Ligand 5,5'-dithiobis(2-nitrobenzoic acid)

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Basic Ligand Information

Molecular Structure
Picture of 5,5'-dithiobis(2-nitrobenzoic acid) (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C14H8N2O8S2
5,5'-dithiobis(2-nitrobenzoic 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(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, Dithionitrobenzoic acid, DTNB

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (31 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
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
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
glyoxylate + acetyl-CoA + 5,5'-dithiobis-(2-nitrobenzoic acid) = 5-mercapto-2-nitrobenzoic acid + ?
-

Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (16 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (632 results)

COMMENTARY
EC NUMBER
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
-
56% inhibition at 0.05 mM
-
complete inhibition at 1 mM
-
complete inhibition at 1 mM concentration
-
complete inhibition at 1 mM
-
D-carnitine dehydrogenase, 1 mM, complete inactivation
-
0.15 mM, 63% inhibition
-
1 h at 0.1 mM inhibits 98% of enzyme activity
-
1 mM, 50% inactivation
-
inhibition of decarboxylation activity
-
sulfhydryl reagent, rapid and complete loss of activity, presence of Mg2+ or Mn2+ enhances inactivation rate
-
0.005 mM, 50% loss of activity after 1 h
-
DTNB
-
Ellman's reagent
-
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
-
1 mM, 35% inhibition
-
complete inhibition at molar excess of reagents in relation to alcohol oxidase 20:1
-
complete inhibition at 2 mM
-
1 mM, 47% inhibition
-
40% inhibition at 0.1 mM
-
5 mM, 80% residual activity, APX 1, 24% residual activity, APX 2
-
96% inhibition at 0.5 mM
-
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
-
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
-
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, 100% inhibition of hydroxylation reaction, EC 1.14.11.26
-
1 mM, no residual activity
-
reactivation by dithiothreitol
-
1 mM, complete inhibition
-
0.1 mM, 5 min incubation, complete inactivation
-
0.5 mM, 87% loss of activity
-
completely
-
40% inhibition at 1 mM, irreversible
-
at least 90% inhibition at 0.2 mM
-
67% residual activity at 1 mM
-
mild inhibition, dehydrogenase
-
94% inhibition at 0.5 mM
-
0.01 mM, 30% inhibition, reactivation by dithiothreitol
-
1 mM, 100% inhibition of expandase reaction, EC 1.14.20.1
-
1 mM, 0.7% residual activity
-
Mn-SOD
-
89% inhibition at 10 mM
-
inhibits the activity of the whole system
-
complete inhibition at 1 mM
-
30% inhibition at 1 mM, presence of NAD+, no conversion from dehydrogenase to oxidase activity detectable
-
45.4% inhibition of hypoxanthine oxidation at 1 mM
-
conversion from of NAD+-dependent to O2-dependent activity without any effect on the total activity
-
conversion of dehydrogenase type D to oxidase type O due to modification of a limited number of critical sulfhydryl groups
-
conversion of dehydrogenase type D to oxidase type O, can be prevented and reversed by dithioerythritol
-
weak inhibition
-
NAD+, NADP+ prevent inhibition
-
0.005 mM, 50% loss of activity after 1 h
-
reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione
-
0.01 mM, 66% residual activity
-
partial
-
0.1 mM causes 100% inhibition at 30°C
-
1 mM, 80% inhibition
-
1.0 mM, 90% inhibition
-
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
-
1.1 mM, 35% inhibition
-
i.e. DTNB, inhibits wild-type enzyme and mutant C145S
-
inhibits DD1 and DD3, inhibition can be overcome by androsterone for DD1 and by benzenedihydrodiol for DD3, not vice versa
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
-
inhibits the regeneration of the enzyme-substrates complex, but has no effect on the photoconversion of the preformed complex
