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Ligand dithionitrobenzoic acid

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Basic Ligand Information

Molecular Structure
Picture of dithionitrobenzoic acid (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C14H8N2O8S2
dithionitrobenzoic acid
KIUMMUBSPKGMOY-UHFFFAOYSA-L
Synonyms:
3,3'-disulfanediylbis(6-nitrobenzoic acid), 3,3'-dithiobis(6-nitrobenzoate), 3,3'-dithiobis(6-nitrobenzoic acid), 5'-dithio-bis-(2-nitrobenzoic acid), 5,5 dithiobis(2-nitrobenzoate), 5,5 dithiobis(2-nitrobenzoic acid), 5,5'-dithio(bis-2-nitrobenzoic acid), 5,5'-dithio-2,2' dinitro-dibenzoate, 5,5'-dithio-bis(2-nitrobenzoate), 5,5'-dithio-bis(2-nitrobenzoic acid), 5,5'-dithio-bis-(2-nitrobenzoate), 5,5'-dithio-bis-(2-nitrobenzoic acid), 5,5'-dithio-bis-2-nitrobenzoic acid, 5,5'-dithio-bis-[2-nitrobenzoic acid], 5,5'-dithiobis(2-nitro-benzoate), 5,5'-dithiobis(2-nitro-benzoic acid), 5,5'-dithiobis(2-nitrobenzoate), 5,5'-dithiobis (2-nitrobenzoate), 5,5'-dithiobis(2-nitrobenzoic) acid, 5,5'-dithiobis(2-nitrobenzoic)acid, 5,5'-dithiobis (2-nitrobenzoic acid), 5,5'-dithiobis(2-nitrobenzoicacid), 5,5'-dithiobis(2-nitrobenzoic acid), 5,5'-dithiobis(nitrobenzoic acid), 5,5'-dithiobis-(2-nitrobenzoate), 5,5'-dithiobis-(2-nitrobenzoic acid), 5,5'-dithiobis-2-nitrobenzoate, 5,5'-dithiobis-2-nitrobenzoic acid, 5,5'-dithiobis-nitrobenzoate, 5,5'-dithiobis-[2-nitrobenzoic acid], 5,5'-dithiobis 2-nitrobenzoic acid, 5,5'-dithiobis[2-nitrobenzoic acid], 5,5'-dithiol-bisnitrobenzoate, 5,5'-dithionitrobenzoic acid, 5,5'dithiobis(2-nitrobenzoic acid), 5,5'dithiobis-(2-nitrobenzoic acid), 5,5-dithio-bis(2-nitrobenzoic acid), 5,5-dithio-bis 2-nitrobenzoic acid, 5,5-dithiobis(2-nitrobenzoate), 5,5-dithiobis(2-nitrobenzoic acid), 5,5-dithiobis-(2-nitrobenzoate), 5-5'-dithiobis(2-nitrobenzoic acid), 5-5'-dithiobis-(2-nitrobenzoic acid), 5-5'dithiobis-(2-nitrobenzoate), 5-[(3-carboxy-4-nitrophenyl)dithio]-2-nitrobenzoic acid, Bis(3-carboxy-4-nitrophenyl)disulfide, dithio-bis-nitrobenzoic acid, dithiobis(2-nitrobenzoic acid), dithiobis-(2-nitrobenzoic acid), Dithiobis-nitrobenzoate, Dithiobisnitrobenzoate, Dithiobisnitrobenzoic acid, Dithionitrobenzoate, DTNB

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (31 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
5,5'-dithiobis(2-nitrobenzoic acid) + NADH = ?
show the reaction diagram
-
trypanothione + 5,5'-dithiobis-(2-nitrobenzoic acid) = trypanothione disulfide + thionitrobenzoate
show the reaction diagram
-
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH = 4-nitrobenzenethiol + NADP+
show the reaction diagram
-
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+ = 2-nitro-5-thiobenzoate + NAD+
show the reaction diagram
-
DTNB + NADPH = ?
show the reaction diagram
-
5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+ = ? + NAD+
show the reaction diagram
-
5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+ = 2-nitro-5-thiobenzoate + NADP+
show the reaction diagram
-
5,5'-dithiobis(2-nitrobenzoic acid) + O2 = ? + H2O
show the reaction diagram
-
GSH + 5,5'-dithiobis(nitrobenzoic acid) = ?
show the reaction diagram
-
acetyl-CoA + 5,5'-dithiobis-(2-nitrobenzoic acid) = CoA + 5-thio-2-nitrobenzoic acid
show the reaction diagram
-
5,5'-dithiobis-2-nitrobenzoic acid + H2O = ?
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (2 results)

