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Ligand menadiol

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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Show Natural Product (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.5.1

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione = 1-(beta-D-ribofuranosyl)nicotinamide + menadiol

0

-

1.3.5.3

protoporphyrinogen IX + 3 menadione = protoporphyrin IX + 3 menadiol

0

-

1.5.1.53

5-methyltetrahydrofolate + oxidized menadione = 5,10-methylenetetrahydrofolate + reduced menadione

0

-

1.6.5.2

NADH + H+ + 2-methyl-1,4-naphthoquinone = NAD+ + 2-methyl-1,4-naphthoquinol

0

-

1.6.5.2

NADPH + H+ + 2-methyl-1,4-naphthoquinone = NADP+ + 2-methyl-1,4-naphthoquinol

0

-

1.6.5.2

2 entries

Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Substrate (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.10.5.1

5-(aziridin-1-yl)-2,4-dinitrobenzamide + menadiol = ? + reduced menadiol

671708

-

1.10.5.1

N-benzylnicotinamide + menadiol = ?

658434

-

1.10.5.1

N-ribosylnicotinamide + menadiol = ?

658434

-

1.10.5.1

nicotinamide riboside + menadiol = dihydronicotinamide riboside + menadione

711729

-

1.10.5.1

tetrahydrofolate + menadiol = ?

658434

-

1.5.1.54

5,10-methylenetetrahydrofolate + menadiol = 5-methyltetrahydrofolate + menadione

761422, 761372

-

1.5.1.54

NAD+ + menadiol = NADH + H+ + menadione

760562

-

1.10.5.1

5 entries

1.5.1.54

2 entries

1.7.5.1

nitrate + 2-methyl-1,4-naphthoquinol = nitrite + 2-methyl-1,4-naphthoquinone + H2O

696212, 696201, 697207, 700372, 697708, 696200

-

2.4.1.17

UDP-D-glucuronate + menadiol = UDP + mendadiol 1-O-beta-D-glucuronoside

702016

-

2.4.1.17

UDP-D-glucuronate + menadiol = UDP + mendadiol 4-O-beta-D-glucuronoside

702016

-

2.4.1.17

2 entries

2.5.1.111

dimethylallyl diphosphate + menadione hydroquinol = diphosphate + vitamin MK1

758689

-

7.1.1.4

menadiol + oxidized dithiothreitol = menadione + dithiothreitol

720484

-

7.1.1.5

menadiol + O2 + n H+[side 1] = menadione + H2O + n H+[side 2]

713979, 713980

-

7.1.1.7

2 menadiol + O2 + 4 H+[side 1] = 2 menadione + 2 H2O + 4 H+[side 2]

727727

-

7.1.1.7

menadiol + O2 + H+[side 1] = menadione + H2O + H+[side 2]

743792

-

7.1.1.7

2 entries

Product in Enzyme-catalyzed Reactions (76 results)

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Show Product (76 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.145

menadione + NADPH = menadiol + NADP+

0

-

1.1.1.328

menadione + NADPH + H+ = menadiol + NADP+

0

-

1.1.5.3

sn-glycerol 3-phosphate + menadione = glycerone phosphate + reduced menadione

0

-

1.1.5.9

D-glucose + menadione = D-glucono-1,5-lactone + menadiol

0

-

1.1.98.4

2-methyl-1,4-naphthoquinone + reduced coenzyme F420 = 2-methyl-1,4-naphthoquinol + oxidized coenzyme F420

0

-

1.10.5.1

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + menadione = 1-(beta-D-ribofuranosyl)nicotinamide + menadiol

0

-

1.10.5.1

1-carbamoylmethyl-3-carbamoyl-1,4-dihydropyrimidine + menadione = 1-carbamoylmethyl-3-carbamoylpyrimidine + menadiol