-
i.e. DTNB, inhibition can be prevented by preincubation with NADPH, thus a SH-group is involved in cofactor binding
-
extremely potent inhibitor
-
thiol-modifying agent
-
30-40% inhibition at 1 mM
-
significant inhibition, IC50: 0.05 mM
-
inactivates by modification of sulfhydryl groups and loss of FAD
-
inactivates, conformation-change type inhibition, the presence of the substrate provides marked protection
-
inhibition is reversed by addition of dithiothreitol or dithionite
-
7% inhibition with 0.01 M and 40% inhibition with 0.1 mM
-
0.5 mM, 70% inhibition, 40% inhibition after preincubation with 10 mM L-lysine, 98.5% inhibition after preincubation with 1 mM NAD+
-
complete inactivation
-
almost complete inhibition in presence of NAD+, 40% inhibition in presence of L-lysine
-
inactivation via blocking of the only two Cys residues, Cys144 in helix alpha7a of domain I, the substrate-binding domain, and Cys320 in a loop that connects betak and alpha13 in domain II, the coenzyme-binding domain
-
0.17 mM, complete inhibition
-
0.17 mM: 26% inhibition
-
0.01 mM, 95% inhibition
-
complete inhibition
-
90% inhibition at 0.012 mM
-
sulfhydryl reagents restore activity
-
0.13 mM, complete inhibition
-
with 0.1 mM 28.8% activity
-
0.1 mM, 60% inhibition
-
0.57 mM, 98% inhibition
-
no inactivation in the presence of NADH
-
0.001 M, 38% inhibition
-
28% inhibition at 1 mM
-
inhibits holoenzyme formation from apoenzyme and FAD, can be prevented by addition of 2-mercaptoethanol
-
0.02 mM, 51% inhibition, 92% inhibition in the presence of 2 mM Mg2+
-
NADPH, NADP+, or NADP site-specific inhibitors protect from inactivation
-
in absence of FAD or NADPH
-
1 mM, 7 min, 50% loss of activity
-
1 mM, 67% inhibition, 10 mM, complete inhibition
-
1 mM, 23% inhibition
-
inactivation is caused by a modification of one Cys per subunit, reactivation by dithiothreitol or KCN. NADPH partially protects from inactivation, 9,10-phenanthrenequinone enhances the modification
-
0.1 mM
-
0.66 mM, 33% inhibition after 30 min
-
above 0.1 mM
-
2 mol DTNB per mol enzyme causes complete inactivation
-
reversed by addition of dithiothreitol
-
substrate does not protect against inactivation
-
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
-
complete inactivation at alkaline pH
-
strong inhibition
-
0.15mM, 90% inhibition in sonicated vesicles
-
1 mM, 20-30% inhibition of activity on palmitoyl-CoA, complete inhibition of activity on other acyl-CoAs
-
1 mM, 77% inhibition
-
inhibition of microsomal enzyme, mitochondrial enzyme is not inhibited
-
0.1 mM, 33% residual activity
-
0.01 mM, rapid inactivation, inactivation half-life: approx. 15 s, both acetyl-CoA and malonyl-CoA protect
-
inhibits the acetyl-CoA/CO exchange reaction
-
phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation
-
11% inhibition at 1 mM
-
i.e. DTNB, complete inhibition, DTT protects
-
complete inhibition of LPCAT in wild-type and in recombinant heterologous yeast microsomes
-
50% inhibition of ACAT1 at 0.01 mM
-
0.025 mM, 82% inhibition
-
5 mM, moderate; i.e. DTNB
-
i.e. DTNB
-
i.e. DTNB; no inhibition
-
not (10 mM)
-
83% inhibition at 1.4 mM of the activity in plasma
-
partly reversible by dithioerythritol
-
0.5 mM 76% activity
-
activity inhibited above 2 mM
-
strong inhibition
-
99% inhibition
-
complete inhibition
-
covalent binding to palmitoyl residues, malonyl-CoA protects
-
0.4 mM, 87% inhibition
-
low but significant inhibition
-
1 mol per mol enzyme, 85% inactivation, not reversed by glutathione
-
irreversible, carbobenzoxy-Phe protects
-
reversed by dithiothreitol
-
no inhibition
-
weak
-
Ellman's reagent
-
residual activity 51%
-
inactivation of the glyoxysomal isozyme, half-life: approx. 1 min, not mitochondrial isozyme
-