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EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (16 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.5 mM, 2.7fold increase in oxaloacetate reduction activity
-
retains its maximum activity when preincubated at pH 7.0 or 8.5
-
i.e. DTNB, substrate 1-O-alk-1’-enyl-2-acyl-sn-glycerol
-
low concentrations lead to increase of activity at a physiological pH, higher concentrations lead to complete inactivation
-
0.5 mM, 11% activation of isozyme IT II, 24% inhibition of isozyme IT I
-
1 mM, 10% inhibition
-
0.1 mM, relative activity 138%
-
stimulates
-

Inhibitor in Enzyme-catalyzed Reactions (634 results)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
0.25 mM, 90% inhibition, 67% activity is recovered after incubation with 1 mM, 2-mercaptoethanol or dithieothreitol for 15 min
-
1 mM, 50% inhibition after 4.6 min, half-inactivation time increases to 7.0 min in the presence of 20 mM D-pantoate
-
0.05 mM, 80% inhibition
-
complete inactivation at 0.24 mM
-
complete inhibition at 1 mM concentration
-
complete inhibition at 1 mM
-
D-carnitine dehydrogenase, 1 mM, complete inactivation
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0.15 mM, 63% inhibition
-
1 h at 0.1 mM inhibits 98% of enzyme activity
-
1 mM, 50% inactivation
-
0.005 mM, 50% loss of activity after 1 h
-
1 mM, room temperature, pH 9.0, 50% inactivation
-
reacts with first 4 sulfhydryl groups of enzyme, inhibition is completely reversible upon addition of reducing agents, NAD+ and NADH protect against inactivation
-
1 mM, 15% inhibition
-
complete inhibition at 2 mM
-
1 mM, 47% inhibition
-
complete inhibition at 0.4 mM
-
modification of thiol groups of activated enzyme results in rapid inactivation of both activities, modification of the residues of nonactivated enzyme has small effects on the enzyme activities, pH-dependence and kinetics of modifications/inactivation
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chemical modification of cysteine residues, 8 residues modified by 0.5 mM. 16 residues modified in the presence of 2% sodium dodecyl sulfate. 20 residues modified by 1 mM and in the presence of urea, EDTA, NaBH4
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1 mM, complete inhibition
-
cysteine-directed reagent, 1 mM, complete inhibition
-
complete inhibition at 0.5 mM
-
1 mM, 0.7% residual activity
-
1 mM, complete inhibition
-
40% inhibition at 1 mM, irreversible
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at least 90% inhibition at 0.2 mM
-
67% residual activity at 1 mM
-
mild inhibition, dehydrogenase
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94% inhibition at 0.5 mM
-
1 mM, 0.7% residual activity
-
Mn-SOD
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complete inhibition at 1 mM
-
weak inhibition
-
NAD+, NADP+ prevent inhibition
-
0.005 mM, 50% loss of activity after 1 h
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reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
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partial
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0.01 mM, 29% residual activity
-
the effect of the thiol reagent DTNB on the native enzyme structure of the wild type enzyme and the mutants is examined
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1.1 mM, 35% inhibition
-
inhibits the regeneration of the enzyme-substrates complex, but has no effect on the photoconversion of the preformed complex
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i.e. DTNB, inhibition can be prevented by preincubation with NADPH, thus a SH-group is involved in cofactor binding
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extremely potent inhibitor
-
thiol-modifying agent
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inactivates by modification of sulfhydryl groups and loss of FAD
-
0.5 mM, 70% inhibition, 40% inhibition after preincubation with 10 mM L-lysine, 98.5% inhibition after preincubation with 1 mM NAD+
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complete inactivation
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almost complete inhibition in presence of NAD+, 40% inhibition in presence of L-lysine
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0.01 mM, 95% inhibition
-
complete inhibition
-
90% inhibition at 0.012 mM
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sulfhydryl reagents restore activity
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0.13 mM, complete inhibition
-
with 0.1 mM 28.8% activity
-
0.001 M, 38% inhibition
-
28% inhibition at 1 mM
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inhibits holoenzyme formation from apoenzyme and FAD, can be prevented by addition of 2-mercaptoethanol
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in absence of FAD or NADPH
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1 mM, 7 min, 50% loss of activity
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0.1 mM
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0.66 mM, 33% inhibition after 30 min
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above 0.1 mM
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2 mol DTNB per mol enzyme causes complete inactivation
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complete loss of activity, second-order kinetics, inactivation is reversed by dithiothreitol, inactivation involves the modification of one thiol group per mol of dimeric enzyme
