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Ligand trimethylamine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

methane metabolism, phosphatidylethanolamine bioynthesis

KEGG

Carbon metabolism, Methane metabolism, Microbial metabolism in diverse environments

MetaCyc

choline degradation III, formate to trimethylamine N-oxide electron transfer, gamma-butyrobetaine degradation I, hydrogen to trimethylamine N-oxide electron transfer, L-carnitine degradation II, methanogenesis from tetramethylammonium, methanogenesis from trimethylamine, NADH to trimethylamine N-oxide electron transfer, trimethylamine degradation, trimethylamine N-oxide biosynthesis more

Show all BRENDA pathways known for trimethylamine

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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

1.14.13.148

N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O

717229, 718454, 717640

-

1.14.13.8

trimethylamine + NADPH + H+ + O2 = trimethylamine N-oxide + NADP+ + H2O

710837, 764561, 764562, 684678

-

1.14.13.8

trimethylamine + NADPH + O2 = trimethylamine N-oxide + NADP+ + H2O

676315, 671729, 676116, 673313

-

1.5.8.2

trimethylamine + H2O + electron acceptor = dimethylamine + formaldehyde + reduced electron acceptor

393913, 393914, 393916, 393917, 393918, 393919, 393921, 393925, 393881, 393923, 393920

-

1.5.8.2

trimethylamine + H2O + electron transferring flavoprotein = dimethylamine + formaldehyde + reduced electron transferring flavoprotein

393879, 393884, 393887, 393890, 393891, 393893, 393895, 393896, 393897, 393899, 393901, 393902, 393903, 393904, 393905, 393915, 393889, 393898, 393878, 393885, 393909

-

1.5.8.2

trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

711031

-

1.5.8.2

trimethylamine + H2O + FMN = dimethylamine + formaldehyde + FMNH2

654192, 654971

-

2.1.1.250

trimethylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine

717525, 717781

-

2.1.1.250

trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine

717771

-

2.1.1.250

trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine

717721, 717723, 756781

-

1.14.13.8

2 entries

1.5.8.2

4 entries

2.1.1.250

3 entries

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

1.14.13.239

L-carnitine + NADH + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

L-carnitine + NADPH + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O

0

-

1.14.13.239

2 entries

1.21.4.4

N,N,N-trimethylglycine + phosphate + thioredoxin = acetyl phosphate + trimethylamine + thioredoxin disulfide

0

-

1.7.2.3

trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ = trimethylamine + (ferricytochrome c)-subunit + H2O

0

-

1.7.2.3

trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ = trimethylamine + 2 (ferricytochrome c)-subunit + H2O

0

-

1.7.2.3

trimethylamine N-oxide + NADH = NAD+ + trimethylamine + H2O

0

-

1.7.2.3

trimethylamine-N-oxide + electron donor = trimethylamine + oxidized electron donor + H2O

392775, 392762, 0, 392759, 392769, 392768, 392766

-

1.7.2.3

trimethylamine-N-oxide + enzyme-MoIV = trimethylamine + enzyme-MoVI + H2O

0

-

1.7.2.3

5 entries

4.3.99.4

choline = trimethylamine + acetaldehyde

0

-

Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.148

N,N,N-trimethylamine + NADH + H+ + O2 = N,N,N-trimethylamine N-oxide + NAD+ + H2O

717207, 764744

-

1.14.13.148

N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O

717226, 717229, 717652, 718454, 717533, 717207, 718325, 717640, 717521, 763968

-

1.14.13.148

2 entries

1.14.13.238

trimethylamine + NADH + H+ + O2 = ?

743014

-

1.14.13.8

N,N,N-trimethylamine + NADPH + H+ + O2 = N,N,N-trimethylamine N-oxide + NADP+ + H2O

717226

-

1.14.13.8

trimethylamine + NADPH + H+ + O2 = ?

742335, 742171, 742256, 687477

-

1.14.13.8

trimethylamine + NADPH + H+ + O2 = trimethylamine N-oxide + NADP+ + H2O

684678, 710837, 689806, 742352, 764561, 764562, 724128, 724246, 741863

-

1.14.13.8

trimethylamine + NADPH + O2 = ?

