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• • Molecular Structure
  • Sum Formula
  • BRENDA Name
  • Synonyms
  • InChIKey
  • Pathways
• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
  • Links

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Ligand menaquinol

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

heme metabolism, propionate fermentation, vitamin K metabolism

KEGG

Biosynthesis of cofactors, Biosynthesis of secondary metabolites, Ubiquinone and other terpenoid-quinone biosynthesis

MetaCyc

(S)-lactate fermentation to propanoate, acetate and hydrogen, 3,8-divinyl-chlorophyllide a biosynthesis II (anaerobic), formate to dimethyl sulfoxide electron transfer, formate to nitrite electron transfer, formate to trimethylamine N-oxide electron transfer, glycerol-3-phosphate to fumarate electron transfer, glycerol-3-phosphate to hydrogen peroxide electron transport, heme b biosynthesis II (oxygen-independent), hydrogen to dimethyl sulfoxide electron transfer, hydrogen to fumarate electron transfer, hydrogen to trimethylamine N-oxide electron transfer, incomplete reductive TCA cycle, mixed acid fermentation, NADH to dimethyl sulfoxide electron transfer, NADH to fumarate electron transfer, NADH to hydrogen peroxide electron transfer, NADH to trimethylamine N-oxide electron transfer, nitrate reduction III (dissimilatory), nitrate reduction IX (dissimilatory), nitrate reduction VII (denitrification), nitrate reduction VIII (dissimilatory), pyruvate fermentation to propanoate I, reductive TCA cycle I, reductive TCA cycle II, sulfite oxidation V (SoeABC), TCA cycle VI (Helicobacter), thiosulfate disproportionation III (quinone) more

Show all BRENDA pathways known for menaquinol

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.B7

menaquinol + acceptor = ?

739964

-

1.3.5.1

fumarate + menaquinol = succinate + menaquinone

391137

-

1.3.5.4

fumarate + a menaquinol = succinate + a menaquinone

700278

-

1.3.5.4

fumarate + menaquinol = succinate + menaquinone

391089, 391090

-

1.3.5.4

2 entries

1.7.5.2

NO + menaquinol = N2O + H2O + menaquinone

659256

-

7.1.1.3

menaquinol + O2 + H+[side 1] = menaquinone + H2O + H+[side 2]

742647

-

7.1.1.5

menaquinol + O2 = menaquinone + H2O

713980, 741850, 741917, 742646, 715507

-

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

-

-

1.17.5.3

formate + menaquinone = CO2 + menaquinol

-

-

1.3.5.1

succinate + menaquinone = fumarate + menaquinol

-

-

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

-

-

1.3.5.4

succinate + a menaquinone = fumarate + a menaquinol

-

-

1.8.5.3

dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol

-

-

1.8.5.9

a [DsbA protein] with reduced L-cysteine residues + menaquinone = a [DsbA protein] carrying a disulfide bond + menaquinol

-

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + menaquinone = [DsbA protein] carrying a disulfide bond + menaquinol

-

-

1.8.5.9

2 entries

7.1.1.2

NADH + H+ + menaquinone = NAD+ + menaquinol

-

-

Substrate in Enzyme-catalyzed Reactions (15 results)

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Show Substrate (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.B7

menaquinol + acceptor = ?

739964

-

1.14.18.3

propylene + menaquinol + O2 = propylene oxide + menaquinone + H2O

713934

-

1.3.5.1

fumarate + menaquinol = succinate + menaquinone

391137

-

1.3.5.4

fumarate + a menaquinol = succinate + a menaquinone

700278

-

1.3.5.4

fumarate + menaquinol = succinate + ?

391089, 391090

-

1.3.5.4

fumarate + menaquinol = succinate + menaquinone

674634, 707470, 674532, 742846, 391089, 391090, 654820

-

1.3.5.4

3 entries

1.7.2.5

NO + menaquinol = N2O + H2O + menaquinone

658038

-

1.7.5.1

nitrate + menaquinol = nitrite + menaquinone + H2O

672331

-

1.7.5.2

nitric oxide + menaquinol = nitrous oxide + menaquinone + H2O

714116, 714147, 658038

-

1.7.5.2

NO + menaquinol = N2O + H2O + menaquinone

659256

-

1.7.5.2

2 entries

1.8.5.5

thiosulfate + menaquinol = sulfite + hydrogen sulfide + menaquinone

725273

-

2.8.1.5

thiosulfate + menaquinol = sulfite + oxidized menaquinol + sulfide

725273

-

7.1.1.3

menaquinol + O2 + H+[side 1] = menaquinone + H2O + H+[side 2]