0

-

1.10.5.1

dihydronicotinamide riboside + menadione = ribosyl nicotinamide + menadiol

0

-

1.10.5.1

menadione + dihydronicotinamide riboside = menadiol + nicotinamide riboside

0

-

1.10.5.1

N-benzyldihydronicotinamide + menadione = N-benzylnicotamide + menadiol

0

-

1.10.5.1

N-benzyldihydronicotinamide + menadione = N-benzylnicotinamide + menadiol

0

-

1.10.5.1

N-methyldihydronicotinamide + menadione = N-methylnicotinamide + menadiol

0

-

1.10.5.1

reduced N-methyldihydronicotinamide + menadione = ? + menadiol

0

-

1.10.5.1

reduced N1-(benzyl)-nicotinamide + menadione = N1-(benzyl)-nicotinamide + menadiol

0

-

1.10.5.1

reduced N1-(n-propyl)-nicotinamide + menadione = N1-(n-propyl)-nicotinamide + menadiol

0

-

1.10.5.1

10 entries

1.17.5.1

phenylacetyl-CoA + H2O + menadione = phenylglyoxylyl-CoA + menadiol

644661

-

1.18.1.1

NADH + 2-methyl-1,4-naphthoquinone = NAD+ + 2-methyl-1,4-naphthoquinol

0

-

1.3.5.1

succinate + menadione = fumarate + menadiol

0

-

1.3.5.2

(S)-dihydroorotate + menadione = orotate + menadiol

0

-

1.3.5.2

dihydroorotate + menadione = orotate + reduced menadione

0

-

1.3.5.2

2 entries

1.3.5.3

protoporphyrinogen IX + 3 menadione = protoporphyrin IX + 3 menadiol

0

-

1.3.98.1

S-dihydroorotate + menadione = orotate + menadiol

0

-

1.3.99.6

3,12-dioxo-5beta-cholan-24-oic acid + menaphthone = 3,12-dioxo-4-cholen-24-oic acid + reduced menaphthone

0

-

1.3.99.6

3,12-dioxo-5beta-cholan-24-oic acid methyl ester + menaphthone = 3,12-dioxo-4-cholen-24 oic acid methyl ester + reduced menaphthone

0

-

1.3.99.6

3-oxo-5beta-cholan-24-oic acid + menaphthone = 3-oxo-4-cholen-24-oic acid + reduced menaphthone

0

-

1.3.99.6

5beta-pregnan-3,20-dione + menaphthone = 4-pregnen-3,20-dione + reduced menaphthone

0

-

1.3.99.6

4 entries

1.4.1.13

menadione + NADPH + H+ = menadiol + NADP+

0

-

1.5.1.20

NADPH + H+ + menadione = NADP+ + menadiol

392157, 0

-

1.5.1.20

5-methyltetrahydrofolate + oxidized menadione = 5,10-methylenetetrahydrofolate + reduced menadione

392157, 392149, 0

-

1.5.1.20

NADH + menadione = NAD+ + reduced menadione

0

-

1.5.1.20

3 entries

1.5.1.30

menadione + NADH + H+ = menadiol + NAD+

0

-

1.5.1.53

5-methyltetrahydrofolate + oxidized menadione = 5,10-methylenetetrahydrofolate + reduced menadione

0

-

1.5.1.53

NADPH + H+ + oxidized menadione = NADP+ + reduced menadione

0

-

1.5.1.54

5-methyltetrahydrofolate + menadione = 5,10-methylenetetrahydrofolate + menadiol

0

-

1.5.1.54

NADH + H+ + menadione = NAD+ + menadiol

0

-

1.5.1.53

2 entries

1.5.1.54

2 entries

1.5.5.1

reduced electron-transferring-flavoprotein + menadione = electron-transferring-flavoprotein + menadiol

0

-

1.5.5.3

trans-4-hydroxy-L-proline + menadione = (3R,5S)-3-hydroxy-1-pyrroline-5-carboxylate + menadiol

