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Ligand 4-trimethylammoniobutanal

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 4-trimethylammoniobutanal

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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

1.2.1.47

4-(trimethylamino)butyraldehyde + NAD+ + H2O = 4-(trimethylamino)butyrate + NADH + 2 H+

762831

-

1.2.1.47

4-N-trimethylaminobutyraldehyde + NAD+ + H2O = gamma-butyrobetaine + NADH + H+

724438, 726537

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ + H2O = 4-N-trimethylaminobutyrate + NADH + H+

762675

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ = 4-trimethylaminobutanoate + NADH + H+

671302

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ = 4-trimethylaminobutyrate + NADH + H+

288255, 288254

-

1.2.1.47

4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+

671302, 763484, 743576

-

1.2.1.47

trimethylaminobutyraldehyde + NAD+ + H2O = gamma-butyrobetaine + NADH + 2 H+

699966

-

1.2.1.47

7 entries

Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Substrate (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.19

N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O = N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+

742854

-

1.2.1.19

N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O = N,N,N-trimethyl-4-aminobutanoate + NADH + H+

712753

-

1.2.1.47

4-(trimethylamino)butyraldehyde + NAD+ + H2O = 4-(trimethylamino)butyrate + NADH + 2 H+

762831

-

1.2.1.47

4-N-trimethylaminobutyraldehyde + NAD+ + H2O = gamma-butyrobetaine + NADH + H+

724438, 726537

-

1.2.1.47

4-N-trimethylaminobutyraldehyde + NAD+ = 4-N-trimethylaminobutanoate + NADH

691376

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ + H2O = 4-N-trimethylaminobutyrate + NADH + H+

762675

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ = 4-trimethylaminobutanoate + NADH + H+

671302

-

1.2.1.47

4-trimethylaminobutyraldehyde + NAD+ = 4-trimethylaminobutyrate + NADH + H+

288254, 288255

-

1.2.1.47

4-trimethylaminobutyraldehyde + NADP+ + H2O = 4-trimethylaminobutyrate + NADPH + H+

288255

-

1.2.1.47

4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+

671302, 763484, 743576

-

1.2.1.47

trimethylaminobutyraldehyde + NAD+ + H2O = gamma-butyrobetaine + NADH + 2 H+

699966

-

1.2.1.8

4-N-trimethylaminobutyraldehyde + NAD(P)+ + H2O = ?

695893

-

1.2.1.8

4-N-trimethylaminobutyraldehyde + NAD+ + H2O = 4-N-trimethylaminobutyrate + NADH + H+

712013

-

1.2.1.8

4-N-trimethylaminobutyraldehyde + NAD+ + H2O = 4-N-trmethylaminobutanoate + NADH + H+

741442

-

1.2.1.8

4-N-trimethylaminobutyraldehyde + NAD+ + H2O = ?

700697

-

1.2.1.8

4-trimethylaminobutyraldehyde + NAD+ + H2O = 3-trimethylaminobutyrate + NADH

390357

-

1.2.1.19

2 entries

1.2.1.47

9 entries

1.2.1.8

5 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.19

substrate inhibition; substrate inhibition

742854

-

1.2.1.47

-

762831

-

1.2.1.47

the substrate inhibits at 0.24 mM

691376

-

1.2.1.47

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (5 results)

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Show Turnover Number (5 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.19

2

-

pH 9.0, 37°C

742854

1.2.1.19

3.6

-

pH 9.0, 37°C

742854

1.2.1.19

5.1

-

pH 9.0, 37°C

742854

1.2.1.19

5.7

-

pH 9.0, 37°C

742854

1.2.1.19

10.8

-

pH 9.0, 37°C

742854

1.2.1.19

5 entries

K_M Value (16 results)

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Show KM Value (16 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.19

0.006

-

pH 9.0, 37°C

742854

1.2.1.19

0.01

-

isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C

712753

1.2.1.19

0.01

-

pH 9.0, 37°C

742854

1.2.1.19

0.016

-

pH 9.0, 37°C

742854

1.2.1.19

0.017

-

pH 9.0, 37°C

742854

1.2.1.19

0.021

-

isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C

712753

1.2.1.19

0.141

-

pH 9.0, 37°C

742854

1.2.1.47

0.0014

-

-

288255

1.2.1.47

0.00417

-

-

288254

1.2.1.47

0.006

-

pH 7.5, temperature not specified in the publication

762831

1.2.1.47

0.0074

-

-

691376

1.2.1.47

0.31

-

at pH 9.5 and 30°C

726537

1.2.1.8

0.0014

-

cytoplasmic enzyme

390357

1.2.1.8

0.0078

-

isozyme BADH1, pH and temperature not specified in the publication

712013

1.2.1.8

0.0221

-

at pH 8.0 and 30°C

741442

1.2.1.8

0.041

-

isozyme BADH2, pH and temperature not specified in the publication

712013

1.2.1.19

7 entries

1.2.1.47

5 entries

1.2.1.8

4 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.19

0.09

-

pH 9.0, 37°C

742854

1.2.1.19

1.56

-

pH 9.0, 37°C

742854

1.2.1.19

2 entries

1.2.1.47

7.23

-

pH 7.5, temperature not specified in the publication

762831

References & Links

Literature References (18)

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Show Reference (18 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

288254

7356654

Carnitine biosynthesis. Purification of 4-N-trimethylaminobutyraldehyde dehydrogenase from beef liver

1980

Hulse, J.D.; Henderson, L.M.