742647

-

7.1.1.5

menaquinol + O2 = menaquinone + H2O

713979, 713980, 715416, 741850, 741917, 742646, 715507

-

7.1.1.8

menaquinol + 2 ferricytochrome c = menaquinone + 2 ferrocytochrome c + 2 H+

440031, 742379

-

Product in Enzyme-catalyzed Reactions (19 results)

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Show Product (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.98.4

menaquinone + reduced coenzyme F420 = menaquinol + oxidized coenzyme F420

-

-

1.12.5.1

H2 + menaquinone = menaquinol

-

-

1.17.5.3

formate + menaquinone = CO2 + menaquinol

-

-

1.2.5.1

pyruvate + menaquinone + H2O = acetate + CO2 + menaquinol

-

-

1.3.5.1

succinate + menaquinone = fumarate + menaquinol

-

-

1.3.5.3

protoporphyrinogen IX + 3 menaquinone = protoporphyrin IX + 3 menaquinol

-

-

1.3.5.4

succinate + a menaquinone = fumarate + a menaquinol

-

-

1.3.5.4

succinate + menaquinone = fumarate + menaquinol

-

-

1.3.5.4

2 entries

1.5.5.3

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

-

-

1.6.5.9

NADH + H+ + menaquinone = NAD+ + menaquinol

-

-

1.8.5.3

dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol

-

-

1.8.5.5

sulfite + hydrogen sulfide + menaquinone = thiosulfate + menaquinol

-

-

1.8.5.9

a [DsbA protein] with reduced L-cysteine residues + menaquinone = a [DsbA protein] carrying a disulfide bond + menaquinol

-

-

1.8.5.9

[DsbA protein] with reduced L-cysteine residues + menaquinone = [DsbA protein] carrying a disulfide bond + menaquinol

-

-

1.8.5.9

2 entries

2.1.1.163

demethylmenaquinol + S-adenosyl-L-methionine = menaquinol + S-adenosyl-L-homocysteine

-

-

7.1.1.2

NADH + H+ + menaquinone = NAD+ + menaquinol

-

-

7.1.1.2

NADH + menaquinone + H+ = NAD+ + menaquinol

-

-

7.1.1.2

NADH + menaquinone = NAD+ + menaquinol

-

-

7.1.1.2

3 entries

7.2.1.1

NADH + menaquinone = NAD+ + reduced menaquinone

-

-

Enzyme Cofactor/Cosubstrate (1 result)

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Show Cofactor (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.8.5.5

menaquinol is the sole electron donor to thiosulfate reductase

725273

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

7.1.1.8

-

674665

-

7.1.1.8

inhibitory ubiquinol analogue binds to the ubiquinol oxidation site in the bc1 complex, 1 molecule bound per enzyme dimer causes full inhibition, binding is anti-cooperative

658160

-

7.1.1.8

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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Show Turnover Number (16 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.3.5.4

2.8

-

mutant R28E/E29I, pH 8.0, 30°C

742846

1.3.5.4

3

-

mutant R28E/E29I, pH 7.0, 30°C

742846

1.3.5.4

6.1

-

mutant R81A, pH 8.0, 30°C

742846

1.3.5.4

10.6

-

mutant R81A, pH 7.0, 30°C

742846

1.3.5.4

11.1

-

mutant R28L/E29L, pH 8.0, 30°C

742846

1.3.5.4

12.2

-

mutant R28L/E29L, pH 7.0, 30°C

742846

1.3.5.4

12.8

-

mutant R81E, pH 8.0, 30°C

742846

1.3.5.4

14

-

mutant R81E, pH 7.0, 30°C

742846

1.3.5.4

65.4

-

mutant R28N, pH 8.0, 30°C

742846

1.3.5.4

67.8

-

mutant R28L, pH 8.0, 30°C

742846

1.3.5.4

68.6

-

mutant R28N, pH 7.0, 30°C

742846

1.3.5.4

71.1

-

mutant R28L, pH 7.0, 30°C

742846

1.3.5.4

123.7

-

mutant R81K, pH 7.0, 30°C

742846

1.3.5.4

138.9

-

mutant R81K, pH 8.0, 30°C

742846

1.3.5.4

211

-

wild-type, pH 8.0, 30°C

742846

1.3.5.4

222.2

-

wild-type, pH 7.0, 30°C

742846

1.3.5.4

16 entries

K_M Value (8 results)

