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• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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Ligand cumene hydroperoxide

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (10 results)

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Show Natural Substrate (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.9

cumene hydroperoxide + GSH = ?

396644, 396632, 396635, 396638, 396645, 396639, 396640, 396642

-

1.11.2.3

aniline + cumene hydroperoxide = ?

712359

-

1.11.2.3

aniline + cumene hydroperoxide = nitrosobenzene + ?

713295

-

1.11.2.3

linoleic acid + cumene hydroperoxide = ?

712359, 724973

-

1.11.2.3

linolenic acid + cumene hydroperoxide = linolenic acid 9,10-15,16-diepoxide + ?

724973

-

1.11.2.3

methyl 4-tolyl sulfide + cumene hydroperoxide = ?

712359

-

1.11.2.3

oleic acid + cumene hydroperoxide = ?

713275

-

1.11.2.3

oleic acid + cumene hydroperoxide = cis-9,10-epoxystearic acid + ?

712359

-

1.11.2.3

thiobenzamide + cumene hydroperoxide = ?

712359

-

1.11.2.3

8 entries

5.3.99.2

cumene hydroperoxide + 2 GSH = cumene hydroxide + GSSG + H2O

649720

-

Substrate in Enzyme-catalyzed Reactions (55 results)

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Show Substrate (55 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.11.1.11

L-ascorbate + cumene hydroperoxide = ?

711139

-

1.11.1.11

L-ascorbic acid + cumene hydroperoxide = dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O

439858, 439871, 439874, 439867

-

1.11.1.11

p-cresol + cumene-hydroperoxide = 4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + 1,1-dimethylbenzylalcohol + bis-(1-methyl-1-phenylethyl)peroxide

439877

-

1.11.1.12

glutathione + cumene hydroperoxide = ?

394878, 394871, 394880, 701060, 394864, 394865, 394868, 394875, 394882, 394876

-

1.11.1.12

GSH + cumene hydroperoxide = GSSG + ?

659647, 658606

-

1.11.1.20

thioredoxin + cumene hydroperoxide = thioredoxin disulfide + ?

687797

-

1.11.1.20

thioredoxin + cumene hydroperoxide = thioredoxin disulfide + H2O + 2-phenylpropan-2-ol

687797

-

1.11.1.11

3 entries

1.11.1.12

2 entries

1.11.1.20

2 entries

1.11.1.22

cumene hydroperoxide + NADPH + H+ = ? + NADP+ + H2O

722255

-

1.11.1.24

2 thioredoxin + cumene hydroperoxide = thioredoxin disulfide + H2O + 2-phenylpropan-2-ol

711784, 711785, 712427, 713425

-

1.11.1.24

cumene hydroperoxide + dithiothreitol = 2-phenylpropan-2-ol + oxidized dithiothreitol

684691, 745231

-

1.11.1.24

cumene hydroperoxide + reduced dithiothreitol = 2-phenylpropan-2-ol + oxidized dithiothreitol

687541

-

1.11.1.24

cumene hydroperoxide + reduced thioredoxin = 2-phenylpropan-2-ol + oxidized thioredoxin + H2O

687610, 676508, 686887, 689812, 698025

-

1.11.1.24

cumene hydroperoxide + reduced thioredoxin = ?

675585, 673665

-

1.11.1.24

cumene hydroperoxide + tryparedoxin 2 = 2-phenylpropan-2-ol + oxidized tryparedoxin 2

655661

-

1.11.1.24

thioredoxin + cumene hydroperoxide = thioredoxin disulfide + H2O + cumene hydroxide

752698

-

1.11.1.24

thioredoxin A + cumene hydroperoxide = thioredoxin A disulfide + H2O + cumene hydroxide

754009

-

1.11.1.24

8 entries

1.11.1.25

cumene hydroperoxide + reduced glutaredoxin = 2-phenylpropan-2-ol + oxidized glutaredoxin

656927

-

1.11.1.27

cumene hydroperoxide + GSH = 2-phenylpropan-2-ol + GSSG

673786

-

1.11.1.28

a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide = a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide

754057, 754070

-

1.11.1.28

cumene hydroperoxide + dihydrolipoamide = 2-phenylpropan-2-ol + lipoamide

758317

-

1.11.1.28

cumene hydroperoxide + dithiothreitol = 2-phenylpropan-2-ol + oxidized dithiothreitol

758317

-

1.11.1.7

2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + cumene hydroperoxide = ?

701107

-

1.11.1.7

AmplexRed + cumene hydroperoxide = ?