J. Biol. Chem.

255

1146-1151

288255

10702312

Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis

2000

Vaz, F.M.; Fouchier, S.W.; Ofman, R.; Sommer, M.; Wanders, R.J.A.

J. Biol. Chem.

275

7390-7394

390357

11306043

Betaine aldehyde dehydrogenase from rat liver mitochondrial matrix

2001

Pietruszko, R.; Chern, M.K.

Chem. Biol. Interact.

130-132

193-199

671302

16707092

Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: differences between the mouse and the rat

2006

van Vlies, N.; Wanders, R.J.; Vaz, F.M.

Anal. Biochem.

354

132-139

691376

18175913

4-N-trimethylaminobutyraldehyde dehydrogenase: purification and characterization of an enzyme from Pseudomonas sp. 13CM

2008

Hassan, M.; Okada, M.; Ichiyanagi, T.; Mori, N.

Biosci. Biotechnol. Biochem.

72

155-162

695893

19766587

Kinetic and structural features of betaine aldehyde dehydrogenases: Mechanistic and regulatory implications

2010

Munoz-Clares, R.A.; Diaz-Sanchez, A.G.; Gonzalez-Segura, L.; Montiel, C.

Arch. Biochem. Biophys.

493

71-81

699966

19150623

Ontogeny of Na(+)/L-carnitine transporter and of gamma-trimethylaminobutyraldehyde dehydrogenase and gamma-butyrobetaine hydroxylase genes expression in rat kidney

2009

Garcia-Delgado, M.; Peral, M.J.; Duran, J.M.; Garcia-Miranda, P.; Calonge, M.L.; Ilundain, A.A.

Mech. Ageing Dev.

130

227-233

700697

19228319

Betaine aldehyde dehydrogenase in plants

2009

Fitzgerald, T.L.; Waters, D.L.; Henry, R.J.

Plant Biol.

11

119-130

712013

19850038

OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes

2009

Mitsuya, S.; Yokota, Y.; Fujiwara, T.; Mori, N.; Takabe, T.

FEBS Lett.

583

3625-3629

712753

20026072

Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes

2010

Tylichova, M.; Kopecny, D.; Morera, S.; Briozzo, P.; Lenobel, R.; Snegaroff, J.; Sebela, M.

J. Mol. Biol.

396

870-882

724438

22285688

The mouse gene encoding the carnitine biosynthetic enzyme 4-N-trimethylaminobutyraldehyde dehydrogenase is regulated by peroxisome proliferator-activated receptor alpha

2012

Wen, G.; Ringseis, R.; Rauer, C.; Eder, K.

Biochim. Biophys. Acta

1819

357-365

726537

23225139

Gene cloning and biochemical characterization of 4-N-trimethylaminobutyraldehyde dehydrogenase II from Pseudomonas sp. 13CM

2013

Bari, M.R.; Hassan, M.; Akai, N.; Arima, J.; Mori, N.

World J. Microbiol. Biotechnol.

29

683-692

741442

25992309

Functional and expression analyses of two kinds of betaine aldehyde dehydrogenases in a glycinebetaine-hyperaccumulating graminaceous halophyte, Leymus chinensis

2015

Mitsuya, S.; Tsuchiya, A.; Kono-Ozaki, K.; Fujiwara, T.; Takabe, T.; Takabe, T.

SpringerPlus

4

202

742854

23408433

Plant ALDH10 family identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate

2013

Kopecny, D.; Koncitikova, R.; Tylichova, M.; Vigouroux, A.; Moskalikova, H.; Soural, M.; Sebela, M.; Morera, S.

J. Biol. Chem.

288

9491-9507

743576

26010099

Identification of 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) as a candidate serum autoantibody target for Kawasaki disease

2015

Matsunaga, A.; Harita, Y.; Shibagaki, Y.; Shimizu, N.; Shibuya, K.; Ono, H.; Kato, H.; Sekine, T.; Sakamoto, N.; Igarashi, T.; Hattori, S.

PLoS ONE

10

e0128189

762675

32717224

Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1

2020

Wyatt, J.W.; Korasick, D.A.; Qureshi, I.A.; Campbell, A.C.; Gates, K.S.; Tanner, J.J.

Arch. Biochem. Biophys.

691

108477

762831

30914451

Kinetic and structural analysis of human ALDH9A1

2019

Koncitikova, R.; Vigouroux, A.; Kopecna, M.; Sebela, M.; Morera, S.; Kopecny, D.

Biosci. Rep.

39

BSR20190558

763484

31500110

Carnitine inborn errors of metabolism

2019

Almannai, M.; Alfadhel, M.; El-Hattab, A.W.

Molecules

24

3251

Links to other databases for 4-trimethylammoniobutanal

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Show Links (1 entry)

ChEBI

PubChem