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Show KM Value (8 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.3.5.4

0.0009

-

mutant R81A, pH 7.0, 30°C

742846

1.3.5.4

0.0013

-

mutant R81E, pH 7.0, 30°C

742846

1.3.5.4

0.0027

-

mutant R81K, pH 7.0, 30°C

742846

1.3.5.4

0.003

-

mutant R28L, pH 7.0, 30°C

742846

1.3.5.4

0.0031

-

mutant R28N, pH 7.0, 30°C

742846

1.3.5.4

0.0039

-

mutant R28L/E29L, pH 7.0, 30°C

742846

1.3.5.4

0.004

-

mutant R28E/E29I, pH 7.0, 30°C

742846

1.3.5.4

0.0054

-

wild-type, pH 7.0, 30°C

742846

1.3.5.4

8 entries

References & Links

Literature References (29)

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Show Reference (29 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

391089

3609021

Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes

1987

Lauterbach, F.; Körtner, C.; Tripier, D.; Unden, G.

Eur. J. Biochem.

166

447-452

391090

2388563

Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b

1990

Körtner, C.; Lauterbach, F.; Tripier, D.; Unden, G.; Kröger, A.

Mol. Microbiol.

4

855-860

391137

10486141

Comparison of catalytic activity and inhibitors of quinone reactions of succinate dehydrogenase (Succinate-ubiquinone oxidoreductase) and fumarate reductase (Menaquinol-fumarate oxidoreductase) from Escherichia coli

1999

Maklashina, E.; Cecchini, G.

Arch. Biochem. Biophys.

369

223-232

440031

9693731

Mechanism of ubiquinol oxidation by the cytochrome bc1 complex: pre-steady-state kinetics of cytochrome bc1 complexes containing site-directed mutants of the Rieske iron-sulfur protein

1998

Snyder, C.; Trumpower, B.L.

Biochim. Biophys. Acta

1365

125-134

654820

11803023

Succinate dehydrogenase and fumrate reductase from Escherichia coli

2002

Cecchini, G.; Schröder, I.; GUnsalus, R.P.; Maklashina, E.

Biochim. Biophys. Acta

1553

140-157

658038

15491156

NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551

2004

Suharti; Heering, H.A.; de Vries, S.

Biochemistry

43

13487-13495

658160

12206910

A concerted, alternating sites mechanism of ubiquinol oxidation by the dimeric cytochrome bc1 complex

2002

Trumpower, B.L.

Biochim. Biophys. Acta

1555

166-173

659256

12799376

Purification and characterization of the MQH2:NO oxidoreductase from the hyperthermophilic archaeon Pyrobaculum aerophilum

2003

de Vries, S.; Strampraad, M.J.; Lu, S.; Moenne-Loccoz, P.; Schroder, I.

J. Biol. Chem.

278

35861-35868

672331

15804488

Isolation and spectroscopic characterization of the membrane-bound nitrate reductase from Pseudomonas chlororaphis DSM 50135

2005

Pinho, D.; Besson, S.; Silva, P.J.; de Castro, B.; Moura, I.

Biochim. Biophys. Acta

1723

151-162

674532

16484232

Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain

2006

Maklashina, E.; Iverson, T.M.; Sher, Y.; Kotlyar, V.; Andrell, J.; Mirza, O.; Hudson, J.M.; Armstrong, F.A.; Rothery, R.A.; Weiner, J.H.; Cecchini, G.

J. Biol. Chem.

281

11357-11365

674634

16829675

Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli

2006

Maklashina, E.; Hellwig, P.; Rothery, R.A.; Kotlyar, V.; Sher, Y.; Weiner, J.H.; Cecchini, G.

J. Biol. Chem.

281

26655-26664

674665

16908520

Regulatory interactions between ubiquinol oxidation and ubiquinone reduction sites in the dimeric cytochrome bc1 complex

2006

Covian, R.; Trumpower, B.L.

