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Ligand 5-thio-2-nitrobenzoate

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Substrate (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.9

cumene hydroperoxide + 2 2-nitro-5-sulfanylbenzoic acid = 2-phenylpropan-2-ol + 3,3'-disulfanediylbis(6-nitrobenzoic acid) + H2O

742280

-

1.11.1.9

cumene hydroperoxide + 2-nitro-5-sulfanylbenzoic acid = 2-phenylpropan-2-ol + 3,3'-disulfanediylbis(6-nitrobenzoic acid) + H2O

741798

-

1.11.1.9

tert-butylhydroperoxide + 3-carboxy-4-nitrobenzenethiol = ?

685492

-

1.11.1.9

3 entries

1.8.3.2

2-nitro-5-thiobenzoic acid + O2 = ? + H2O

393051

-

2.5.1.47

beta-chloro-L-alanine + 2-nitro-5-thiobenzoate = ?

661281

-

2.5.1.47

O3-acetyl-L-serine + 2-nitro-5-thiobenzoate = ?

662157, 661281

-

2.5.1.47

O-acetyl-L-Ser + 5-mercapto-2-nitrobenzoate = S-(3-carboxy-4-nitrophenyl)-L-cysteine + ?

637374

-

2.5.1.47

5-thio-2-nitrobenzoate + O-acetyl-L-serine = acetate + ?

701920

-

2.5.1.47

O-acetyl-L-serine + 5-thio-2-nitrobenzoate = ? + acetate

684707, 685397, 686675

-

2.5.1.47

O3-acetyl-L-serine + 5-thio-2-nitrobenzoate = ? + acetate

684707, 685397, 701920

-

2.5.1.47

6 entries

Product in Enzyme-catalyzed Reactions (22 results)

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Show Product (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.12

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

0

-

1.8.1.14

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

0

-

1.8.1.7

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

0

-

1.8.1.8

DTNB + NAD(P)H = 5-mercapto-2-nitrobenzoate + NAD(P)+

0

-

1.8.1.8

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

0

-

1.8.1.9

5,5'-dithiobis(2-nitrobenzoic acid) + dithiothreitol = 2-nitro-5-thiobenzoate + oxidized dithiothreitol

0

-

1.8.1.9

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

0

-

1.8.1.9

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

0

-

1.8.1.9

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

0

-

1.8.1.9

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

0, 394949, 394952

-

1.8.1.9

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

0

-

1.8.1.9

5,5'-dithio-bis(2-nitrobenzoic acid) + NADH + H+ = 5'-thionitrobenzoic acid + NAD+

0

-

1.8.1.9

5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+ = 5'-thionitrobenzoic acid + NADP+

0

-

1.8.1.9

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

0

-

1.8.1.9

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

0

-

1.8.1.9

5,5'-dithiobis(2-nitrobenzoicacid) + NADPH + H+ = 5'-thionitrobenzoic acid + NADP+

0

-

1.8.1.9

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

0

-

1.8.1.B1

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

0

-

1.8.1.B1

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

0

-

1.8.1.B1

5,5'-dithio-bis(2-nitrobenzoic acid) + NADPH + H+ = 5'-thionitrobenzoic acid + NADP+

0

-

1.8.1.8

2 entries

1.8.1.9

12 entries

1.8.1.B1

3 entries

2.3.1.183

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

0

-

3.4.21.9

thiobenzyl benzyloxycarbonyl-L-lysinate + H2O = 3-carboxy-4-nitrothiophenoxide + ?

0

-

Inhibitor in Enzyme-catalyzed Reactions (5 results)

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Show Inhibitors (5 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.103

40fold molar excess, gradual 99% loss of enzyme activity

285710

-

1.11.2.2

competitive inhibitor of myeloperoxidase

711124

-

1.8.4.11

binds specifically to the sulfenic acid reaction intermediate

658215

-

1.8.4.12

binds specifically to the sulfenic acid reaction intermediate

658215

-

5.3.4.1

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

691481

-

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

1.20.4.1

1rxe, 3D-view

Enzyme Kinetic Parameters

K_M Value (11 results)

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Show KM Value (11 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.3.2

100

-

-

393051

2.5.1.47

0.018

-

mutant W50Y, pH 7.0, 20°C

662157

2.5.1.47

0.049

-

wild-type, pH 7.0, 20°C

662157

2.5.1.47

0.061

-

mutant W161Y, pH 7.0, 20°C

662157

2.5.1.47

0.07

-

K120Q mutant with 9fold decrease compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C

685397

2.5.1.47

0.07

-

mutant H52A, pH 6.5

685397

2.5.1.47

0.12

-

pH 7.0, 50°C

661281

2.5.1.47

0.6

-

wild type, 100 mM HEPES, pH 7.0, 0.5 mM O3-acetyl-L-serine, 25°C

684707, 685397

2.5.1.47

0.6

-

wild-type, pH 7.0

684707

2.5.1.47

2.5

-

H152A mutant with 4.1fold increase compared to wild type, 100 mM MES, pH 6.5, 0.5 mM O3-acetyl-L-serine, 25°C

684707

2.5.1.47

2.5

-

mutant H52A, pH 6.5

684707

2.5.1.47

10 entries

References & Links

Literature References (17)

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Show Reference (17 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285710

2104757

The sulfhydryl content of L-threonine dehydrogenase from Escherichia coli K-12: relation to catalytic activity and Mn2+ activation

1990

Craig, P.A.; Dekker, E.E.