inactivation, half-lifes at 0.4 mM: 2.8 min for CS 1, 50 min for CS II
-
no inhibition
-
30% inhibition at 10 mM
-
enzyme inactivation, lauroyl-CoA or palmitoyl-CoA protects
-
1 mM, weak
-
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
-
52% inhibition at 0.5 mM
-
strong inhibition at 1.25 mM
-
0.2 mM, 85% inhibition
-
98.7% inhibition at 10 mM
-
10 mM, 88.7% inhibition
-
4 mM, 87% inhibition after 30 min
-
0.01 mM, 50% inhibition, 0.1 mM, 97% inhibition
-
potent inhibition, activity is restored to more than 95% with 0.1 mM DTT
-
1 mM, 92% inactivation
-
non-competitive
-
5 mM, pH 8.0, 50% inhibition
-
complete inhibition at 0.01 M; i.e. DTNB
-
inactivation reversed by dithiothreitol
-
irreversible inhibition
-
95% loss of activity
-
reduces specific activity by 50%
-
inactivation, protection by MgADP-, AMP, 2-deoxyglucose, glucose, and mannose probably via binary complex formation, no protection by glucose 6-phosphate, slight protection by MgATP2-
-
0.06 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione
-
complete inactivation, 3 mM ATP protects
-
DTNB, Ellman’s reagent, almost complete inhibition at 0.0045 mM
-
substrates protect
-
0.1 mM, 74% inhibition
-
0.5 mM, 62% inhibition of isoenzyme 1 and 33% inhibition of isoenzyme 2
-
inactivation reversed by dithiothreitol
-
modest inhibitory activity
-
substrates partially protect against inactivation
-
0.03 mM, 10 min, 95% inhibition
-
DTT prevents inhibition
-
only gradual loss of activity after more than 10 min, pH-dependent
-
most potent at 0.001 mM
-
59% inhibition at 0.002 mM
-
complete loss of activity
-
nucleotide ligands protect, e.g. MgATP2-, MgADP-, Mg-beta,gamma-methylene-adenosine-5'-triphosphate, Mg-beta,gamma-imido-adenosine-5'-triphosphate
-
rabbit muscle enzyme
-
reversible
-
less than 5% residual activity at 0.1 mM
-
modification and inactivation course with DTNB and the reactivation course of DTNB-modified enzyme. Modified enzyme can be reactivated by an excess concentration of dithiothreitol in a monophasic kinetic course
-
the arginine kinase modified by DTNB can be fully reactivated by dithiothreitol in a monophasic kinetic course. This reactivation can be slowed down in the presence of ATP, suggesting that the essential Cys is located near the ATP binding site
-
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
-
DTT reverses
-
DTT reverses; not: mitochondrial enzyme
-
DTT reverses; strong for muscle enzyme, less effective with dystrophic muscle or liver enzymes
-
muscle enzyme
-
not
-
not: liver enzyme
-
not: mitochondrial enzyme; only cytosolic
-
general thymidylate kinase inhibitor
-
binds to SH-group in the active center
-
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
-
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
-
substrate 1,2-diacylglycerol
-
50% inhibition at 0.023 mM
-
2-mercaptoethanol protects
-
rapid inactivation of wild-type enzyme and mutant C196S, less rapid inactivation of mutant C28S, CoA, linked to the enzyme, allows the rapid modification of Cys28 by 5,5'-dithiobis(2-nitrobenzoicacid), reflecting a conformational change of SCOT upon formation of the thioester, overview
-
slow inactivation of the free enzyme by the thiol-modifying reagent DTNB, wild-type SCOT and C196S are both inactivated by DTNB with more rapid kinetics in the presence of succinyl- or acetoacetyl-CoA (about 70-80% inactivation in 25 min) than in the absence of acyl-CoA (only about 30% inactivation in 25 min and about 40-50% inactivation in 50 min), the rate of C28S inactivation by DTNB is accelerated to a much lesser extent by succinyl- or acetoacetyl-CoA, and C28S is inactivated less rapidly than wild-type SCOT or C196S, the inactivation with DNTB is reversible, the enzyme can be reactivated by adding dithiothreitol, kinetics of inactivation by DNTB
-
80% inhibition at 10 mM
-
