Ligand dithionitrobenzoic acid

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Basic Ligand Information

Molecular Structure

C₁₄H₈N₂O₈S₂

dithionitrobenzoic acid

KIUMMUBSPKGMOY-UHFFFAOYSA-L

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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-nitro benzoic 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-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-nitro)benzoate, dithiobis(2-nitrobenzoic acid), dithiobis-(2-nitrobenzoic acid), Dithiobis-nitrobenzoate, Dithiobisnitrobenzoate, Dithiobisnitrobenzoic acid, Dithionitrobenzoate, DTNB

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (33 results)

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1.18.1.4

5,5'-dithiobis(2-nitrobenzoic acid) + NADH = ?

437841

1.20.4.3

5,5'-dithiobis-(2-nitrobenzoic acid) + mycoredoxin = ?

767236, 767235

1.8.1.12

trypanothione + 5,5'-dithiobis-(2-nitrobenzoic acid) = trypanothione disulfide + thionitrobenzoate

688813, 686095, 685567, 684759, 685553, 686809, 700087, 697339

1.8.1.13

5,5'-dithiobis(2-nitrobenzoic acid) + NADPH = 4-nitrobenzenethiol + NADP+

392951

1.8.1.14

5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+ = 2-nitro-5-thiobenzoate + NAD+

DTNB + NADPH = ?

5,5'-dithiobis-(2-nitrobenzoic acid) + NADH + H+ = ? + NAD+

724002

1.8.1.7

5,5'-dithiobis(2-nitrobenzoic acid) + NADPH + H+ = 2-nitro-5-thiobenzoate + NADP+

5,5'-dithiobis(2-nitrobenzoic acid) + O2 = ? + H2O

393041, 393052, 393040, 765289

1.8.4.2

GSH + 5,5'-dithiobis(nitrobenzoic acid) = ?

725470

2.3.1.183

acetyl-CoA + 5,5'-dithiobis-(2-nitrobenzoic acid) = CoA + 5-thio-2-nitrobenzoic acid

702740

2.3.2.B14

5,5'-dithiobis(2-nitrobenzoic acid) = ? + thionitrobenzoate

777259

3.2.2.30

5,5'-dithiobis-2-nitrobenzoic acid + H2O = ?

727044

Product in Enzyme-catalyzed Reactions (2 results)

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1.11.1.9

2 entries

Activator in Enzyme-catalyzed Reactions (16 results)

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1.1.1.38

0.5 mM, 2.7fold increase in oxaloacetate reduction activity

286689

2.3.1.137

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

644413

2.8.2.9

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 (642 results)

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1.1.1.103

0.25 mM, 90% inhibition, 67% activity is recovered after incubation with 1 mM, 2-mercaptoethanol or dithieothreitol for 15 min

285716

1.1.1.106

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

286053

1.1.1.17

complete inactivation at 0.24 mM

complete inhibition at 1 mM concentration

complete inhibition at 1 mM

741249

1.1.1.254

D-carnitine dehydrogenase, 1 mM, complete inactivation

0.15 mM, 63% inhibition

286534

1.1.1.312

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

639110

1.1.1.48

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

654782

1.12.99.6

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

688848

1.13.11.15

1 mM, complete inhibition

cysteine-directed reagent, 1 mM, complete inhibition

649382

1.13.11.74

complete inhibition at 0.5 mM

722603

1.13.12.19

1 mM, 0.7% residual activity

1 mM, complete inhibition

40% inhibition at 1 mM, irreversible

438859

1.14.13.40

at least 90% inhibition at 0.2 mM

67% residual activity at 1 mM

715329

1.14.14.108

mild inhibition, dehydrogenase

438763

1.14.14.21

94% inhibition at 0.5 mM

1 mM, 0.7% residual activity

Mn-SOD

complete inhibition at 1 mM

weak inhibition

strong inhibition

NAD+, NADP+ prevent inhibition

285521

1.2.1.102

0.005 mM, 50% loss of activity after 1 h

reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione

partial

0.01 mM, 29% residual activity

288042

1.2.1.8

the effect of the thiol reagent DTNB on the native enzyme structure of the wild type enzyme and the mutants is examined

671741

1.2.4.1

1.1 mM, 35% inhibition

inhibits the regeneration of the enzyme-substrates complex, but has no effect on the photoconversion of the preformed complex

393835

1.3.1.38

i.e. DTNB, inhibition can be prevented by preincubation with NADPH, thus a SH-group is involved in cofactor binding

extremely potent inhibitor

390850

1.3.2.3

thiol-modifying agent

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+

391499

1.4.1.16

complete inactivation

391512

1.4.1.18

almost complete inhibition in presence of NAD+, 40% inhibition in presence of L-lysine

0.01 mM, 95% inhibition

complete inhibition

90% inhibition at 0.012 mM

392119

1.5.1.23

sulfhydryl reagents restore activity

13436

1.5.1.28

0.13 mM, complete inhibition

94167

1.5.1.3

392245, 392256, 392263

1.5.1.30

with 0.1 mM 28.8% activity

0.001 M, 38% inhibition

28% inhibition at 1 mM

394961

1.5.3.6

inhibits holoenzyme formation from apoenzyme and FAD, can be prevented by addition of 2-mercaptoethanol

in absence of FAD or NADPH

1 mM, 7 min, 50% loss of activity

0.1 mM

0.66 mM, 33% inhibition after 30 min

above 0.1 mM

2 mol DTNB per mol enzyme causes complete 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

strong inhibition

complete inhibition at 1 mM

0.01 mM, rapid inactivation, inactivation half-life: approx. 15 s, both acetyl-CoA and malonyl-CoA protect