0

-

1.5.99.4

(S)-nicotine + menadione + H2O = (S)-6-hydroxynicotine + menadiol

0

-

1.5.99.B2

L-proline + menadione = (S)-1-pyrroline-5-carboxylate + menadiol

0

-

1.6.2.4

NADPH + H+ + menadione = NADP+ + menadiol

0

-

1.6.2.4

NADPH + H+ + oxidized menadione = NADP+ + reduced menadione

0

-

1.6.5.10

2-methyl-1,4-naphthoquinone + NADPH + H+ = 2-methyl-1,4-naphthoquinol + NADP+

0

-

1.6.5.10

menadione + NADPH + H+ = menadiol + NADP+

0

-

1.6.5.10

NADPH + H+ + menadione = NADP+ + menadiol

392826, 0

-

1.6.2.4

2 entries

1.6.5.10

3 entries

1.6.5.12

menadione + NADPH + H+ = menadiol + NADP+

0

-

1.6.5.2

2-methyl-1,4-naphthoquinone + NAD(P)H = 2-methyl-1,4-naphthoquinol + NAD(P)+

0, 394375, 394383, 394378, 394382, 394364, 394352, 394356, 394363, 394366, 394349, 394350

-

1.6.5.2

2-methyl-1,4-naphthoquinone + NADH = 2-methyl-1,4-naphthoquinol + NAD+

0

-

1.6.5.2

2-methyl-1,4-naphthoquinone + NADPH = 2-methyl-1,4-naphthoquinol + NADp+

0

-

1.6.5.2

NADH + H+ + 2-methyl-1,4-naphthoquinone = NAD+ + 2-methyl-1,4-naphthoquinol

0

-

1.6.5.2

NADPH + H+ + 2-methyl-1,4-naphthoquinone = NADP+ + 2-methyl-1,4-naphthoquinol

0

-

1.6.5.2

menadione + NADH + H+ = menadiol + NAD+

0

-

1.6.5.2

cytochrome C + menadione + NADH = ? + reduced menadione + NAD+

0

-

1.6.5.2

menadione + NAD(P)H = reduced menadione + NAD(P)+

0

-

1.6.5.2

menadione + NAD(P)H = reduced menadione + NADP+

0

-

1.6.5.2

menadione + NADH + H+ = reduced menadione + NAD+

0

-

1.6.5.2

menadione + NADH = reduced menadione + NAD+

0

-

1.6.5.2

menadione + NADPH + H+ = reduced menadione + NADP+

0

-

1.6.5.2

menadione + NADPH = reduced menadione + NADP+

0

-

1.6.5.2

menadione + reduced nicotinamide 2-azidoadenine dinucleotide = reduced menadione + oxidized nicotinamide 2-azidoadenine dinucleotide

394357

-

1.6.5.2

menadione + reduced nicotinamide 8-azidoadenine dinucleotide = reduced menadione + oxidized nicotinamide 8-azidoadenine dinucleotide

