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Ligand N-acetylputrescine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.5.1.62

acetylputrescine + H2O = acetate + putrescine

752759

7kur, 3D-view

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

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.57

acetyl-CoA + putrescine = CoA + acetylputrescine

487256

-

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.10

N-acetylputrescine + O2 + H2O = N4-acetylaminobutanal + NH3 + H2O2

395442

-

1.4.3.22

N-acetyl-1,4-diaminobutane + H2O + O2 = N-acetyl-aminobutanal + acetylamine + H2O2

391947

-

2.3.1.57

acetyl-CoA + N-acetylputrescine = CoA + N1,N4-diacetylputrescine

487256

-

3.5.1.4

acetylputrescine + H2O = acetate + putrescine

655874

-

3.5.1.48

acetylputrescine + H2O = acetate + putrescine

733494, 754843

7kur, 3D-view

3.5.1.53

N-acetylputrescin + H2O = putrescine + acetate

692846

-

3.5.1.62

acetylputrescine + H2O = acetate + putrescine

753079, 752759

7kur, 3D-view

3.5.1.62

N-acetylputrescine + H2O = acetate + putrescine

172070

7kur, 3D-view

3.5.1.62

2 entries

Product in Enzyme-catalyzed Reactions (3 results)

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Show Product (3 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.57

acetyl-CoA + putrescine = CoA + acetylputrescine

487256

-

2.3.1.57

acetyl-CoA + putrescine = CoA + N-acetylputrescine

487261, 487259, 487256, 487260

-

2.3.1.57

acetyl-CoA + putrescine = CoA + N1-acetylputrescine

0

-

2.3.1.57

3 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.57

slight, competitive inhibition

487259

-

3.5.1.48

Ki: 0.8 mM

172051

7kur, 3D-view

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

3.5.1.48

7kur, 3D-view

3.5.1.62

7kur, 3D-view

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

3.5.1.48

0.034

-

pH 8.0, 22°C, recombinant mutant E274L

754843

3.5.1.48

0.126

-

pH 8.0, 22°C, recombinant mutant N93A

754843

3.5.1.48

0.24

-

pH 8.0, 22°C, recombinant mutant D94A

754843

3.5.1.48

0.35

-

pH 8.0, 22°C, recombinant enzyme

754843

3.5.1.48

0.7

-

pH 8.0, 22°C, recombinant wild-type enzyme

754843

3.5.1.48

5 entries

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

1.4.3.22

9.71

-

-

391947

2.3.1.57

2.4

-

-

487256

3.5.1.48

0.11

-

pH 8.0, 22°C, recombinant mutant D94A

754843

3.5.1.48

0.13

-

pH 8.0, 22°C, recombinant mutant N93A

754843

3.5.1.48

0.16

-

pH 8.0, 22°C, recombinant mutant E274L

754843

3.5.1.48

0.16

-

pH 8.0, 22°C, recombinant wild-type enzyme

754843

3.5.1.48

0.17

-

pH 8.0, 22°C, recombinant enzyme

754843

3.5.1.62

0.321

-

-

172070

3.5.1.62

0.411

-

pH 8.0, 30°C

753079

3.5.1.62

0.503

-

pH 8.0, 30°C

753079

3.5.1.48

5 entries

3.5.1.62

3 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

2.3.1.57

1.7

-

-

487259

3.5.1.48

0.8

-

-

172051

References & Links

Literature References (14)

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Show Reference (14 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

172051

-

Inhibitor studies on the characteristics of the active site of rat liver N8-acetylspermidine deacetylase

1985

Manneh, V.A.; Blankenship, J.

Proc. West. Pharmacol. Soc.

28

255-258

172070

-

Acetylputrescine deacetylase from Micrococcus luteus K-11

1986

Suzuki, O.; Ishikawa, Y.; Miyazaki, K.; Izu, K.; Matsumoto, T.

Biochim. Biophys. Acta

882

140-142

391947

-

Purification and properties of diamine oxidase from human kidney

1987

Suzuki, O.; Matsumoto, T.

Biogenic Amines

4

237-245

395442

7092834

Polyamine degradation in foetal and adult bovine serum

1982

Gahl, W.A.; Pitot, H.C.

Biochem. J.

202

603-611

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

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

487260

2320051

Putrescine N-acetyltransferase in Onchocerca volvulus and Ascaris suum, an enzyme which is involved in polyamine degradation and release of N-acetylputrescine

1990

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

Mol. Biochem. Parasitol.

38

13-18

487261

4841346

Acetyl-CoA:1,4-diaminobutane N-acetyltransferase. Occurence in vertebrate organs and subcellular localization

1974

Seiler, N.; Al-Therib, J.

Biochim. Biophys. Acta

354

206-212

655874

15060035

A new amidohydrolase from Bordetella or Alcaligenes strain FB188 with similarities to histone deacetylases

2004

Hildmann, C.; Ninkovic, M.; Dietrich, R.; Wegener, D.; Riester, D.; Zimmermann, T.; Birch, O.M.; Bernegger, C.; Loidl, P.; Schwienhorst, A.

J. Bacteriol.

186

2328-2339

692846

18192388

Transcriptome analysis of agmatine and putrescine catabolism in Pseudomonas aeruginosa PAO1

2008

Chou, H.T.; Kwon, D.H.; Hegazy, M.; Lu, C.D.

J. Bacteriol.

190

1966-1975

733494

23790721

Synthesis and evaluation of N8-acetylspermidine analogues as inhibitors of bacterial acetylpolyamine amidohydrolase

2013

Decroos, C.; Bowman, C.M.; Christianson, D.W.

Bioorg. Med. Chem.

21

4530-4540

752759

26200446

Design, synthesis, and evaluation of polyamine deacetylase inhibitors, and high-resolution crystal structures of their complexes with acetylpolyamine amidohydrolase

2015

Decroos, C.; Christianson, D.W.

Biochemistry

54

4692-4703

753079

26956223

Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

2016

Krämer, A.; Herzer, J.; Overhage, J.; Meyer-Almes, F.

BMC Biochem.

17

4

754843

28516954

Histone deacetylase 10 structure and molecular function as a polyamine deacetylase

2017

Hai, Y.; Shinsky, S.A.; Porter, N.J.; Christianson, D.W.

Nat. Commun.

8

15368

Links to other databases for N-acetylputrescine

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Show Links (1 entry)

ChEBI

PubChem