completely inactivated, activity can not be recovered by adding dithiothreitol
-
competitive inhibition of LIII, 30% inhibition at 5 mM
-
can be reversed by dithiothreitol
-
plasmalogen-specific PLA2
-
69% inhibition at 2 mM
-
inactivation, the peripheral site ligand propidium accelerates inactivation in the wild type ChE2, but retards inactivation in the F312I mutant
-
complete inhibition
-
0.5 mM, 30-40% inhibition
-
the recombinant enzyme is completely inhibited at 1 mM
-
the enzyme is relatively insensitive to sulfhydryl reagents
-
48% inhibition at 0.001 mM
-
above 0.3 mM; above 0.3 mM
-
above 0.3 mM
-
50% inhibition at 0.15 mM
-
75% inhibition at 0.3 mM, complete inhibition at 1.3 mM
-
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
-
inhibits more rapidly at pH 7 than at pH 8.5
-
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)
-
25-40% inhibition at 0.1 mM, 85-90% inhibition at 5 mM
-
0.2 mM, 80% inhibition of Mg2+-dependent enzyme, no inhibition of Mg2+-independent enzyme
-
50 nM, 50% inhibition, incorporation of 1 mol per mol of subunit leads to complete inactivation, phosphate or dithiothreitol protects
-
inhibition is potentiated by MgCl2
-
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
-
16.3% inhibition at 25 mM
-
86% inhibition at 0.1 mM
-
complete inhibition at 0.01 mM after 10 min
-
strong inhibition at 1 mM
-
10 mM, 35% inhibition
-
10 mM, complete inhibition
-
55.2% inhibition at 5 mM
-
inhibition of isozymes AI-1 and AI-2, and AII, at 5 mM
-
2% residual activity at 10 mM
-
about 8% residual activity at 2 mM
-
chemical modification of the exposed sulfhydryl groups in beta-amylase from unmalted seeds with 5,5'-dithiobis-(2-nitrobenzoic acid) results in loss of activity. In the beta-amylase from malted seed the 5,5'-dithiobis-(2-nitrobenzoic acid) chemical modification results in the increase in the KM from 2.81 to 4.14 mg/ml
-
weak
-
66% inhibition of isozyme MG4, 41% inhibition of isozyme MG6
-
8.67% inhibitory effect at 1 mM
-
complete inhibition at 0.2 mM
-
nearly complete inhibition at 5 mM
-
0.5 mM, 24% inhibition of isozyme IT I, 11% activation of isozyme IT II
-
42% inhibition at 10 mM, no inhibition at 1 mM
-
50% inhibition, reversed by glycogen
-
DTNB
-
rapid inactivation by modification of an essential thiol group
-
53% residual activity at 10 mM
-
69% residual activity at 1 mM
-
59% inhibition at 1 mM at pH 7.4
-
86% inhibition at 1 mM at pH 7.4
-
inhibition is through covalent modifiction of residue C105
-
the enzyme is fully reactivated when incubated with tris(2-carboxyethyl)-phosphine hydrochloride
-
1 mM, 74.89% enzyme inhibition
-
1.5 mM, 81% residual activity
-
1 mM, 57% inhibition
-
1.0 mM inhibitor, 54% inhibition, 2.5 mM inhibitor, 87% inhibition
-
13% residual activity at 2.5 mM, beta-mercaptoethanol and dithiothreitlol completely restores enzyme activity
-
reactivation by DTT or 2-mercaptoethanol
-
partial
-
activity is restored by 2-mercaptoethanol
-
11% inhibition by 1 mM
-
complete inhibition at 5 mM
-
enzyme from brain
-
52-57% inhibition at 1-5 mM
-
100% inhibition at 1 mM
-
95% inhibition at 0.1 mM, substrate Leu-2-N-naphthylamine
-
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
-
64% inhibition at 50 mM
-
reversible, synergism with pyridoxal 5'-phosphate or phenylglyoxal
-
1 mM: 70% inhibition, in presence of 2 mM Ca2+: 30% inhibition
-
inhibitory, partially prevented by addition of Ca2+
-
65% residual activity
-
0.02 mM: complete inhibition; Ellman's reagent
-
Ellman's reagent
-
with 20 micromol DTNB the activity is 5% after 10 min
-
15-18% inhibition of wild-type, MM6 and MM8, 35% inhibition of the MM15 activity
-
preincubated for 30 min, remaining activity in presence of 1 mM DTT
-
0.5 mM: 50% inhibition of mitochondrial, 42% inhibition of microsomal enzyme
-
1 mM, 66% loss of activity