394357

-

1.6.5.5

2-methyl-1,4-naphthoquinone + NADPH + H+ = 2-methyl-1,4-naphthoquinol + NADP+

0

-

1.6.5.5

menadione + NADPH + H+ = menadiol + NADP+

0

-

1.6.5.2

15 entries

1.6.5.5

2 entries

1.6.5.9

NADH + H+ + menadione = NAD+ + menadiol

0

-

1.7.1.1

menadione + NADH = reduced menadione + NAD+

0

-

1.7.1.16

nitrobenzene + menadione = N-hydroxyaniline + menadiol + H2O

0

-

1.7.5.1

nitrite + menadione + H2O = nitrate + menadiol

0

-

1.8.5.4

sulfide + menadione = polysulfide + menadiol

0

-

1.8.5.4

sulfide + menadione = sulfur + menadiol

0

-

1.8.5.4

2 entries

1.8.5.7

glutathione + 2-(glutathione-S-yl)-menadiol = glutathione disulfide + menadiol

0

-

7.1.1.2

2-methyl-1,4-naphthoquinone + NADH + H+ = 2-methyl-1,4-naphthoquinol + NAD+

0

-

7.1.1.2

NADH + 2-methyl-1,4-naphthoquinone = NAD+ + 2-methyl-1,4-naphthoquinol

0

-

7.1.1.2

NADH + H+ + 2-methyl-1,4-naphthoquinone = NAD+ + 2-methyl-1,4-naphthoquinol

0

-

7.1.1.2

NADH + H+ + menadione = NAD+ + menadiol

0

-

7.1.1.2

NADH + menadione = NAD+ + menadiol

0, 392831

-

7.1.1.2

NADH + menadione = NAD+ + reduced menadione

0

-

7.1.1.2

6 entries

7.2.1.1

reduced nicotinamide hypoxanthine dinucleotide + menadione = oxidized nicotinamide hypoxanthine dinucleotide + menadiol

0

-

Inhibitor in Enzyme-catalyzed Reactions (1 result)

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Show Inhibitors (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.5.1.111

the relative activity is drastically decreased when the reaction system is supplemented with more than 1.5 mM of menadione hydroquinol. 3 mM menadione hydroquinol almost absolutely inhibits the prenylation by precipitating the enzyme in the reaction system

758689

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.111

0.003

-

mutant enzyme E281R, at pH 8.0 and 32°C

758689

2.5.1.111

0.005

-

mutant enzyme E281A, at pH 8.0 and 32°C

758689

2.5.1.111

0.014

-

mutant enzyme E281S, at pH 8.0 and 32°C

758689

2.5.1.111

0.022

-

mutant enzyme E281K, at pH 8.0 and 32°C

758689

2.5.1.111

0.026

-

mutant enzyme E281T, at pH 8.0 and 32°C

758689

2.5.1.111

0.038

-

mutant enzyme E281V, at pH 8.0 and 32°C

758689

2.5.1.111

0.038

-

wild type enzyme, at pH 8.0 and 32°C

758689

2.5.1.111

0.039

-

mutant enzyme E281M, at pH 8.0 and 32°C

758689

2.5.1.111

0.045

-

mutant enzyme E281D, at pH 8.0 and 32°C

758689

2.5.1.111

0.083

-

mutant enzyme E281Q, at pH 8.0 and 32°C

758689

2.5.1.111

10 entries

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

2.5.1.111

0.1044

-

mutant enzyme E281R, at pH 8.0 and 32°C

758689

2.5.1.111

0.1537

-

mutant enzyme E281Q, at pH 8.0 and 32°C

758689

2.5.1.111

0.1737

-

wild type enzyme, at pH 8.0 and 32°C

758689

2.5.1.111

0.2106

-

mutant enzyme E281M, at pH 8.0 and 32°C

758689

2.5.1.111

0.2181

-

mutant enzyme E281K, at pH 8.0 and 32°C

758689

2.5.1.111

0.2933

-

mutant enzyme E281V, at pH 8.0 and 32°C

758689

2.5.1.111

0.3623

-

mutant enzyme E281A, at pH 8.0 and 32°C

758689

2.5.1.111

0.4097

-

mutant enzyme E281S, at pH 8.0 and 32°C

758689

2.5.1.111

0.4799

-

mutant enzyme E281T, at pH 8.0 and 32°C

758689

2.5.1.111

0.5202

-

mutant enzyme E281D, at pH 8.0 and 32°C

758689

2.5.1.111

10 entries

7.1.1.4

0.23

-

pH 6. 40°C

720484

References & Links

Literature References (36)

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Show Reference (36 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

392149

4399897

Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine

1971

Kutzbach, C.; Stokstad, E.L.R.

Biochim. Biophys. Acta

250

459-477

392157

2383427

Purification and characterization of methylenetetrahydrofolate reductase from human cadaver liver [published erratum appears in Biochem Med Metab Biol 1990 Oct;44(2):200]

1990

Zhou, J.; Kang, S.S.; Wong, P.W.K.; Fournier, B.; Rozen, R.

Biochem. Med. Metab. Biol.

43

234-242

392826

4388793

Purification and properties of three separate menadione reductases from hog liver

1969

Koli, A.K.; Yearby, C.; Scott, W.; Donaldson, K.O.