348497, 348508, 348513

-

1.14.13.8

trimethylamine + NADPH + O2 = trimethylamine N-oxide + NADP+ + H2O

676315, 671729, 673313, 675603, 676116

-

1.5.8.2

trimethylamine + H2O + 2,6-dichlorophenolindophenol = dimethylamine + formaldehyde + reduced 2,6-dichlorophenolindophenol

393887, 393892, 393908, 393920, 655622, 393894

-

1.5.8.2

trimethylamine + H2O + alphaR237K mutant electron transferring flavoprotein = dimethylamine + formaldehyde + reduced alphaR237K mutant electron transferring flavoprotein

685241

-

1.5.8.2

trimethylamine + H2O + electron acceptor = dimethylamine + formaldehyde + reduced electron acceptor

711031, 393913, 393914, 393916, 393917, 393918, 393919, 393921, 393925, 393881, 393923, 393920

-

1.5.8.2

trimethylamine + H2O + electron transferring flavoprotein = dimethylamine + formaldehyde + reduced electron transferring flavoprotein

393879, 393884, 393887, 393890, 393891, 393893, 393895, 393896, 393897, 393899, 393901, 393902, 393903, 393904, 393905, 393915, 685241, 393889, 393898, 393878, 393885, 393909

-

1.5.8.2

trimethylamine + H2O + electron-transfer flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

711031

-

1.5.8.2

trimethylamine + H2O + ferricenium hexafluorophosphate = dimethylamine + formaldehyde + ferrocenium hexafluorophosphate

393888

-

1.5.8.2

trimethylamine + H2O + FMN = dimethylamine + formaldehyde + FMNH2

654192, 654971

-

1.5.8.2

trimethylamine + H2O + NADP+ = dimethylamine + formaldehyde + NADPH

655622

-

1.5.8.2

trimethylamine + H2O + oxidized electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

656284

-

1.5.8.2

trimethylamine + H2O + phenazine methosulfate = dimethylamine + formaldehyde + reduced phenazine methosulfate

393892, 393911, 393920, 393923, 393924, 393922, 393900

-

1.5.8.2

trimethylamine + H2O + semiquinone electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein

656284

-

2.1.1.250

trimethylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine

717525, 717781

-

2.1.1.250

trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine

717771

-

2.1.1.250

trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine

717721, 717723, 756781

-

1.14.13.8

5 entries

1.5.8.2

11 entries

2.1.1.250

3 entries

Product in Enzyme-catalyzed Reactions (26 results)

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Show Product (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.239

1-butyl-trimethylammonium + NADH + H+ + O2 = ? + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

D-carnitine + NADH + H+ + O2 = (3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

D-carnitine + NADPH + H+ + O2 = (3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O

0

-

1.14.13.239

gamma-butyrobetaine + NADH + H+ + O2 = ? + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

L-carnitine + NADH + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

L-carnitine + NADPH + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O

0

-

1.14.13.239

meldonium + NADH + H+ + O2 = ? + trimethylamine + NAD+ + H2O

0

-

1.14.13.239

7 entries

1.21.4.4

N,N,N-trimethylglycine + phosphate + thioredoxin = acetyl phosphate + trimethylamine + thioredoxin disulfide

0, 636281

-

1.7.2.3

trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ = trimethylamine + (ferricytochrome c)-subunit + H2O

0, 392764

-

1.7.2.3

trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ = trimethylamine + 2 (ferricytochrome c)-subunit + H2O

0

-

1.7.2.3

trimethylamine N-oxide + benzyl viologen + H+ = trimethylamine + oxidized benzyl viologen + H2O

0

-

1.7.2.3

trimethylamine N-oxide + electron donor = trimethylamine + oxidized electron donor + H2O

392775, 392770, 0, 392768, 392755, 392756, 392757, 392773, 392774, 392776, 392772, 392769, 392759

-

1.7.2.3

trimethylamine N-oxide + NADH = NAD+ + trimethylamine + H2O

0

-

1.7.2.3

trimethylamine N-oxide + oxidized benzyl viologen + 2 H+ = trimethylamine + reduced benzyl viologen + H2O

0

-

1.7.2.3

trimethylamine N-oxide + oxidized benzyl viologen + H+ = trimethylamine + reduced benzyl viologen + H2O

0

-

1.7.2.3

trimethylamine N-oxide + oxidized methyl viologen + H+ = trimethylamine + reduced methyl viologen + H2O

0

-

1.7.2.3

trimethylamine-N-oxide + electron donor = trimethylamine + oxidized electron donor + H2O

392775, 392762, 0, 392759, 392769, 392768, 392766

-

1.7.2.3

trimethylamine-N-oxide + enzyme-MoIV = trimethylamine + enzyme-MoVI + H2O

0

-

1.8.5.3

trimethylamine N-oxide + reduced benzyl viologen + H2O = trimethylamine + oxidized benzyl viologen

0

-

1.8.5.3

trimethylamine N-oxide + reduced benzyl viologen = trimethylamine + oxidized benzyl viologen