686088

-

1.11.1.7

reduced thioredoxin 1 + cumene hydroperoxide = oxidized thioredoxin 1 + cumene hydroxide

659307

-

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 4-nitrobenzenethiol = 2-phenylpropan-2-ol + 1,1'-disulfanediylbis(4-nitrobenzene) + H2O

742280

-

1.11.1.9

cumene hydroperoxide + 2 GSH = 2-phenylpropan-2-ol + GSSG + H2O

758029, 743785, 741798, 742280, 742015

-

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

cumene hydroperoxide + 2GSH = 2-phenylpropan-2-ol + GSSG + H2O

743399

-

1.11.1.9

cumene hydroperoxide + GSH = 2-phenylpropan-2-ol + GSSG + H2O

659416, 658820

-

1.11.1.9

cumene hydroperoxide + GSH = ?

396644, 396607, 396632, 690043, 396635, 396638, 396645, 690120, 396639, 396640, 396642

-

1.11.1.9

cumene hydroperoxide + H2O2 = ?

685411

-

1.11.1.9

glutathione + cumene hydroperoxide = ?

701160

-

1.11.2.3

10-cis-heptadecenoic acid + cumene hydroperoxide = 10,11-epoxyheptadecanoic acid + ?

726222

-

1.11.2.3

10-cis-pentadecenoic acid + cumene hydroperoxide = 10,11-epoxypentadecanoic acid + ?

726222

-

1.11.2.3

9-cis-hexadecenoic acid + cumene hydroperoxide = 9,10-epoxy hexadecanoic acid + ?

726222

-

1.11.2.3

aniline + cumene hydroperoxide = ?

712359

-

1.11.2.3

aniline + cumene hydroperoxide = N-phenylhydroxylamine + H2O

743492

-

1.11.2.3

aniline + cumene hydroperoxide = nitrosobenzene + ?

713295

-

1.11.2.3

linoleic acid + cumene hydroperoxide = ?

712359, 743492, 724973, 726222

-

1.11.2.3

linolenic acid + cumene hydroperoxide = ?

743492

-

1.11.2.3

linolenic acid + cumene hydroperoxide = linolenic acid 9,10-15,16-diepoxide + ?

724973

-

1.11.2.3

methyl 4-tolyl sulfide + cumene hydroperoxide = ?

712359

-

1.11.2.3

oleic acid + cumene hydroperoxide = ?

713275, 743492, 726222

-

1.11.2.3

oleic acid + cumene hydroperoxide = cis-9,10-epoxystearic acid + ?

712359

-

1.11.2.3

parathion ethyl + cumene hydroperoxide = paraoxon + ?

713275

-

1.11.2.3

thiobenzamide + cumene hydroperoxide = ?

712359

-

1.11.1.28

3 entries

1.11.1.7

3 entries

1.11.1.9

9 entries

1.11.2.3

14 entries

1.11.2.4

myristic acid + cumene hydroperoxide = ?

710994

-

1.21.4.2

dithiothreitol + cumene hydroperoxide = ?

671651

-

2.5.1.18

cumene hydroperoxide + glutathione = ?

702461, 702404, 704632, 738406, 739246, 704872, 737769, 737761

-

2.5.1.18

cumene hydroperoxide + GSH = ?

661414, 661699, 661527, 660795

-

2.5.1.18

glutathione + cumene hydroperoxide = ?

637906, 637907, 637911, 637913, 637920, 671828, 637893, 637908, 637914, 637918, 637934, 637912, 637937, 637956, 396634, 637951, 701576, 637943, 684978, 686225, 684236, 684726, 706266, 759301, 759268, 759345, 760092, 637892, 684841, 759912, 759011

-

5.3.99.2

cumene hydroperoxide + 2 GSH = cumene hydroxide + GSSG + H2O

649720

-

5.3.99.2

cumene hydroperoxide = cumene hydroxide

649654

-

2.5.1.18

3 entries

5.3.99.2

2 entries

5.3.99.3

cumene hydroperoxide + 2 GSH = cumene hydroxide + GSSG + H2O

652399

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.15.1

considerable amount of the putative Cpd II species accumulates, even at pH 7.4. By contrast, reactions with meta-chloroperbenzoic acid at pH 7.4 yield very little of the ca. 420 nm species, unless methanol is included

704713

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.49

1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h

678997

-

1.11.1.20

competitive inhibition of prostamide F synthase activity

687797

-

1.14.99.15

-

438348

-

2.5.1.18

2.5 mM, 43.3% inhibition of wild-type enzyme, 27% of mutant enzyme H144A, 50.6% of mutant enzyme V147A, 41.5% of mutant enzyme V147L, 48.1% of mutant enzyme R96A