J. Biol. Chem.

244

621-629

392831

2679883

Purification of NADH-ferricyanide dehydrogenase and NADH-quinone reductase from Escherichia coli membranes and their roles in the respiratory chain

1989

Hayashi, M.; Miyoshi, T.; Takashina, S.; Unemoto, T.

Biochim. Biophys. Acta

977

62-69

394349

13705804

Purification and some properties of a brain diaphorase

1961

Giuditta, A.; Strecker, H.J.

Biochim. Biophys. Acta

48

10-19

394350

13846011

The reduction of vitamin K1 by an enzyme from dog liver

1960

Wosilait, W.D.

J. Biol. Chem.

235

1196-1201

394352

-

Vitamin K-Reduktase, Darstellung und eigenschaften

1960

Märki, F.; Martius, C.

Biochem. Z.

333

111-135

394356

1372830

Separation and characterization of isoforms of DT-diaphorase from rat liver cytosol

1992

Segura-Aguilar, J.; Kaiser, R.; Lind, C.

Biochim. Biophys. Acta

1120

33-42

394357

1906347

Photodependent inhibition of rat liver NAD(P)H:quinone acceptor oxidoreductase by (A)-2-azido-NAD+ and (A)-8-azido-NAD

1991

Deng, P.S.K.; Zhao, S.H.; Iyanagi, T.; Chen, S.

Biochemistry

30

6942-6948

394363

6803779

Vitamin K1 hydroquinone formation catalyzed by DT-diaphorase

1982

Fasco, M.J.; Principe, L.M.

Biochem. Biophys. Res. Commun.

104

187-192

394364

2418014

Purification and characterization of two isofunctional forms of NAD(P)H: quinone reductase from mouse liver

1986

Prochaska, H.J.; Talalay, P.

J. Biol. Chem.

261

1372-1378

394366

2233301

DT-diaphorase: purification, properties, and function

1990

Lind, C.; Cadenas, E.; Hochstein, P.; Ernster, L.

Methods Enzymol.

186

287-301

394375

7746280

Catalytic properties of NAD(P)H:quinone acceptor oxidoreductase: study involving mouse, rat, human, and mouse-rat chimeric enzymes

1995

Chen, S.; Knox, R.; Lewis, A.D.; Friedlos, F.; Workman, P.; Deng, P.S.K.; Fung, M.; Ebenstein, D.; Wu, K.; Tsai, T.M.

Mol. Pharmacol.

47

934-939

394378

-

Heterologous expression and biochemical characterization of an NAD(P)H:quinone oxidoreductase from the hemiparasitic plant Triphysaria versicolor

2002

Wrobel, R.L.; Matvienko, M.; Yoder, J.I.

Plant Physiol. Biochem.

40

265-272

394382

10683249

Characterization and partial purification of microsomal NAD(P)H:quinone oxidoreductases

2000

Jaiswal, A.K.

Arch. Biochem. Biophys.

375

62-68

394383

11238963

NAD(P)H:menadione oxidoreductase of the amitochondriate eukaryote Giardia lamblia: a simpler homologue of the vertebrate enzyme

2001

Sanchez, L.B.; Elmendorf, H.; Nash, T.E.; Muller, M.

Microbiology

147

561-570

644661

10336636

Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica

1999

Rhee, S.K.; Fuchs, G.

Eur. J. Biochem.

262

507-515

658434

15733542

Quinone reductase 2 substrate specificity and inhibitgion pharmacology

2005

Boutin, J.A.; Chatelein-Egger, F.; Vella, F.; Delagrange, P.; Ferry, G.

Chem. Biol. Interact.

151

213-228

671708

16129418

Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954

2005

Fu, Y.; Buryanovskyy, L.; Zhang, Z.

Biochem. Biophys. Res. Commun.

336

332-338

696200

14640690

Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study

2003

Zhao, Z.; Rothery, R.A.; Weiner, J.H.