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strong inhibition
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0.01 mM, rapid inactivation, inactivation half-life: approx. 15 s, both acetyl-CoA and malonyl-CoA protect
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inhibits the acetyl-CoA/CO exchange reaction
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phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation
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complete inhibition of LPCAT in wild-type and in recombinant heterologous yeast microsomes
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50% inhibition of ACAT1 at 0.01 mM
-
0.5 mM 76% activity
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activity inhibited above 2 mM
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strong inhibition
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30% inhibition at 10 mM
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enzyme inactivation, lauroyl-CoA or palmitoyl-CoA protects
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inactivation is partially prevented by prior addition of donor or acceptor substrate and by sulfhydryl reducing agents. 1 mM inhibits 94%
-
77% inactivation at 1 mM
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52% inhibition at 0.5 mM
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strong inhibition at 1.25 mM
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0.2 mM, 85% inhibition
-
98.7% inhibition at 10 mM
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10 mM, 88.7% inhibition
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4 mM, 87% inhibition after 30 min
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0.01 mM, 50% inhibition, 0.1 mM, 97% inhibition
-
potent inhibition, activity is restored to more than 95% with 0.1 mM DTT
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5 mM, pH 8.0, 50% inhibition
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complete inhibition at 0.01 M; i.e. DTNB
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95% loss of activity
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reduces specific activity by 50%
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0.06 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
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substrates protect
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inactivation reversed by dithiothreitol
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substrates partially protect against inactivation
-
0.03 mM, 10 min, 95% inhibition
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DTT prevents inhibition
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0.009 mM, 50% inhibition
-
0.1 mM, almost complete inactivation after 5 min, phosphomevalonate partially protects, inactivation is reverted by 2-mercaptoethanol or dithiothreitol
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general thymidylate kinase inhibitor
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binds to SH-group in the active center
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0.05 mM, rapid decrease in activity of wild-type enzyme (t1/2: 20 s), truncated enzyme del396-573 retains more than 97% of its activity after 30 min
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progressive loss of activity with increasing amounts of DTNB. Thus, sulfhydryl groups are involved in maintaining the active state of the enzyme or are involved in the mechanism
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substrate 1,2-diacylglycerol
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50% inhibition at 0.023 mM
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2-mercaptoethanol protects
-
80% inhibition at 10 mM
-
completely inactivated, activity can not be recovered by adding dithiothreitol
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inactivation, the peripheral site ligand propidium accelerates inactivation in the wild type ChE2, but retards inactivation in the F312I mutant
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complete inhibition
-
0.5 mM, 30-40% inhibition
-
the enzyme is relatively insensitive to sulfhydryl reagents
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3 mM, 100% inhibition
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
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inhibits more rapidly at pH 7 than at pH 8.5
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13.26% residual activity at 0.1% (w/v); 39.83% residual activity at 0.1% (w/v); 9.1% residual activity at 0.1% (w/v)
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25-40% inhibition at 0.1 mM, 85-90% inhibition at 5 mM
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0.2 mM, 80% inhibition of Mg2+-dependent enzyme, no inhibition of Mg2+-independent enzyme
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97% inhibition of the catalytic fragment of CNP1 in a time- and dose-dependent manner, kinetics, fully reversed by excess dithiothreitol or 2-mercaptoethanol, inhibition is attributable to steric effects of modification of Cys-236 and Cys-314 by the inhibitor
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16.3% inhibition at 25 mM
-
66% inhibition of isozyme MG4, 41% inhibition of isozyme MG6