J. Biol. Chem.

281

30925-30932

700278

19170876

Production, characterization and determination of the real catalytic properties of the putative succinate dehydrogenase from Wolinella succinogenes

2009

Juhnke, H.D.; Hiltscher, H.; Nasiri, H.R.; Schwalbe, H.; Lancaster, C.R.

Mol. Microbiol.

71

1088-1101

707470

17154542

Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate:menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis

2006

Madej, M.G.; Nasiri, H.R.; Hilgendorff, N.S.; Schwalbe, H.; Unden, G.; Lancaster, C.R.

Biochemistry

45

15049-15055

713934

7646068

Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors

1995

Shiemke, A.K.; Cook, S.A.; Miley, T.; Singleton, P.

Arch. Biochem. Biophys.

321

421-428

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

714116

15667284

Membrane-bound denitrification in the Gram-positive bacterium Bacillus azotoformans

2005

Suharti, S.; de Vries, S.

Biochem. Soc. Trans.

33

130-133

714147

11327887

A novel copper A containing menaquinol NO reductase from Bacillus azotoformans

2001

Suhart, S.; Strampraad, M.; Schröder, I.; De Vries, S.

Biochemistry

40

2632-2639

715416

8388393

The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties

1993

Lauraeus, M.; Wikstroem, M.

J. Biol. Chem.

268

11470-11473

715507

20351111

Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis

2010

Yi, S.M.; Narasimhulu, K.V.; Samoilova, R.I.; Gennis, R.B.; Dikanov, S.A.

J. Biol. Chem.

285

18241-18251

725273

22081391

Thiosulfate reduction in Salmonella enterica is driven by the proton motive force

2012

Stoffels, L.; Krehenbrink, M.; Berks, B.C.; Unden, G.

J. Bacteriol.

194

475-485

739964

26345487

Assessment of the carbon monoxide metabolism of the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus VC-16 by comparative transcriptome analyses

2015

Hocking, W.P.; Roalkvam, I.; Magnussen, C.; Stokke, R.; Steen, I.H.

Archaea

2015

235384

741850

24779955

Prediction of high- and low-affinity quinol-analogue-binding sites in the aa3 and bo3 terminal oxidases from Bacillus subtilis and Escherichia coli

2014

Bossis, F.; De Grassi, A.; Palese, L.L.; Pierri, C.L.

Biochem. J.

461

305-314

741917

26196462

Plasticity in the high affinity menaquinone binding site of the cytochrome aa3-600 menaquinol oxidase from Bacillus subtilis

2015

Yi, S.M.; Taguchi, A.T.; Samoilova, R.I.; OMalley, P.J.; Gennis, R.B.; Dikanov, S.A.

Biochemistry

54

5030-5044

742379

24650148

Evidence for function overlapping of CymA and the cytochrome bc1 complex in the Shewanella oneidensis nitrate and nitrite respiration

2014

Fu, H.; Jin, M.; Ju, L.; Mao, Y.; Gao, H.

Environ. Microbiol.

16

3181-3195

742646

28808161

Listeria monocytogenes has both a bd-type and an aa3-type terminal oxidase which allow growth in different oxygen levels and both are important in infection

2017

Corbett, D.; Goldrick, M.; Fernandes, V.E.; Davidge, K.; Poole, R.K.; Andrew, P.W.; Cavet, J.; Roberts, I.S.

Infect. Immun.

85

e00354-17

742647

28808161

Listeria monocytogenes has both a bd-type and an aa3-type terminal oxidase which allow growth in different oxygen levels and both are important in infection

2017

Corbett, D.; Goldrick, M.; Fernandes, V.E.; Davidge, K.; Poole, R.K.; Andrew, P.W.; Cavet, J.; Roberts, I.S.

Infect. Immun.

85

e00354-17

742846

23836905

Plasticity of the quinone-binding site of the complex II homolog quinol fumarate reductase

2013

Singh, P.K.; Sarwar, M.; Maklashina, E.; Kotlyar, V.; Rajagukguk, S.; Tomasiak, T.M.; Cecchini, G.; Iverson, T.M.

J. Biol. Chem.

288

24293-24301

Links to other databases for menaquinol

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Show Links (1 entry)

ChEBI

PubChem

-