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Ligand aminopropylcadaverine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

LITERATURE

REACTION DIAGRAM

PROVEN IN VIVO REACTION

ENZYME 3D STRUCTURE

2.5.1.104

-

S-adenosyl 3-(methylthio)propylamine + cadaverine = 5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine

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Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Substrate (3 entries)

EC NUMBER

LITERATURE

REACTION DIAGRAM

REACTION

ENZYME 3D STRUCTURE

2.3.1.57

674508

acetyl-CoA + aminopropylcadaverine = ?

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2.5.1.22

489861

S-adenosylmethioninamine + N-(3-aminopropyl)cadaverine = 5'-methylthioadenosine + ?

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2.5.1.46

638083

aminopropylcadaverine + [eIF5A-precursor]-lysine = [eIF5A-precursor]-homodeoxyhypusine + ?

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Product in Enzyme-catalyzed Reactions (2 results)

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Show Product (2 entries)

EC NUMBER

LITERATURE

REACTION DIAGRAM

REACTION

ENZYME 3D STRUCTURE

2.5.1.104

-

S-adenosyl 3-(methylthio)propylamine + cadaverine = 5'-S-methyl-5'-thioadenosine + N-(3-aminopropyl)cadaverine

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2.5.1.16

639706, , 639709

S-adenosyl-3-methylthio-1-propylamine + 1,5-diaminopentane = 5'-methylthioadenosine + N-(3-aminopropyl)-1,5-diaminopentane

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Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

COMMENTARY

EC NUMBER

LITERATURE

ENZYME 3D STRUCTURE

weak

2.5.1.22

489867

-

-

2.5.1.46

638076

-

inhibition of deoxyhypusine synthesis

2.5.1.46

638083

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (1 result)

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Show Turnover Number (1 entry)

COMMENTARY

EC NUMBER

LITERATURE

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

pH 9

2.3.1.57

674508

0.1

-

K_M Value (1 result)

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Show KM Value (1 entry)

COMMENTARY

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

LITERATURE

pH 9

2.3.1.57

0.41

-

674508

References & Links

Literature References (7)

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Show Reference (7 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

639706

4572733

Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli

1973

Bowman, W.H.; White Tabor, C.; Tabor, H.

J. Biol. Chem.

248

2480-2486

639709

7103507

Purification of spermidine synthase from rat ventral prostate by affinity chromatography on immobilized S-adenosyl(5)-3-thiopropylamine

1982

Samejima, K.; Yamanoha, B.

Arch. Biochem. Biophys.

216

213-222

674508

16210326

Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase

2005

Forouhar, F.; Lee, I.S.; Vujcic, J.; Vujcic, S.; Shen, J.; Vorobiev, S.M.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Porter, C.W.; Tong, L.

J. Biol. Chem.

280

40328-40336

Links to other databases for aminopropylcadaverine

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Show Links (1 entry)

ChEBI

PubChem

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