661886

-

2.7.1.40

1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h

678997

-

4.2.1.11

1% residual activity after treatment with 17 mM cumene hydroperoxide at 50°C and pH 7 for 2 h

678997

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (24 results)

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Show Turnover Number (24 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.11.1.20

0.1

-

in 0.1 M KPB (pH 7.0), at 24°C

687797

1.11.1.20

0.1

-

pH 7.0, 24°C

687797

1.11.1.24

0.274

-

PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

687610

1.11.1.24

0.281

-

PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

687610

1.11.1.24

0.41

-

pH 7.4, 37°C, recombinant enzyme

712427

1.11.1.24

6.3

-

22°C, pH 7.0

673665

1.11.1.24

7.3

-

pH 7.0, temperature not specified in the publication, Prx197

711784

1.11.1.24

9.8

-

pH 7.0, 25°C, TpAhpC

713425

1.11.1.24

15.2

-

pH 7.0, temperature not specified in the publication, Prx231

711784

1.11.1.24

52

-

in 50 mM potassium phosphate pH 7.0, at 25°C

689812

1.11.1.20

2 entries

1.11.1.24

8 entries

1.11.1.25

0.9

-

-

656927

1.11.1.28

0.033

-

pH 7.0, 25°C

754057

1.11.1.28

0.067

-

pH 7.0, 25°C

754057

1.11.1.7

70.1

-

25°C, pH 7.0

659307

1.11.1.7

330

-

in 50 mM potassium phosphate buffer, pH 7.0

701107

2.5.1.18

0.0007

-

mutant enzyme N24A, pH and temperature not specified in the publication

759345

2.5.1.18

0.21

-

wild type enzyme, pH and temperature not specified in the publication

759345

2.5.1.18

0.27

-

isoform GSTU45, pH not specified in the publication, at 30°C

737761

2.5.1.18

0.58

-

isoform GSTU16, pH not specified in the publication, at 30°C

737761

2.5.1.18

9.03

-

at pH 7.0, temperature not specified in the publication

759011

2.5.1.18

200

-

30°C, mutant enzyme Y108A

661414

2.5.1.18

2700

-

30°C, mutant enzyme Y108W

661414

2.5.1.18

8100

-

30°C, mutant enzyme Y108F

661414

2.5.1.18

9600

-

30°C, wild-type enzyme

661414

1.11.1.28

2 entries

1.11.1.7

2 entries

2.5.1.18

9 entries

K_M Value (38 results)

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Show KM Value (38 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.11.1.12

0.0017

-

recombinant enzyme

394875

1.11.1.12

0.119

-

-

658606

1.11.1.12

608

-

-

658606

1.11.1.20

0.026

-

in 0.1 M KPB (pH 7.0), at 24°C

687797

1.11.1.20

0.026

-

pH 7.0, 24°C

687797

1.11.1.24

0.00665

-

PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

687610

1.11.1.24

0.00848

-

PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

687610

1.11.1.24

0.0096

-

pH 7.0, 25°C, TpAhpC

713425

1.11.1.24

0.0127

-

22°C, pH 7.0

673665

1.11.1.24

0.037

-

pH 7.4, 37°C, recombinant enzyme

712427

1.11.1.24

0.107

-

in 50 mM potassium phosphate pH 7.0, at 25°C

689812

1.11.1.24

0.152

-

pH 7.0, temperature not specified in the publication, Prx231

711784

1.11.1.24

0.191

-

pH 7.0, temperature not specified in the publication, Prx197

711784

1.11.1.12

3 entries

1.11.1.20

2 entries

1.11.1.24

8 entries

1.11.1.27

0.12

-

-

673786

1.11.1.28

0.052

-

pH 7.0, 25°C

754057

1.11.1.28

0.55

-

pH 7.0, 25°C

754057

1.11.1.7

0.009

-

25°C, pH 7.0

659307

1.11.1.7

3

-

in 50 mM potassium phosphate buffer, pH 7.0

701107

1.11.1.9

0.006

-

-

396607

1.11.1.9

0.111

-

-

396642

1.11.1.9

0.144

-

-

396612

1.11.1.9

0.145

-

pH 8.0, 30°C

758029

1.11.1.9

0.26

-

-

396640

1.11.1.9

7.8

-

pH 7.5, 25°C

659416

1.11.2.4

0.11

-

mutant enzyme R242A, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C

710994

1.11.2.4

0.2

-

wild type enzyme, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C

710994

1.11.2.4

0.24

-

mutant enzyme R242K, using myristic acid as cosubstrate, in 0.1 M potassium phosphate buffer (pH 6.7), at 25°C