Biochim. Biophys. Acta

1037

30-38

393051

-

Sulphadryl oxidase: properties and application

1986

Swaisgood, H.E.

Enzyme Microb. Technol.

2

265-272

394949

11796729

Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability

2002

Missirlis, F.; Ulschmid, J.K.; Hirosawa-Takamori, M.; Gronke, S.; Schafer, U.; Becker, K.; Phillips, J.P.; Jackle, H.

J. Biol. Chem.

277

11521-11526

394952

10447675

Mitochondrial thioredoxin reductase in bovine adrenal cortex its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine

1999

Watabe, S.; Makino, Y.; Ogawa, K.; Hiroi, T.; Yamamoto, Y.; Takahashi, S.Y.

Eur. J. Biochem.

264

74-84

637374

8518286

Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants

1993

Tai, C.H.; Nalabolu, S.R.; Jacobson, T.M.; Minter, D.E.; Cook, P.F.

Biochemistry

32

6433-6442

658215

15680231

The enzymology and biochemistry of methionine sulfoxide reductases

2005

Boschi-Muller, S.; Olry, A.; Antoine, M.; Branlant, G.

Biochim. Biophys. Acta

1703

231-238

661281

15308337

Biochemical characterization of a thermostable cysteine synthase from Geobacillus stearothermophilus V

2004

Saavedra, C.P.; Encinas, M.V.; Araya, M.A.; Perez, J.M.; Tantalean, J.C.; Fuentes, D.E.; Calderon, I.L.; Pichuantes, S.E.; Vasquez, C.C.

Biochimie

86

481-485

662157

12813039

Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability

2003

Campanini, B.; Raboni, S.; Vaccari, S.; Zhang, L.; Cook, P.F.; Hazlett, T.L.; Mozzarelli, A.; Bettati, S.

J. Biol. Chem.

278

37511-37519

684707

18275838

Role of histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction

2008

Tai, C.H.; Rabeh, W.M.; Guan, R.; Schnackerz, K.D.; Cook, P.F.

Arch. Biochem. Biophys.

472

115-125

685397

18243146

Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium

2008

Tai, C.H.; Rabeh, W.M.; Guan, R.; Schnackerz, K.D.; Cook, P.F.

Biochim. Biophys. Acta

1784

629-637

685492

18163571

Functional mimicry of the active site of glutathione peroxidase by glutathione imprinted selenium-containing protein

2008

Liu, L.; Mao, S.Z.; Liu, X.M.; Huang, X.; Xu, J.Y.; Liu, J.Q.; Luo, G.M.; Shen, J.C.

Biomacromolecules

9

363-368

686675

17894825

High resolution structure and catalysis of O-acetylserine sulfhydrylase isozyme B from Escherichia coli

2007

Zocher, G.; Wiesand, U.; Schulz, G.E.

FEBS J.

274

5382-5389

691481

19091013

Molecular docking studies of dithionitrobenzoic acid and its related compounds to protein disulfide isomerase: computational screening of inhibitors to HIV-1 entry

2008

Gowthaman, U.; Jayakanthan, M.; Sundar, D.

BMC Bioinformatics

9 Suppl 12

S14

701920

19501038

(31)P NMR studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium

2009

Guan, R.; Nimmo, S.A.; Schnackerz, K.D.; Cook, P.F.

Arch. Biochem. Biophys.

487

85-90

711124

9359420

Thiocyanate and chloride as competing substrates for myeloperoxidase

1997

van Dalen, C.J.; Whitehouse, M.W.; Winterbourn, C.C.; Kettle, A.J.

Biochem. J.

327

487-492

741798

-

Solvent-dependent catalytic behavior of telluride-containing guest artificial glutathione peroxidase using cumene hydroperoxide and 3-carboxyl-4-nitrobenzenethiol as substrates

2015

Jiao, S.; Yin, Y.; Zhang, R.; Zhong, S.; Wang, X.; Zhang, L.; Yang, L.

Asian J. Chem.

27

2665-2668

742280

25683962

Construction of a artificial glutathione peroxidase with temperature-dependent activity based on a supramolecular graft copolymer

2015

Yin, Y.; Jiao, S.; Wang, Y.; Zhang, R.; Shi, Z.; Hu, X.

ChemBioChem

16

670-676

Links to other databases for 5-thio-2-nitrobenzoate

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Show Links (1 entry)

ChEBI

PubChem

-