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Ligand bis(3-aminopropyl)amine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for bis(3-aminopropyl)amine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.57

acetyl-CoA + norspermidine = CoA + N1-acetylnorspermidine

757687

-

2.5.1.126

S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine

727512

-

2.5.1.127

S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine

727512

-

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

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Show Natural Product (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.17

thermospermine + O2 + H2O = norspermidine + 3-acetamidopropanal + H2O2

0

-

2.5.1.126

S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-5'-thioadenosine + norspermidine

0

-

2.5.1.23

S-adenosylmethioninamine + propane-1,3-diamine = 5'-methylthioadenosine + N-(3-aminopropyl)-1,3-diaminopropane

0

-

Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Substrate (14 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.14

norspermidine + O2 + H2O = 1,3-diaminopropane + H2O2 + ?

743455

-

1.5.3.16

norspermidine + O2 + H2O = ?

690790

-

1.5.3.17

norspermidine + O2 + H2O = ?

690790

-

1.5.99.6

3,3'-diaminodipropylamine + electron acceptor = ? + reduced electron acceptor

392547

-

1.5.99.6

N-(3-aminopropyl)-1,3-diaminopropane + electron acceptor = ? + reduced electron acceptor

392548, 392551

-

1.5.99.6

N-(3-aminopropyl)-1,3-propanediamine + electron acceptor = ? + reduced electron acceptor

392545, 392546

-

2.3.1.57

acetyl-CoA + norspermidine = CoA + N1-acetylnorspermidine

757687, 660954

-

2.3.1.57

acetyl-CoA + sym-norspermidine = CoA + N1-acetyl-sym-norspermidine

487258, 701662, 487259, 487256, 487257

-

1.5.99.6

3 entries

2.3.1.57

2 entries

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + N,N'-bis(3-aminopropyl)-1,3-propanediamine

720250

-

2.5.1.126

S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine

727512

-

2.5.1.127

S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine

727512

-

2.5.1.22

S-adenosylmethioninamine + sym-norspermidine = 5'-methylthioadenosine + ?

489861

-

2.5.1.23

S-adenosylmethioninamine + sym-norspermidine = 5'-S-methyl-5'-thioadenosine + ?

719387

-

2.5.1.46

caldine + putrescine = spermidine + ?

638083

-

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.16

thermospermine + O2 + H2O = norspermidine + ?

0

-

1.5.3.17

thermospermine + O2 + H2O = norspermidine + 3-acetamidopropanal + H2O2

0

-

1.5.3.17

thermospermine + O2 + H2O = norspermidine + ?

0

-

1.5.3.17

2 entries

2.5.1.104

S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = 5'-S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine

0

-

2.5.1.126

S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-5'-thioadenosine + norspermidine

0

-

2.5.1.127

S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-5'-thioadenosine + norspermidine

0

-

2.5.1.23

S-adenosyl 3-(methylthio)propylamine + propane-1,3-diamine = S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine

0

-

2.5.1.23

S-adenosylmethioninamine + propane-1,3-diamine = 5'-S-methyl-5'-thioadenosine + bis(3-aminopropyl)amine

0

-

2.5.1.23

S-adenosylmethioninamine + propane-1,3-diamine = 5'-methylthioadenosine + N-(3-aminopropyl)-1,3-diaminopropane

0, 638427

-

2.5.1.23

3 entries

4.1.1.96

carboxynorspermidine = bis(3-aminopropyl)amine + CO2

0

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.7.8

optimal polymerization activity requires presence, 2fold increase in activity at 30 mM

643694

-

Inhibitor in Enzyme-catalyzed Reactions (7 results)

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Show Inhibitors (7 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.14.99.29

47% of initial activity at 0.5 mM

438288

-

1.4.1.B4

10 mM, 10% inhibition

712623

-

2.5.1.22

weak

489867

-

2.5.1.46

-

638076

-

2.5.1.46

inhibition of deoxyhypusine synthesis

638083

-

2.5.1.46

1 mM, less than 50% inhibition

638076

-

2.5.1.46

3 entries

2.6.1.13

-

721755

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (3 results)

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Show Turnover Number (3 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.5.3.14

1.1

-

pH 6.5, 30°C

743455

1.5.3.14

2.3

-

pH 7.0, 37°C

743455

1.5.3.14

2 entries

2.5.1.104

0.53

-

pH 9.0, 37°C

720250

K_M Value (10 results)

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Show KM Value (10 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.5.3.14

0.109

-

pH 7.0, 37°C

743455

1.5.3.14

0.1578

-

pH 6.5, 30°C

743455

1.5.3.14

2 entries

1.5.3.16

5

-

pH 8.5, 37°C

690790

1.5.3.17

5

-

pH 8.5, 37°C

690790

1.5.99.6

0.047

-

-

392548

2.3.1.57

0.008

-

-

487257

2.3.1.57

0.015

-

pH 7.8, 37°C, SSAT in hepatoma cells

701662

2.3.1.57

0.5

-

-

487256

2.3.1.57

3 entries

2.5.1.104

0.57

-

pH 9.0, 37°C

720250

2.5.1.23

0.954

-

pH 7.5, 78°C

719387

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.6.1.13

13

-

pH 8.0, 37°C

721755

References & Links

Literature References (26)

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Show Reference (26 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

392545

4628436

Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines

1972

Tabor, H.; Tabor, C.W.

Adv. Enzymol. Relat. Areas Mol. Biol.

36

203-268

392546

4918845

Identification of flavin adenine dinucleotide and heme in a homogeneous spermidine dehydrogenase from Serratia marcescens

1970

Tabor, C.W.; Kellog, P.D.