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42% inhibition at 10 mM, no inhibition at 1 mM
-
rapid inactivation by modification of an essential thiol group
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53% residual activity at 10 mM
-
69% residual activity at 1 mM
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1.5 mM, 81% residual activity
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11% inhibition by 1 mM
-
52-57% inhibition at 1-5 mM
-
5 mM, 49% inhibition
-
enzyme activity is lost when a mixed disulfide is formed between 5,5'-dithiobis(2-nitrobenzoic acid) and Cys95, the same mixed disulfide at Cys67 reduces activity by 50%. Normal activity can be restored when the enzyme is treated with dithiothreitol
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64% inhibition at 50 mM
-
reversible, synergism with pyridoxal 5'-phosphate or phenylglyoxal
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65% residual activity
-
with 20 micromol DTNB the activity is 5% after 10 min
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0.5 mM: 50% inhibition of mitochondrial, 42% inhibition of microsomal enzyme
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1 mM, 66% loss of activity
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weak
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10 mM, 41% inhibition
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0.1 mM, 15 min, 78% residual activity in absence of substrate S-pantetheine-3-pyruvate, 33% residual activity in presence of the substrate S-pantetheine-3-pyruvate
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25% inhibition at 1 mM
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2 mM, 50% inhibition
-
0.1 mM
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could be reactivated with dithiothreitol
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1 mM, 23% loss of activity
-
inhibits the reaction slightly
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11% inhibition at concentration of 5.0 mM
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compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal. The enzyme is protected from inactivation by inclusion of the substrate N1-(5'-phosphoribosyl)adenosine 5'-monophosphate, while Mg2+, a metal required for catalytic activity, enhanced the rate of inactivation
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reaction with thiol groups, leads to a decrease of 20-30% in Vmax
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strong
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slight inhibition
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1 mM, 40% inhibition
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1 mM, complete inhibition
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1 mM, 100% inhibition
-
glyoxylate and pyruvate protect
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50% residual activity at 0.3 mg/ml
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34.9% inhibition at 1 mM
-
inhibition is primarily due to modification of Cys186. DTNB-treated C186S remains fully active
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1 mM: 97% inhibition
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weak inhibition
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presence of ATP, MgCl2, and dithiothreitol prevent rapid sulfhydryl modification. With the enzyme of a gramicidin S non-producing and phenylalanine racemization-lacking mutant the substrate protection against rapid sulfhydryl modification is not detected
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complete inhibition at 1 mM
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30 nM, complete inhibition
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reactivation in presence of mercaptoethanol, protection by UDPglucose or UDPgalactose, inactivated enzyme retains the dimeric structure and NAD+ is not dissociated from the protein moiety
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inhibition is reversed by incubation of the inactivated enzyme with 10 mM dithiothreitol
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irreversibly inactivates
-
-
-
-
-
-
-
1 mM, 92% inhibition
-
E2, no effect on isoenzyme E3
-
-
-
less than 10% residual activity at 0.1 mM
-
-
-
slight effect
-
complete inhibition at 0.02 mM
-

Metals and Ions (1 result)

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EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
slightly activating at 0.1 mM
-

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (80 results)

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EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE

KM Value (73 results)

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EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
3.3
-
-

Ki Value (5 results)

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EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.63
-
pH 6.8, 37 C
0.25
-
pH 8.0, 37°C
0.015
-
-
0.6
-
-
0.5
-
mitochondrial

IC50 Value (3 results)

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EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
3
-
at 25°C and pH 9
0.05
-
significant inhibition, IC50: 0.05 mM
0.0018
-
at pH 8.5 and 25°C

References & Links

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