0

-

1.8.5.3

trimethylamine N-oxide + reduced dichlorophenolindophenol = trimethylamine + H2O + oxidized dichlorophenolindophenol

0

-

1.8.5.3

trimethylamine N-oxide + reduced lapachol = trimethylamine + oxidized lapachol

0

-

1.8.5.3

trimethylamine-N-oxide + reduced methyl viologen = trimethylamine + H2O + oxidized methyl viologen

0

-

1.7.2.3

10 entries

1.8.5.3

5 entries

1.8.5.B1

trimethylamine N-oxide + reduced benzyl viologen = trimethylamine + oxidized benzyl viologen + H2O

0

-

2.1.1.252

tetramethylammonium + a [Co(I) tetramethylammonium-specific corrinoid protein] = a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine

0

-

4.3.99.4

choline = trimethylamine + acetaldehyde

0

-

Activator in Enzyme-catalyzed Reactions (4 results)

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Show Activating Compound (4 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.2.8

-

742110

-

1.1.5.5

-

740180

-

2.7.4.1

5% activation compared to NH4+

756630

-

3.6.1.11

5% activation compared to NH4+

756630

-

Inhibitor in Enzyme-catalyzed Reactions (17 results)

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Show Inhibitors (17 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.108

L-carnitine dehydrogenase, strong inhibition

285737

-

1.1.3.17

-

654371

-

1.14.13.8

-

348509, 712902

-

1.14.13.8

1 mM, oxidation of dimethylaniline, competitive

348501

-

1.14.13.8

a FMO3-specific inhibitor, exhibits anegligible effect on the N,N-dimethylamphetamine N-oxide formation

706921

-

1.14.13.8

3 entries

1.5.8.1

-

393880

-

1.5.8.2

-

393893

-

1.5.8.2

hyperbolic substrate inhibition

393878

-

1.5.8.2

inhibitory at higher concentrations

393923

-

1.5.8.2

substrate inhibition

711031

-

1.5.8.2

4 entries

2.8.2.6

competitive dead-end inhibitor with respect to choline, uncompetitive with respect to PAPS

643829

-

3.1.3.2

-

666337

-

3.1.3.75

-

714874

-

3.1.6.6

uncompetitive inhibitor

135659

-

4.1.2.32

-

5136

-

4.1.2.32

non-competitive

5135

-

4.1.2.32

2 entries

4.1.3.27

reaction of component I with NH4+ as substrate

33277

-

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

1.12.98.1

4omf, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (22 results)

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Show Turnover Number (22 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.13.148

0.373

-

wild-type, pH 7, 25°C

764744

1.14.13.8

0.034

-

recombinant wild-type enzyme, pH 8.5

675603

1.14.13.8

0.051

-

recombinant mutant K416N, pH 8.5

675603

1.14.13.8

0.065

-

recombinant mutant E24D, pH 8.5

675603

1.14.13.8

1.25

-

mutant W47F, pH 8.5, 25°C

724128

1.14.13.8

2.6

-

at pH 8.0 and 25°C

742171

1.14.13.8

6.1

-

pH 8.5, 25°C

689806

1.14.13.8

6.1

-

wild-type, pH 8.5, 25°C

724128

1.5.8.2

0.25

-

mutant Y442G, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

0.5

-

mutant Y442G, electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

3.8

-

mutant Y442L, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

5.6

-

mutant delta725-729, electron acceptor: phenazine methosulfate

393892

1.5.8.2

6.4

-

mutant delta720-729, electron acceptor: phenazine methosulfate

393892

1.5.8.2

6.7

-

mutant V344I, electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

10.2

-

recombinant wild-type form, electron acceptor: phenazine methosulfate

393892

1.5.8.2

10.3

-

mutant Y442F, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

15.6

-

native wild-type form, electron acceptor: phenazine methosulfate

393892

1.5.8.2

16.5

-

wild-type form, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

16.8

-

electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

17

-

mutant C30A, electron acceptor: ferricenium hexafluorophosphate

393888

1.5.8.2

38

-

electron acceptor: ferricenium hexafluorophosphate

393888

1.5.8.2

40

-

recombinant enzyme, electron acceptor: ferricenium hexafluorophosphate

393888

1.14.13.8

7 entries

1.5.8.2

14 entries

K_M Value (36 results)

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Show KM Value (36 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.148

0.0003

-

in potassium diphosphate buffer (pH 7.7), at 14°C

717521

1.14.13.148

0.0094

-

recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

718325

1.14.13.148

0.013

0.0548

the Km for isoform FMO3 determined in human liver microsomes ranges from 0.013.to 0.0548 mM, at pH 7.4 and 22°C