486450

2.3.1.169

inhibits the acetyl-CoA/CO exchange reaction

390459

2.3.1.192

phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation

complete inhibition of LPCAT in wild-type and in recombinant heterologous yeast microsomes

757540

2.3.1.26

50% inhibition of ACAT1 at 0.01 mM

487286, 487287, 487298, 487300, 487308, 487309

0.5 mM 76% activity

487398, 487406, 487407, 487413, 487421

2.3.1.76

activity inhibited above 2 mM

strong inhibition

30% inhibition at 10 mM

736357

2.3.3.4

enzyme inactivation, lauroyl-CoA or palmitoyl-CoA protects

inactivation is partially prevented by prior addition of donor or acceptor substrate and by sulfhydryl reducing agents. 1 mM inhibits 94%

658191

2.4.1.11

77% inactivation at 1 mM

488431

2.4.1.212

52% inhibition at 0.5 mM

659171

2.4.1.219

strong inhibition at 1.25 mM

488935

2.4.1.304

0.2 mM, 85% inhibition

722531

2.4.1.5

98.7% inhibition at 10 mM

10 mM, 88.7% inhibition

4 mM, 87% inhibition after 30 min

638368

2.4.3.7

0.01 mM, 50% inhibition, 0.1 mM, 97% inhibition

638771

2.5.1.16

potent inhibition, activity is restored to more than 95% with 0.1 mM DTT

5 mM, pH 8.0, 50% inhibition

489953

2.5.1.7

complete inhibition at 0.01 M; i.e. DTNB

95% loss of activity

reduces specific activity by 50%

0.06 mM, 80% inhibition of PFK III, reversed by 2-mercaptoethanol, dithiothreitol or reduced glutathione

substrates protect

inactivation reversed by dithiothreitol

substrates partially protect against inactivation

0.03 mM, 10 min, 95% inhibition

641798

2.7.1.94

DTT prevents inhibition

0.009 mM, 50% inhibition

645147

2.7.4.2

0.1 mM, almost complete inactivation after 5 min, phosphomevalonate partially protects, inactivation is reverted by 2-mercaptoethanol or dithiothreitol

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

712335

2.7.8.1

substrate 1,2-diacylglycerol

50% inhibition at 0.023 mM

645838

2.8.2.24

2-mercaptoethanol protects

80% inhibition at 10 mM

133840

3.1.1.24

completely inactivated, activity can not be recovered by adding dithiothreitol

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 enzyme is relatively insensitive to sulfhydryl reagents

3 mM, 100% inhibition

738425

3.1.3.11

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

170763

3.1.3.15

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

134811

3.1.3.4

0.2 mM, 80% inhibition of Mg2+-dependent enzyme, no inhibition of Mg2+-independent enzyme

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

208558, 208559, 208568

3.2.1.2

3 entries

3.2.1.20

66% inhibition of isozyme MG4, 41% inhibition of isozyme MG6

42% inhibition at 10 mM, no inhibition at 1 mM

rapid inactivation by modification of an essential thiol group

53% residual activity at 10 mM

705482

3.2.1.B1

69% residual activity at 1 mM

1.5 mM, 81% residual activity

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

648143

3.4.24.28

64% inhibition at 50 mM

733130

3.4.24.40

reversible, synergism with pyridoxal 5'-phosphate or phenylglyoxal

46% residual activity at 1 mM

769105

3.5.1.24

65% residual activity

with 20 micromol DTNB the activity is 5% after 10 min

0.5 mM: 50% inhibition of mitochondrial, 42% inhibition of microsomal enzyme

209214

3.5.1.73

1 mM, 66% loss of activity

weak

10 mM, 41% inhibition

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

658224

3.5.1.B18

25% inhibition at 1 mM

2 mM, 50% inhibition

0.1 mM

could be reactivated with dithiothreitol

209375

3.5.3.1

1 mM, 23% loss of activity

753041

3.5.3.2

inhibits the reaction slightly

209437

3.5.3.20

11% inhibition at concentration of 5.0 mM

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

strong

slight inhibition

4425, 4426, 4427, 4433, 4434, 4440, 4443, 4445

1 mM, 40% inhibition

1 mM, complete inhibition

1 mM, 100% inhibition

glyoxylate and pyruvate protect

5247

4.1.3.3

50% residual activity at 0.3 mg/ml

34.9% inhibition at 1 mM

inhibition is primarily due to modification of Cys186. DTNB-treated C186S remains fully active

1 mM: 97% inhibition

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

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

inhibition is reversed by incubation of the inactivated enzyme with 10 mM dithiothreitol

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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1.14.14.22

slightly activating at 0.1 mM

736529

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (80 results)

K_M Value (73 results)

3.3

K_i Value (5 results)

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2.5.1.47

0.63

pH 6.8, 37 C

637334

3.1.1.3

0.25

pH 8.0, 37°C

0.015

0.6

0.5

mitochondrial

209214

IC₅₀ Value (3 results)

at 25°C and pH 9

0.05

significant inhibition, IC50: 0.05 mM

390956

2.7.2.3

0.0018

at pH 8.5 and 25Â°C

762312

References & Links

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Show Reference (869 entries)

Links to other databases for dithionitrobenzoic acid

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UniChem

Ligand dithionitrobenzoic acid

Basic Ligand Information

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (33 results)

Product in Enzyme-catalyzed Reactions (2 results)

Activator in Enzyme-catalyzed Reactions (16 results)

Inhibitor in Enzyme-catalyzed Reactions (642 results)

Metals and Ions (1 result)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (80 results)

KM Value (73 results)

Ki Value (5 results)

IC50 Value (3 results)

References & Links

Literature References (869)

Links to other databases for dithionitrobenzoic acid

k_cat Value (Turnover Number) (80 results)

K_M Value (73 results)

K_i Value (5 results)

IC₅₀ Value (3 results)