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Ligand gamma-butyrobetaine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for gamma-butyrobetaine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.1

4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2

711108, 744503, 744690, 745521, 745684, 745953, 764457, 765384, 744717, 763867, 439286

3o2g, 3D-view

3.4.22.52

alpha-actinin + H2O = ?

708194

-

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

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.47

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

0

-

1.2.1.47

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

0

-

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+

0

-

1.2.1.47

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

0

-

1.2.1.47

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

0

-

1.2.1.47

6 entries

3.1.3.48

phosphorylated alpha-actinin + H2O = alpha-actinin + phosphate

0

-

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.11.1

4-(trimethylammonio)butanoic acid + 2-oxoglutarate + O2 = ?

727308

3o2g, 3D-view

1.14.11.1

4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2

439296, 439287, 439289, 439285, 439290, 439291, 439297, 439301, 439286, 439295, 439284, 439288, 439292, 439293, 439294, 711108, 744503, 744690, 745521, 745684, 745953, 764457, 765384, 744717, 763867, 439283

3o2g, 3D-view

1.14.11.1

gamma-butyrobetaine + 2-oxoglutarate + O2 = carnitine + succinate + CO2

727308, 697453

3o2g, 3D-view

1.14.11.1

3 entries

1.14.13.239

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

765072

6y8s, 3D-view

2.1.1.383

gamma-butyrobetaine + cob(I)alamin = methylcob(I)alamin + 4-(dimethylamino)butanoate

763267

-

2.1.1.B141

gamma-butyrobetaine + [corrinoid-binding protein Co(I)-MtqC] = [methyl-corrinoid-protein Co(I)-MtqC] + 4-(dimethylamino)butanoate

763275

-

3.4.22.52

alpha-actinin + H2O = ?

708194

-

6.2.1.48

ATP + gamma-butyrobetaine + CoA = AMP + diphosphate + gamma-butyrobetainyl-CoA

740589

-

Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.17

4-trimethylamino-1-butanol + 2 O2 + H2O = 4-trimethylaminobutanoate + 2 H2O2

0

-

1.2.1.19

N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O = gamma-butyrobetaine + NADH + H+

0

-

1.2.1.47

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

0

-

1.2.1.47

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

0

-

1.2.1.47

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

0

-

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+

0

-

1.2.1.47

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

0

-

1.2.1.47

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

0

-

1.2.1.47

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

0

-

1.2.1.8

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

0

-

1.2.1.8

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

0

-

1.2.1.47

8 entries

1.2.1.8

2 entries

1.3.8.13

crotonobetaine + reduced benzylviologen = gamma-butyrobetaine + oxidized benzylviologen

0

-

2.8.3.21

4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA

0

-

2.8.3.21

gamma-butyrobetainyl-CoA + L-carnitine = gamma-butyrobetaine + L-carnitinyl-CoA

0

-

2.8.3.21

2 entries

3.1.3.48

phosphorylated alpha-actinin + H2O = alpha-actinin + phosphate

0

-

Inhibitor in Enzyme-catalyzed Reactions (15 results)

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Show Inhibitors (15 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.108

competitive inhibition vs. L-carnitine

285744

-

1.1.1.254

competitive inhibitor of (S)-carnitine oxidation; D-carnitine dehydrogenase, competitive inhibition

9589

-

1.14.11.1

substrate inhibition

745953

3o2g, 3D-view

1.14.11.1

substrate inhibition associated with age is observed at concentrations above 0.6 mM

763867

3o2g, 3D-view

1.14.11.1

substrate inhibition at concentrations above 0.2 mM

711108

3o2g, 3D-view

1.14.11.1

substrate inhibition at high concentrations

745953

3o2g, 3D-view

1.14.11.1

at concentrations above 0.2 mM

439301

3o2g, 3D-view

1.14.11.1

GBB, substrate inhibition at high concentrations

744690

3o2g, 3D-view

1.14.11.1

substrate inhibition at high concentrations. Enzyme-inhibitor interactions from structure PDB ID 3MS5

745521

3o2g, 3D-view

1.3.8.13

350 mM, complete loss of activity

740464

-

1.3.8.13

competitive, 100 mM, complete loss of activity

739868

-

1.14.11.1

7 entries

1.3.8.13

2 entries

2.3.1.21

-

486523

-

2.3.1.7

competitive inhibition

487398

-

2.7.11.15

-

672408, 677232

-

2.7.11.16

-

672408

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.11.1

3o2g, 3D-view

1.14.13.239

6y8s, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.11.1

0.83

-

pH 7.5, temperature not specified in the publication

745953

1.14.11.1

5.3

-

co-substrate: 2-oxoglutarate, pH 7.5, 25°C, NMR assay

727308

1.14.11.1

7.02

-

pH 7.5, 23°C

744717

1.14.11.1

21.3

-

pH 7.5, temperature not specified in the publication

745953

1.14.11.1

34

-

-

439284

1.14.11.1

5 entries

2.1.1.B141

3

-

pH 7.2, 37°C

763275

K_M Value (25 results)