717226

1.14.13.148

0.0208

-

recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

718325

1.14.13.148

0.0216

-

recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

718325

1.14.13.148

0.0275

-

recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

718325

1.14.13.148

0.028

-

recombinant isoform FMO3, at pH 7.4 and 22°C

717226

1.14.13.148

0.0285

-

recombinant enzyme, in 80 mM PIPES buffer (pH 7.6), at 22°C

718325

1.14.13.148

0.139

-

wild-type, pH 7, 25°C

764744

1.14.13.148

9 entries

1.14.13.238

0.00118

-

with NADH as cosubstrate, at pH 7.0 and 25°C

743014

1.14.13.8

0.0015

-

mutant W47F, pH 8.5, 25°C

724128

1.14.13.8

0.0026

-

wild-type, pH 8.5, 25°C

724128

1.14.13.8

0.00875

-

pH 8.4, 37°C, recombinant FMO3

687477

1.14.13.8

0.0202

-

at pH 8.0 and 30°C

742256

1.14.13.8

0.0209

-

recombinant wild-type enzyme, pH 8.5

675603

1.14.13.8

0.0228

-

recombinant mutant E24D, pH 8.5

675603

1.14.13.8

0.0373

-

recombinant mutant K416N, pH 8.5

675603

1.14.13.8

0.073

-

pH 8.5, 25°C

689806

1.14.13.8

0.58

-

at pH 8.0 and 25°C

742171

1.5.8.2

0.002

-

electron acceptor: phenazine methosulfate

393923

1.5.8.2

0.0046

-

mutant DELTA725-729, electron acceptor: phenazine methosulfate

393892

1.5.8.2

0.0047

-

mutant DELTA720-729, electron acceptor: phenazine methosulfate

393892

1.5.8.2

0.0096

-

recombinant wild-type form, electron acceptor: phenazine methosulfate

393892

1.5.8.2

0.0137

-

native wild-type form, electron acceptor: phenazine methosulfate

393892

1.5.8.2

0.0143

-

mutant Y442F, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

0.0148

-

wild-type form, electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

0.017

-

electron acceptor: ferricenium hexafluorophosphate, wild-type enzyme

393888

1.5.8.2

0.0175

-

wild-type form, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

0.019

-

electron acceptor: ferricenium hexafluorophosphate, recombinant enzyme

393888

1.5.8.2

0.0196

-

mutant Y442L, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

0.0242

-

mutant V344I, electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

0.0262

-

mutant Y442G, electron acceptor: electron transferring flavoprotein

393891

1.5.8.2

0.0659

-

mutant Y442G, electron acceptor: electron transferring flavoprotein

393895

1.5.8.2

2

-

electron acceptor: ferricenium hexafluorophosphate, mutant C30A

393888

1.5.8.2

4

-

pH 7.4, 30°C

711031

1.5.8.2

4

-

pH not specified in the publication, temperature not specified in the publication

711031

1.14.13.8

9 entries

1.5.8.2

17 entries

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.17

2.4

-

pH 8.0, 25°C

654371

1.5.8.2

0.75

-

-

393893

References & Links

Literature References (118)

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Show Reference (118 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5135

5116524

The metabolism of trimethylamine N-oxide by Bacillus PM 6

1971

Myers, P.A.; Zatman, L.J.

Biochem. J.

121

10P

5136

3759939

Characterisation of trimethylamine-N-oxide (TMAO) demethylase activity from fish muscle microsomes

1986

Parkin, K.L.; Hultin, H.O.

J. Biochem.

100

77-86

33277

4878701

Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium

1968

Zalkin, H.; Kling, D.

Biochemistry

7

3566-3573

135659

4196744

Choline sulfatase of Pseudomonas aeruginosa

1972

Lucas, J.J.; Burchiel, S.W.; Segel, I.H.

Arch. Biochem. Biophys.

153

664-672

285737

8645721

Purification and properties of L(-)-carnitine dehydrogenase from Agrobacterium sp.

1996

Hanschmann, H.; Ehricht, R.; Kleber, H.P.

Biochim. Biophys. Acta

1290

177-183

348497

3925885

Catalytic activity and substrate specificity of the flavin-containing monooxygenase in microsomal systems: characterization of the hepatic, pulmonary and renal enzymes of the mouse, rabbit, and rat

1985

Tynes, R.E.; Hodgson, E.

Arch. Biochem. Biophys.

240

77-93

348501

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Links to other databases for trimethylamine

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