J. Biol. Chem.

245

5424-5433

392547

376503

Spermidine dehydrogenase (Serratia marcescens)

1971

Tabor, C.W.; Kellog, P.D.

Methods Enzymol.

17B

746-753

392548

376502

Affinity chromatography of putrescine oxidase from Micrococcus rubens and spermidine dehydrogenase from Serratia marcescens

1979

Okada, M.; Kawashima, S.; Imahori, K.

J. Biochem.

85

1225-1233

392551

-

Effect of bivalent metal ions on the formation of spermidine dehydrogenase in Citrobacter freundii

1990

Hisano, T.; Abe, S.; Wakashiro, M.; Kimura, A.; Murata, K.

J. Ferment. Bioeng.

70

280-282

438288

2765563

Inhibition of deoxyhypusine hydroxylase by polyamines and by a deoxyhypusine peptide

1989

Abbruzzese, A.; Park, M.H.; Beninati, S.; Folk, J.E.

Biochim. Biophys. Acta

997

248-255

487256

3987688

The occurrence, subcellular localization and partial purification of diamine acetyltransferase in the yeast Candida boidinii grown on spermidine or putrescine as sole nitrogen source

1985

Haywood, G.W.; Large, P.J.

Eur. J. Biochem.

148

277-283

487257

7150547

Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver

1982

Della Ragione, F.; Pegg, A.E.

Biochemistry

21

6152-6158

487258

6621393

Spermidine N1-acetyltransferase

1983

Della Ragione, F.; Pegg, A.E.

Methods Enzymol.

94

321-325

487259

2775189

A novel type of putrescine (diamine)-acetylating enzyme from the nematode Ascaris suum

1989

Wittich, R.M.; Walter, R.D.

Biochem. J.

260

265-269

489861

6798961

Specificity of mammalian spermidine synthase and spermine synthase

1981

Pegg, A.E.; Shuttleworth, K.; Hibasami, H.

Biochem. J.

197

315-320

489867

6621389

Inhibition of aminopropyltransferases

1983

Pegg, A.E.

Methods Enzymol.

94

294-297

638076

8514754

Features of the spermidine-binding site of deoxyhypusine synthase as derived from inhibition studies. Effective inhibition by bis- and mono-guanylated diamines and polyamines

1993

Jakus, J.; Wolff, E.C.; Park, M.H.; Folk, J.E.

J. Biol. Chem.

268

13151-13159

638083

12788913

Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase

2003

Park, J.H.; Wolff, E.C.; Folk, E.C.; Park, M.H.

J. Biol. Chem.

278

32683-32691

638427

116684

Studies on polyamine biosynthesis in Euglena gracilis

1979

Aleksijevic, A.; Grove, J.; Schuber, F.

Biochim. Biophys. Acta

565

199-207

643694

4429350

RNA-synthesizing enzymes in healthy and TMV-infected tobacco leaves. Partial purification and characterization to tobacco polynucleotide phosphorylase

1974

Brishammar, S.; Juntti, N.

Arch. Biochem. Biophys.

164

224-232

660954

12803540

Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase

2003

Chen, Y.; Vujcic, S.; Liang, P.; Diegelman, P.; Kramer, D.L.; Porter, C.W.

Biochem. J.

373

661-667

690790

1567380

Purification and characterization of polyamine oxidase from Ascaris suum

1992

Müller, S.; Walter, R.D.

Biochem. J.

1283

75-80

701662

18334225

Measurement of spermidine/spermine-N1-acetyltransferase activity by high-performance liquid chromatography with N1-dansylnorspermine as the substrate

2008

Takao, K.; Miyatake, S.; Fukazawa, K.; Wada, M.; Sugita, Y.; Shirahata, A.

Anal. Biochem.

376

277-279

712623

1955861

Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine inVibrio alginolyticus

1991

Nakao, H.; Shinoda, S.; Yamamoto, S.

J. Gen. Microbiol.

137

1737-1742

719387

3096734

Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium

1986

Cacciapuoti, G.; Porcelli, M.; Carteni-Farina, M.; Gambacorta, A.; Zappia, V.

Eur. J. Biochem.

161

263-271

720250

21458463

Crystal structures and enzymatic properties of a triamine/agmatine aminopropyltransferase from Thermus thermophilus

2011

Ohnuma, M.; Ganbe, T.; Terui, Y.; Niitsu, M.; Sato, T.; Tanaka, N.; Tamakoshi, M.; Samejima, K.; Kumasaka, T.; Oshima, T.

J. Mol. Biol.

408

971-986

721755

20381578

Biochemical characterization of pea ornithine-delta-aminotransferase: substrate specificity and inhibition by di- and polyamines

2010

Stranska, J.; Tylichova, M.; Kopecny, D.; Snegaroff, J.; Sebela, M.

Biochimie

92

940-948

727512

19822146

Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases from Hyperthermus butylicus and Pyrobaculum aerophilum

2009

Knott, J.M.

FEBS Lett.

583

3519-3524

743455

24634478

Polyamine oxidase 7 is a terminal catabolism-type enzyme in Oryza sativa and is specifically expressed in anthers

2014

Liu, T.; Kim, D.W.; Niitsu, M.; Maeda, S.; Watanabe, M.; Kamio, Y.; Berberich, T.; Kusano, T.

Plant Cell Physiol.

55

1110-1122

757687

30281855

Polyamine-independent growth and biofilm formation, and functional spermidine/spermine N-acetyltransferases in Staphylococcus aureus and Enterococcus faecalis

2019

Li, B.; Maezato, Y.; Kim, S.H.; Kurihara, S.; Liang, J.; Michael, A.J.

Mol. Microbiol.

111

159-175

Links to other databases for bis(3-aminopropyl)amine

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Show Links (1 entry)

ChEBI

PubChem