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Show KM Value (25 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.11.1

0.0042

-

pH 7.5, temperature not specified in the publication

745953

1.14.11.1

0.013

-

apparent kinetic constant (Km), in liver of 1-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.025

-

apparent kinetic constant (Km), in liver of 7-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.026

-

apparent kinetic constant (Km), in liver of 56-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.0275

-

pH 7.0, 37°C, recombinant enzyme

711108

1.14.11.1

0.029

-

-

439291

1.14.11.1

0.032

-

apparent kinetic constant (Km), in kidney of 1-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.037

-

apparent kinetic constant (Km), in kidney of 56-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.038

-

apparent kinetic constant (Km), in liver of 21-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.041

-

apparent kinetic constant (Km), in liver of 35-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.053

-

apparent kinetic constant (Km), in liver of newborn domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.06

-

apparent kinetic constant (Km), in liver of 210-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.061

-

apparent kinetic constant (Km), in kidney of 7-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.063

-

apparent kinetic constant (Km), in kidney of 21-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.074

-

apparent kinetic constant (Km), in kidney of 210-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.08

-

-

439301

1.14.11.1

0.086

-

apparent kinetic constant (Km), in kidney of 35-day-old domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.119

-

apparent kinetic constant (Km), in kidney of newborn domestic pig, pH 7.4, 37°C

763867

1.14.11.1

0.16

-

co-substrate: 2-oxoglutarate, pH 7.5, 25°C, NMR assay

727308

1.14.11.1

0.163

-

pH 7.5, temperature not specified in the publication, only the Michaelis-Menten range is fitted

745953

1.14.11.1

0.51

-

-

439286

1.14.11.1

1

-

pH 7.5, 23°C

744717

1.14.11.1

2.4

-

-

439292

1.14.11.1

2.474

-

pH 7.5, temperature not specified in the publication, the whole range is fitted

745953

1.14.11.1

24 entries

2.1.1.B141

3.5

-

pH 7.2, 37°C

763275

K_i Value (5 results)

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Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.11.1

0.024

-

pH 7.5, temperature not specified in the publication

745953

1.14.11.1

0.125

-

pH 7.5, temperature not specified in the publication

745953

1.14.11.1

2 entries

1.3.8.13

0.03

-

pH 8.0, 37°C

739868

2.3.1.7

1.2

-

-

487398

2.3.1.7

2.3

-

-

487398

2.3.1.7

2 entries

References & Links

Literature References (43)

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Show Reference (43 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

9589

9003445

Purification and characterization of D(+)-carnitine dehydrogenase from Agrobacterium sp. - a new enzyme of carnitine metabolism

1997

Hanschmann, H.; Kleber, H.P.

Biochim. Biophys. Acta

1337

133-142

285744

4310279

Kinetische Untersuchungen zum Reaktionsmechanismus der Carnitindehydrogenase aus Pseudomonas aeruginosa

1969

Schnöpp, W.; Sorger, H.; Kleber, H-P.; Aurich, H.

Eur. J. Biochem.

10

56-60

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

439283

4396068

Cofactor requirements of gamma-butyrobetaine hydroxylase from rat liver

1970

Lindstedt, G.; Lindstedt, S.

J. Biol. Chem.

245

4178-4186

439284

861203

Purification and properties of gamma-butyrobetaine hydroxylase from Pseudomonas sp AK 1

1977

Lindstedt, G.; Lindstedt, S.; Nordin, I.

Biochemistry

16

2181-2188

439285

7358151

A rapid and sensitive assay of gamma-butyrobetaine hydroxylase

1980

Carter, A.L.; Stratman, F.W.

FEBS Lett.

111

112-114

439286

6798936

Purification and properties of calf liver gamma-butyrobetaine hydroxylase

1981

Kondo, A.; Blanchard, J.S.; Englard, S.

Arch. Biochem. Biophys.

212

338-346

439287

7126226

Uncoupling in the gamma-butyrobetaine hydroxylase reaction by D- and L-carnitine

1982

Holme, E.; Lindstedt, S.; Nordin, I.

Biochem. Biophys. Res. Commun.

107

518-524

439288

7165306

gamma-Butyrobetaine hydroxylase: A unique protctive effect of catalase

1982

Blanchard, J.S.; Englard, S.; Kondo, A.

Arch. Biochem. Biophys.

219

327-334

439289

6497835

Multiple forms of gamma-butyrobetaine hydroxylase (EC 1.14.11.1)

1984

Lindstedt, S.; Nordin, I.

Biochem. J.