710994

2.5.1.18

0.038

-

isoform GSTU16, pH not specified in the publication, at 30°C

737761

2.5.1.18

0.11

-

wild type enzyme, pH and temperature not specified in the publication

759345

2.5.1.18

0.252

-

at pH 6.5 and 25°C

737769

2.5.1.18

0.3

-

30°C, wild-type enzyme

661414

2.5.1.18

0.439

-

pH and temperature not specified in the publication

738406

2.5.1.18

0.9

-

30°C, mutant enzyme Y108W

661414

2.5.1.18

2.11

-

30°C, mutant enzyme Y108F

661414

2.5.1.18

4.853

-

isoform GSTU45, pH not specified in the publication, at 30°C

737761

2.5.1.18

5.3

6

mutant enzyme N24A, pH and temperature not specified in the publication

759345

2.5.1.18

8

-

30°C, mutant enzyme Y108A

661414

2.5.1.18

14.3

-

at pH 7.0, temperature not specified in the publication

759011

1.11.1.28

2 entries

1.11.1.7

2 entries

1.11.1.9

6 entries

1.11.2.4

3 entries

2.5.1.18

11 entries

References & Links

Literature References (125)

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Show Reference (125 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

394864

3978121

The selenoenzyme phospholipid hydroperoxide glutathione peroxidase

1985

Ursini, F.; Maiorini, M.; Gregolin, C.

Biochim. Biophys. Acta

839

62-70

394865

3800387

Different effects of Triton X-100, deoxycholate, and fatty acids on the kinetics of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase

1986

Maiorino, M.; Roveri, A.; Gregolin, C.; Ursini, F.

Arch. Biochem. Biophys.

251

600-605

394868

7066358

Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides

1982

Ursini, F.; Maiorino, M.; Valente, M.; Ferri, L.; Gregolin, C.

Biochim. Biophys. Acta

710

197-211

394871

2804065

Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases

1989

Zhang, L.; Maiorini, M.; Roveri, A.; Ursini, F.

Biochim. Biophys. Acta

1006

140-143

394875

11104683

Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity

2000

Wilkinson, S.R.; Meyer, D.J.; Kelly, J.M.

Biochem. J.

352

755-761

394876

8436014

Purification of phospholipid hydroperoxide glutathione peroxidase from bovine retina

1993

Lam, K.W.; Wang, L.; Hong, B.S.; Treble, D.

Curr. Eye Res.

12

9-15

394878

7851631

Purification of a cytosolic enzyme from human liver with phospholipid hydroperoxide glutathione peroxidase activity

1994

Chambers, S.J.; Lambert, N.; Williamson, G.

Int. J. Biochem.

26

1279-1286

394880

7524677

Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes

1994

Roveri, A.; Maiorino, M.; Nisii, C.; Ursini, F.

Biochim. Biophys. Acta

1208

211-221

394882

8706688

A selenium-containing phospholipid-hydroperoxide glutathione peroxidase in Schistosoma mansoni

1996

Maiorino, M.; Roche, C.; Kiess, M.; Koenig, K.; Gawlik, D.; Matthes, M.; Naldini, E.; Pierce, R.; Flohe, L.

Eur. J. Biochem.

238

838-844

396607

6882790

Selenium-dependent and non-selenium-dependent glutathione peroxidases in human tissue extracts

1983

Charmagnol, F.; Sinet, P.M.; Jerome, H.

Biochim. Biophys. Acta

759

49-57

396612

6986175

Purification and immunohistochemical localization of rat liver glutathione peroxidase

1980

Yoshimura, S.; Komatsu, N.; Watanabe, K.

Biochim. Biophys. Acta

621

130-137

396632

8428933

Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI

1993

Chu, F.F.; Doroshow, J.H.; Esworthy, R.S.

J. Biol. Chem.

268

2571-2576

396634

-

Characterization of glutathione transferases and glutathione peroxidases in pea (Pisum sativum)

1996

Edwards, R.

Physiol. Plant.

98

594-604

396635

9030530

Subunit Ya-specific glutathione peroxidase activity toward cholesterol 7-hydroperoxides of glutathione S-transferases in cytosols from rat liver and skin

1997

Hiratsuka, A.; Yamane, H.; Yamazaki, S.; Ozawa, N.; Watabe, T.