-
weak
-
10 mM, 41% inhibition
-
2 mM, 100% inhibition
-
2 mM, slight inhibition
-
specific activity 0.39, relative activity 58%
-
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
-
25% inhibition at 1 mM
-
2 mM, 50% inhibition
-
0.1 mM
-
could be reactivated with dithiothreitol
-
1 mM, 23% loss of activity
-
inhibits the reaction slightly
-
11% inhibition at concentration of 5.0 mM
-
1 mM, dextran-conjugated enzyme and native enzyme retain 46.7% and 4.9% of their initial activities
-
the reaction of 1 sulfhydryl group with 0.3 mM 5,5'-dithiobis-(2-nitrobenzoic acid) has a half-life of about 50 min at pH 8
-
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
-
reaction with thiol groups, leads to a decrease of 20-30% in Vmax
-
45% inhibition at 1 mM
-
complete inhibition at 1 mM
-
complete loss of activity due to modification of Cys165
-
strong
-
5 mM, complete inhibition
-
complete inhibition at 5 mM
-
slight inhibition
-
1 mM
-
0.1 mM, 50.3% inhibition at pH 4.6, irreversible
-
0.001 mM, approx. 80% inhibition of ODC activity after 8 min
-
0.01 mM, 98% inhibition
-
0.01 mM, 99% inhibition
-
inhibits wild-type enzyme, but not C306A or C306S mutant enzymes
-
10 mM, 60% inhibition
-
presence of substrate ATP or mevalonate 5-diphosphate protects effectively against inactivation
-
0.5 mM, 1.5% residual activity
-
0.5 mM, 14.5% residual activity
-
1 mM, 40% inhibition
-
1 mM, complete inhibition
-
1 mM, 100% inhibition
-
glyoxylate and pyruvate protect
-
50% residual activity at 0.3 mg/ml
-
34.9% inhibition at 1 mM
-
0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
-
reversible loss of activity
-
inhibition is primarily due to modification of Cys186. DTNB-treated C186S remains fully active
-
1 mM: 97% inhibition
-
complete
-
1 mM 54%, loss of activity
-
1 mM, complete
-
complete inhibition in the deamination reaction
-
protection of reduced enzyme by Cd2+ against inactivation
-
reversible with dithiothreitol, folate protects
-
8 of the 12 -SH groups in native enzyme react reversibly. Cystathionine at high concentrations, partially relieves the inhibition
-
irreversible
-
weak inhibition
-
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
-
1 mM, complete inhibition, pH 7.0, 30°C, 30 min
-
35% inhibition at 1 mM
-
complete inhibition at 1 mM
-
30 nM, complete inhibition
-
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
-
0.1 mM, more than 95% inhibition
inhibition is reversed by incubation of the inactivated enzyme with 10 mM dithiothreitol
-
about 50% inhibition at about 0.05 mM
-
derivatizes four of the five Cys per subunit of dimeric protein, resulting in inactivation and dissociation of the dimer to stable monomers
-
no inhibition
-
no effect at 1 mM
-
0.0049 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
-
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
-
irreversibly inactivates
-
reversed by DTT
-
1 mM, 92% inhibition
-
E2, no effect on isoenzyme E3
-
-
-
less than 10% residual activity at 0.1 mM
-
-
-
1 mM
-
the major effect on ACVS activity is exerted by thiol-blocking agents, which almost completely inhibited the activity at 1 mM concentration, confirming the importance of thiol groups in ACVS activity
-
Cys289 is the only amino acid residue reactive with DTNB. Modification of Cys289 with DTNB results in complete loss of the catalytic activity
-
inhibition of ADP-ATP exchange reaction, no effect on tripeptide synthesis
-
slight effect
-
complete inhibition at 0.02 mM
-
flippase activity for 1-oleoyl-2-[6-(7-nitrol-2-1,3-benzonadiol-4-yl)amino]-sn-glycerophosphoethanolamine is inhibited by 80% at 20 mM 5,5'-dithiobis(2-nitrobenzoic acid), flippase activity for 1-oleoyl-2-[6-(7-nitrol-2-1,3-benzonadiol-4-yl)amino]-sn-glycerophosphocholine is inhibited by 60% at 20 mM 5,5'-dithiobis(2-nitrobenzoic acid)
-