Biochemistry

42

14225-14233

696201

12731882

Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol

2003

Zhao, Z.; Rothery, R.A.; Weiner, J.H.

Biochemistry

42

5403-5413

696212

17439244

High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD

2007

Lanciano, P.; Magalon, A.; Bertrand, P.; Guigliarelli, B.; Grimaldi, S.

Biochemistry

46

5323-5329

697207

11289300

The coordination and function of the redox centres of the membrane-bound nitrate reductases

2001

Blasco, F.; Guigliarelli, B.; Magalon, A.; Asso, M.; Giordano, G.; Rothery, RA.

Cell. Mol. Life Sci.

58

179-193

697708

15182355

Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli

2004

Giordani, R.; Buc, J.

Eur. J. Biochem.

271

2400-2407

700372

12910261

Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

2003

Bertero, M.G.; Rothery, R.A.; Palak, M.; Hou, C.; Lim, D.; Blasco, F.; Weiner, J.H.; Strynadka, N.C.

Nat. Struct. Biol.

10

681-687

702016

18423374

UDP-glucuronosyltransferases 1A6 and 1A10 catalyze reduced menadione glucuronidation

2008

Nishiyama, T.; Ohnuma, T.; Inoue, Y.; Kishi, T.; Ogura, K.; Hiratsuka, A.

Biochem. Biophys. Res. Commun.

371

247-250

711729

20399199

Old and new inhibitors of quinone reductase 2

2010

Ferry, G.; Hecht, S.; Berger, S.; Moulharat, N.; Coge, F.; Guillaumet, G.; Leclerc, V.; Yous, S.; Delagrange, P.; Boutin, J.A.

Chem. Biol. Interact.

186

103-109

713979

8394685

The menaquinol oxidase of Bacillus subtilis W23

1993

Lemma, E.; Schagger, H.; Kroger, A.

Arch. Microbiol.

159

574-578

713980

7575098

Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis

1995

Lemma, E.; Simon, J.; Schagger, H.; Kroger, A.

Arch. Microbiol.

163

432-438

720484

7984110

The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem

1994

Luebben, M.; Warne, A.; Albracht, S.P.; Saraste, M.

Mol. Microbiol.

13

327-335

727727

8626304

Purification of a cytochrome bd terminal oxidase encoded by the Escherichia coli app locus from a delta cyo delta cyd strain complemented by genes from Bacillus firmus OF4

1996

Sturr, M.G.; Krulwich, T.A.; Hicks, D.B.

J. Bacteriol.

178

1742-1749

743792

26015371

The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress

2015

Lu, P.; Heineke, M.H.; Koul, A.; Andries, K.; Cook, G.M.; Lill, H.; van Spanning, R.; Bald, D.

Sci. Rep.

5

10333

758689

32125480

Combining mutagenesis on Glu281 of prenyltransferase NovQ and metabolic engineering strategies for the increased prenylated activity towards menadione

2020

Ni, W.; Zheng, Z.; Liu, H.; Wang, P.; Wang, H.; Sun, X.; Yang, Q.; Fang, Z.; Tang, H.; Zhao, G.

Appl. Microbiol. Biotechnol.

104

4371-4382

760562

11371181

Methylenetetrahydrofolate reductase from Escherichia coli elucidation of the kinetic mechanism by steady-state and rapid-reaction studies

2001

Trimmer, E.E.; Ballou, D.P.; Matthews, R.G.

Biochemistry

40

6205-6215

761372

9922232

Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli

1999

Sheppard, C.A.; Trimmer, E.E.; Matthews, R.G.

J. Bacteriol.

181

718-725

761422

10593891

Isolation, characterization, and functional expression of cDNAs encoding NADH-dependent methylenetetrahydrofolate reductase from higher plants

1999

Roje, S.; Wang, H.; McNeil, S.D.; Raymond, R.K.; Appling, D.R.; Shachar-Hill, Y.; Bohnert, H.J.; Hanson, A.D.

J. Biol. Chem.

274

36089-36096

Links to other databases for menadiol

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