydroxylamine within 6 h, mapping of modified histidine residues
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inhibition is reversed by hydroxylamine
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formation of a substrate-metal ion complex does not protect against inhibition
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inhibition is reversed by presence of hydroxylamine
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34-59% inhibition at 1.1 mM, dimethylally diphosphate and Mg2+ protect the soluble enzyme, but not the solubilized thylakoid membrane isozyme
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lack of substrate protection against inactivation
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modification of histidine residues, pH-dependent, hydroxylamine restores, substrates protect, no protection by 4-nitrophenyl-3-keto-1-epivalidamine, 4-nitrophenyl-beta-D-3-ketoglucoside, 4-nitrophenylvalidamine, 4-nitrophenyl-alpha-D-glucoside, methyl-alpha-D-glucoside, EGTA or CaCl2
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among the His residues of RNase A, His48 is not accessible to react with diethylpyrocarbonate
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histidine modification using diethyldicarbonate leads to reduction in heme binding and hemozoin formation
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complete loss of activity, galactose partly saves
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irreversible inhibition, saturating concentrations of substrate protect
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92% inhibition at 5 mM
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maximal inactivation at neutral pH, ´reactivation by hydroxylamine
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irreversible, presence of the competitive inhibitors cis-aconitate, trans-aconitate and cis,cis-muconate conferrs some protection
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4,4'-dihydroxychalcone protects, treatment with hydroxylamine does not restore activity. In the presence of morin hydrate, all of the histidine residues of chalcone isomerase can be modified without significant loss in catalytic activity
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reversed by hydroxylamine
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substrates protect, completely reactivated by hydroxylamine
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-
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inactivation follows pseudo-first-order kinetics with a second-order rate constant of 0.00092 /min *microM, partial protection from inactivation by either o-succinylbenzoic acid, ATP, or ATP plus Mg2+ while inactivation is completely prevented by the presence of the combination of ATP, Mg2+ and o-succinylbenzoate
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the electron accepting ability of bovine cytochrome b561 from ascorbate is selectively inhibited by the treatment with diethylpyrocarbonate
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inhibition could be reversed upon subsequent incubation with hydroxylamine
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10 mM, 0.4% residual activity; 10 mM, 0.6% residual activity
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rat liver contains two populations, DEPC-sensitive and DEPC-insensitive, of flippases, which can be in a different of DEPC sensitivity or be two different proteins
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Enzyme Kinetic Parameters

Ki Value (9 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0029
-
pH 3.0, 50°C
0.03
-
-
0.3
-
pH 6.3, 30°C
0.23
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pH 6.0, in ethanol, second order kinetics

IC50 Value (5 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.27
-
in 50 mM potassium phosphate buffer pH 7.0, at 37°C
0.092
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IC50: 0.092 mM. Preincubation at 23°C gives maximal inhibition, 75%, after 180 s. Preincubation at 13°C gives 55% inhibition after 3 min. Preincubation at 4°C results in only 35% inhibition
0.01
-
pH 7.0, 30°C
0.64
-
pH 7.8, temperature not specified in the publication
0.64
-
pH 7.8, temperature not specified in the publication

References & Links

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Links to other databases for diethyldicarbonate

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EXTERNAL LINKS
ChEBI
PubChem
UniChem