Metals and Ions (1 result)

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

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (69 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
1.2
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
16
-
purified, recombinant, dimeric enzyme
106.3
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
2.53
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
1.2
-
truncated mutant, pH 7.2, temperature not specified in the publication
1.23
-
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
15.6
-
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
2.4
-
purified, recombinant, tetrameric enzyme
33.08
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
48.42
-
pH 8.0, 30°C
10.8
-
pH 7.8, 37°C
11.96
-
pH 7.5, 50°C
87.8
-
pH 7.5
0.62
-
pH 7.4
5.5
-
pH 7.2, temperature not specified in the publication
10.7
-
-
0.62
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
21.6
-
pH 7.2, temperature not specified in the publication
0.88
-
TrxR-16 mutant K29R
0.52
-
TrxR-16 mutant K29R/H108Y
0.075
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
0.018
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
0.55
-
wild type enzyme
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
30.02
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
wild type enzyme, in TE buffer, at 20°C
70.3
-
wild-type enzyme
4.58
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.23
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
0.25
-
pH 7, 25°C
2.62
-
chimeric enzyme mutant, partly from Salmonella typhimurium AhpF protein
50.3
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
16
-
full-length Drosophila enzyme with C-terminal sequence SCCS
1.6
-
full-length mouse enzyme with C-terminal sequence GCUG
20.83
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
1.77
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
18.73
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
8.28
-
mutant U498C
0.012
-
mutant enzyme Y116T, in TE buffer, at 20°C
47.72
-
mutant enzyme H509A
0.16
-
mutant enzyme H509Q
0.233
-
mutant enzyme Y116I, in TE buffer, at 20°C
49.87
-
pH 7.8, 25°C
0.17
-
pH 7.0, 25°C, wild-type enzyme
118
-
wild-type, pH 7.0, temperature not specified in the publication
55
-
-
1.2
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
8.16
-
at pH 7.8 and 25°C
0.3
-
pH 7.4, 25°C
16
-
wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
16
-
cytosolic isoform, pH 7.8, temperature not specified in the publication
1.85
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
4
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6
-
mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6
-
mitochondrial isoform, pH 7.8, temperature not specified in the publication
12.6
-
mutant C519S, pH 7.0, temperature not specified in the publication
12
-
mutant C574S, pH 7.0, temperature not specified in the publication
10.2
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
8
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
6
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
16
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
5
-