223

119-127

439290

3571282

gamma-Butyrobetaine hydroxylase and the protective role of glutathione peroxidase

1987

Punekar, N.S.; Wehbie, R.S.; Lardy, H.A.

J. Biol. Chem.

262

6720-6724

439291

3378057

Rat liver gamma-butyrobetaine hydroxylase catalyzed reaction: influence of potassium, substrates, and substrate analogues on hydroxylation and decarboxylation

1988

Wehbie, R.S.; Punekar, N.S.; Lardy, H.A.

Biochemistry

27

2222-2228

439292

-

Mechanism-based inhibition of bacterial gamma-butyrobetaine hydroxylase

1990

Ziering, D.L.; Pascal, R.A.

J. Am. Chem. Soc.

112

834-838

439293

1988434

Cosubstrate binding site of Pseudomonas sp. AK1 gamma-butyrobetaine hydroxylase. Interactions with structural analogs of alpha-ketoglutarate

1991

Ng, S.F.; Hanauske-Abel, H.M.; Englard, S.

J. Biol. Chem.

266

1526-1533

439294

-

Inhibition of gamma-butyrobetaine hydroxylase by cyclopropyl-substituted gamma-butyrobetaines

1990

Petter, R.C.; Banerjee, S.; Englard, S.

J. Org. Chem.

55

3088-3097

439295

4096892

gamma-Butyrobetaine hydroxylase: stereochemical course of the hydroxylation reaction

1985

Englard, S.; Blanchard, J.S.; Midelfort, C.F.

Biochemistry

24

1110-1116

439296

6432788

Carnitine biosynthesis from gamma-butyrobetaine and from exogenous protein-bound 6-N-trimethyl-L-lysine by the perfused guinea pig liver. Effect of ascorbate deficiency on the in situ activity of gamma-butyrobetaine hydroxylase

1984

Dunn, W.A.; Rettura, G.; Seifter, E.; Englard, S.

J. Biol. Chem.

259

10764-10770

439297

4382529

Hydroxylation of gamma-butyrobetaine to carnitine in rat liver

1967

Lindstedt, G.

Biochemistry

6

1271-1282

439301

9546596

Purification and characterization of the rat liver gamma-butyrobetaine hydroxylase

1998

Galland, S.; Le Borgne, F.; Guyonnet, D.; Clouet, P.; Demarquoy, J.

Mol. Cell. Biochem.

178

163-168

486523

-

Purification and properties of an easily solubilized L-carnitine palmitoyltransferase from beef liver mitochondria

1986

Derrick, J.P.; Tubbs, P.K.; Ramsay, R.R.

Biochem. Soc. Trans.

14

698

487398

14299645

Carnitine acetyltransferase. II. Inhibition by carnitine analogues and by sulfhydryl reagents

1965

Fritz, I.B.; Schultz, S.K.

J. Biol. Chem.

240

2188-2192

672408

17084806

The G protein-coupled receptor kinase (GRK) interactome: Role of GRKs in GPCR regulation and signaling

2007

Ribas, C.; Penela, P.; Murga, C.; Salcedo, A.; Garcia-Hoz, C.; Jurado-Pueyo, M.; Aymerich, I.; Mayor, F.

Biochim. Biophys. Acta

1768

913-922

677232

16781951

Role of G-protein-coupled receptor kinase 2 in the heart--do regulatory mechanisms open novel therapeutic perspectives?

2006

Hansen, J.L.; Theilade, J.; Aplin, M.; Sheikh, S.P.

Trends Cardiovasc. Med.

16

169-177

697453

19285565

Activities of gamma-butyrobetaine dioxygenase and concentrations of carnitine in tissues of pigs

2009

Fischer, M.; Keller, J.; Hirche, F.; Kluge, H.; Ringseis, R.; Eder, K.

Comp. Biochem. Physiol. A

153

324-331

708194

19793101

Calpains, skeletal muscle function and exercise

2010

Murphy, R.M.

Clin. Exp. Pharmacol. Physiol.

37

385-391

711108

20599753

Crystal structure of human gamma-butyrobetaine hydroxylase

2010

Tars, K.; Rumnieks, J.; Zeltins, A.; Kazaks, A.; Kotelovica, S.; Leonciks, A.; Sharipo, J.; Viksna, A.; Kuka, J.; Liepinsh, E.; Dambrova, M.

Biochem. Biophys. Res. Commun.

398

634-639

727308

22730246

Development and application of a fluoride-detection-based fluorescence assay for gamma-butyrobetaine hydroxylase

2012

Rydzik, A.M.; Leung, I.K.; Kochan, G.T.; Thalhammer, A.; Oppermann, U.; Claridge, T.D.; Schofield, C.J.

ChemBioChem

13

1559-1563

739868

8060125

Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(-)-carnitine

1994

Roth, S.; Jung, K.; Jung, H.; Hommel, R.; Kleber, H.