J. Biol. Chem.

272

4763-4769

396638

12215683

Nuclear and nucleolar glutathione reductase, peroxidase, and transferase activities in livers of male and female Fischer-344 Rats

2002

Rogers, L.K.; Gupta, S.; Welty, S.E.; Hansen, T.N.; Smith, C.V.

Toxicol. Sci.

69

279-285

396639

8926102

Expression and characterization of glutathione peroxidase activity in the human blood fluke Schistosoma mansoni

1996

Mei, H.; Thakur, A.; Schwartz, J.; Lo Verde, P.T.

Infect. Immun.

64

4299-4306

396640

8193675

Purification and characterization of a glutathione peroxidase from the Aloe vera plant

1994

Sabeh, F.; Wright, T.; Norton, S.J.

Enzyme Protein

47

92-98

396642

11926531

Glutathione peroxidase from the liver of Japanese sea bass Lateolabrax japonicus

2002

Nagai, T.; Yukimoto, T.; Suzuki, N.

Z. Naturforsch. C

57

172-176

396644

8842471

Purification and characterisation of chicken liver monomeric glutathione peroxidase

1996

Miyazaki, S.; Motoi, Y.

Br. Poult. Sci.

37

651-660

396645

7986075

Demonstration of glutathione peroxidase in rat liver peroxisomes and its intraorganellar distribution

1994

Singh, A.K.; Dhaunsi, G.S.; Gupta, M.P.; Orak, J.K.; Asayama, K.; Singh, I.

Arch. Biochem. Biophys.

315

331-338

438348

188654

Kinetic studies on a 4-methoxybenzoate O-demethylase from Pseudomonas putida

1977

Bernhardt, F.H.; Nastainczyk, W.; Seydewitz, U.

Eur. J. Biochem.

72

107-115

439858

6772104

Purification and some properties of L-ascorbic-acid-specific peroxidase in Euglena gracilis Z

1980

Shigeoka, S.; Nahana, Y.; Kitaoka, S.

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The AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosis

2000

Hillas, P.J.; del Alba, F.S.; Oyarzabal, J.; Wilks, A.; Ortiz De Montellano, P.R.

J. Biol. Chem.

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18801-18809

754070

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The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics

2003

Koshkin, A.; Nunn, C.M.; Djordjevic, S.; Ortiz de Montellano, P.R.

J. Biol. Chem.

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758029

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A thioredoxin-dependent glutathione peroxidase (OsGPX5) is required for rice normal development and salt stress tolerance

2017

Wang, X.; Fang, G.; Yang, J.; Li, Y.

Plant Mol. Biol. Rep.

35

333-342

758317

28391181

Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi

2017

Meireles, D.; Domingos, R.; Gaiarsa, J.; Ragnoni, E.; Bannitz-Fernandes, R.; da Silva Neto, J.; de Souza, R.; Netto, L.

Redox Biol.

12

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759011

27639582

Biochemical characterization of the detoxifying enzyme glutathione transferase P1-1 from the camel Camelus dromedarius

2016

Perperopoulou, F.; Ataya, F.S.; Fouad, D.; Malik, A.; Saeed, H.M.; Labrou, N.E.

Cell Biochem. Biophys.

74

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Biochemical functions of glutathione S-transferase family of Salix babylonica

2020

Zhuge, X.L.; Xu, H.; Xiu, Z.J.; Yang, H.L.

Front. Plant Sci.

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Effects of substrate-binding site residues on the biochemical properties of a tau class glutathione S-transferase from Oryza sativa

2019

Yang, X.; Wei, J.; Wu, Z.; Gao, J.

Genes (Basel)

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759345

30928378

Identification of key residues for activities of atypical glutathione S-transferase of Ceriporiopsis subvermispora, a selective degrader of lignin in woody biomass, by crystallography and functional mutagenesis

2019

Osman, W.H.W.; Mikami, B.; Saka, N.; Kondo, K.; Lin, M.I.; Nagata, T.; Katahira, M.

Int. J. Biol. Macromol.

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759912

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Purification of fat body glutathione S-transferase from the desert locust Schistocerca gregaria investigation of flavonoid inhibitory effects on enzyme activity

2019

Hamed, R.; Maharem, T.; Guneidy, R.; Emam, M.; Abdel Karim, G.

Physiol. Entomol.

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760092

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Functional role of Tyr12 in the catalytic activity of novel zeta-like glutathione S-transferase from Acidovorax sp. KKS102

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Shehu, D.; Alias, Z.

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Links to other databases for cumene hydroperoxide

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