KM Value (73 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
-
3.3
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
0.71
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
0.114
-
purified, recombinant, dimeric enzyme
0.2156
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
0.53
-
truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C
0.71
-
truncated mutant, pH 7.2, temperature not specified in the publication
11.9
-
truncated mutant enzyme (missing residues CUG from the C-terminus) so that Gly521 is the C-terminal amino acid
2.72
-
truncated enzyme (missing residues CCS from the C-terminus) so that Ser488 is the C-terminal amino acid
0.92
-
purified, recombinant, tetrameric enzyme
0.139
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
0.83
-
pH 8.0, 30°C
0.238
-
pH 7.8, 37°C
0.28
-
pH 7.5, 50°C
0.032
-
pH 7.4
0.7
-
pH 7.2, temperature not specified in the publication
pH 7, 25°C
0.75
-
pH 7.0, 25°C
1.7
-
truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0
4.1
-
TrxR-16 mutant K29R
3.3
-
TrxR-16 mutant K29R/H108Y
4.5
-
TrxR-16 mutant K29R/H108Y/A119N/V478E
1.1
-
TrxR-16, TrxR lacking the last 16 C-terminal amino acids
2.4
-
wild type enzyme
wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C
0.09
-
wild type enzyme, in 50 mM potassium phosphate at pH 7.0
wild type enzyme, in TE buffer, at 20°C
0.094
-
wild-type enzyme
0.212
-
with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.4
-
with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C
1.1
-
mitochondrial TrxR1 isoform
0.41
-
cytosolic TrxR1 isoform
0.38
-
full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C
0.114
-
full-length Drosophila enzyme with C-terminal sequence SCCS
0.17
-
full-length mouse enzyme with C-terminal sequence GCUG
0.47
-
in 50 mM potassium phosphate buffer (pH 7.0), at 22°C
0.463
-
in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication
0.0186
-
isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
0.105
-
isoform TrxR2, in 50 mM Tris-HCl, 1 mM EDTA, pH 7.0, at 37°C
0.39
-
mutant U498C
0.7
-
mutant enzyme Y116T, in TE buffer, at 20°C
0.0906
-
mutant enzyme Y116I, in TE buffer, at 20°C
0.0971
-
mutant enzyme H509Q
0.05
-
mutant enzyme H509A
0.147
-
pH 7.5, 25°C
0.00434
-
wild-type, pH 7.0, temperature not specified in the publication
0.038
-
mutant enzyme U597C, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.107
-
-
0.71
-
at 25°C in 0.1 M potassium phosphate (pH 7.4)
0.1451
-
at pH 7.8 and 25°C
0.0345
-
wild type enzyme, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.319
-
cytosolic isoform, pH 7.8, temperature not specified in the publication
0.088
-
pH 7.4, 25°C
0.114
-
mutant enzyme C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.043
-
mutant enzyme C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.23
-
pH 7.8, 25°C
0.049
-
mutant enzyme C520A/C574A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.187
-
mutant enzyme C520A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.375
-
pH not specified in the publication, temperature not specified in the publication
0.00434
-
mitochondrial isoform, pH 7.8, temperature not specified in the publication
0.045
-
mutant enzyme C31S, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.169
-
mutant C519S, pH 7.0, temperature not specified in the publication
0.034
-
mutant C574S, pH 7.0, temperature not specified in the publication
0.033
-
mutant enzyme C28A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.23
-
mutant enzyme C28A/C31A, in 0.1 M potassium phosphate buffer and 10 mM EDTA (pH 7.4) at 25°C
0.406
-

Ki Value (5 results)

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

IC50 Value (3 results)

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

References & Links