Antonie van Leeuwenhoek

65

63-69

740464

11257539

Epigenetic regulation of carnitine metabolising enzymes in Proteus sp. under aerobic conditions

2001

Engemann, C.; Kleber, H.P.

FEMS Microbiol. Lett.

196

1-6

740589

18266698

Role of betaine:CoA ligase (CaiC) in the activation of betaines and the transfer of coenzyme A in Escherichia coli

2008

Bernal, V.; Arense, P.; Blatz, V.; Mandrand-Berthelot, M.A.; Canovas, M.; Iborra, J.L.

J. Appl. Microbiol.

105

42-50

744503

25266780

Ejection of structural zinc leads to inhibition of gamma-butyrobetaine hydroxylase

2014

Rydzik, A.M.; Brem, J.; Struwe, W.B.; Kochan, G.T.; Benesch, J.L.; Schofield, C.J.

Bioorg. Med. Chem. Lett.

24

4954-4957

744690

26682037

Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of gamma-butyrobetaine hydroxylase

2014

Rydzik, A.M.; Chowdhury, R.; Kochan, G.T.; Williams, S.T.; McDonough, M.A.; Kawamura, A.; Schofield, C.J.

Chem. Sci.

5

1765-1771

744717

26660433

Cation-Pi interactions contribute to substrate recognition in gamma-butyrobetaine hydroxylase catalysis

2016

Kamps, J.J.; Khan, A.; Choi, H.; Lesniak, R.K.; Brem, J.; Rydzik, A.M.; McDonough, M.A.; Schofield, C.J.; Claridge, T.D.; Mecinovic, J.

Chemistry

22

1270-1276

745521

24571165

Targeting carnitine biosynthesis discovery of new inhibitors against gamma-butyrobetaine hydroxylase

2014

Tars, K.; Leitans, J.; Kazaks, A.; Zelencova, D.; Liepinsh, E.; Kuka, J.; Makrecka, M.; Lola, D.; Andrianovs, V.; Gustina, D.; Grinberga, S.; Liepinsh, E.; Kalvinsh, I.; Dambrova, M.; Loza, E.; Pugovics, O.

J. Med. Chem.

57

2213-2236

745684

-

Development and application of ligand-based NMR screening assays for gamma-butyrobetaine hydroxylase

2016

Khan, A.; Lesniak, R.; Brem, J.; Rydzik, A.; Choi, H.; Leung, I.; McDonough, M.; Schofield, C.; Claridge, T.

MedChemComm

7

873-880

745953

25030770

Comparison of the substrate selectivity and biochemical properties of human and bacterial gamma-butyrobetaine hydroxylase

2014

Rydzik, A.M.; Leung, I.K.; Kochan, G.T.; Loik, N.D.; Henry, L.; McDonough, M.A.; Claridge, T.D.; Schofield, C.J.

Org. Biomol. Chem.

12

6354-6358

763267

32571881

MtcB, a member of the MttB superfamily from the human gut acetogen Eubacterium limosum, is a cobalamindependent carnitine demethylase

2020

Kountz, D.; Behrman, E.; Zhang, L.; Krzycki, J.

J. Biol. Chem.

295

11971-11981

763275

34688665

The MttB superfamily member MtyB from the human gut symbiont Eubacterium limosum is a cobalamin-dependent gamma-butyrobetaine methyltransferase

2021

Ellenbogen, J.; Jiang, R.; Kountz, D.; Zhang, L.; Krzycki, J.

J. Biol. Chem.

297

101327

763867

32432915

Ontogeny of carnitine biosynthesis in Sus scrofa domesticus, inferred from gamma-butyrobetaine hydroxylase (dioxygenase) activity and substrate inhibition

2020

Lin, X.; Lyvers Peffer, P.A.; Woodworth, J.; Odle, J.

Am. J. Physiol. Regul. Integr. Comp. Physiol.

319

R43-R49

764457

31702759

19F NMR studies on gamma-butyrobetaine hydroxylase provide mechanistic insights and suggest a dual inhibition mode

2019

Lesniak, R.K.; Rydzik, A.M.; Kamps, J.J.A.G.; Kahn, A.; Claridge, T.D.W.; Schofield, C.J.

Chem. Commun. (Camb.)

55

14717-14720

765072

33158989

Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer

2021

Quareshy, M.; Shanmugam, M.; Townsend, E.; Jameson, E.; Bugg, T.; Cameron, A.; Chen, Y.

J. Biol. Chem.

296

100038

765384

33241108

BBOX1 promotes triple-negative breast cancer progression by controlling IP3R3 stability

2020

Liao, C.; Zhang, Q.

Mol. Cell. Oncol.

7

1813526

Links to other databases for gamma-butyrobetaine

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ChEBI

PubChem