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Ligand 1-aminopentane

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Natural Substrate (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.13

Alfa-crystallin B glutamine + pentylamine = Alfa-crystallin B N5-pentylglutamine + NH3

758724

-

2.3.2.13

cornifin-A glutamine + pentylamine = cornifin-A N5-pentylglutamine + NH3

758724

-

2.3.2.13

desmoplakin glutamine + pentylamine = desmoplakin N5-pentylglutamine + NH3

758724

-

2.3.2.13

epiplakin glutamine + pentylamine = epiplakin N5-pentylglutamine + NH3

758724

-

2.3.2.13

hornein glutamine + pentylamine = hornein N5-pentylglutamine + NH3

758724

-

2.3.2.13

involucrin glutamine + pentylamine = involucrin N5-pentylglutamine + NH3

758724

-

2.3.2.13

junction plakoglobin glutamine + pentylamine = junction plakoglobin N5-pentylglutamine + NH3

758724

-

2.3.2.13

kallikrein-10 glutamine + pentylamine = kallikrein-10 N5-pentylglutamine + NH3

758724

-

2.3.2.13

plasminogen activator inhibitor 2 glutamine + pentylamine = plasminogen activator inhibitor 2 N5-pentylglutamine + NH3

758724

-

2.3.2.13

protein S100A10 glutamine + pentylamine = protein S100A10 N5-pentylglutamine + NH3

758724

-

2.3.2.13

SPR2D glutamine + pentylamine = SPR2D N5-pentylglutamine + NH3

758724

-

2.3.2.13

11 entries

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

2.6.1.113

cadaverine + pyruvate = 1-aminopentane + alanine

0

-

Substrate in Enzyme-catalyzed Reactions (28 results)

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Show Substrate (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.21

1-aminopentane + H2O + O2 = pentanal + NH3 + H2O2

684685

-

1.4.3.21

amylamine + H2O + O2 = pentanal + NH3 + H2O2

725733, 726290

-

1.4.3.21

n-pentylamine + H2O + O2 = pentanal + NH3 + H2O2

742933

-

1.4.3.22

aminopentane + H2O + O2 = pentanal + NH3 + H2O2

391951

-

1.4.3.22

pentylamine + H2O + O2 = pentanal + NH3 + H2O2

656323

-

1.4.3.4

amylamine + H2O + O2 = ?

394577

-

1.4.3.4

n-pentylamine + H2O + O2 = pentaldehyde + NH3 + H2O2

724603

-

1.4.9.1

1-aminopentane + acceptor + H2O = pentanal + NH3 + reduced acceptor

654866, 656086

-

1.4.9.1

n-pentylamine + acceptor + H2O = pentanal + NH3 + reduced acceptor

396571

-

1.4.9.2

n-amylamine + H2O + 2 blue protein = ? + NH3 + 2 blue protein

714515

-

1.4.9.2

pentylamine + H2O + 2,6-dichlorophenol indophenol = pentanal + NH3 + reduced 2,6-dichlorophenol indophenol

655062

-

2.3.2.13

Alfa-crystallin B glutamine + pentylamine = Alfa-crystallin B N5-pentylglutamine + NH3

758724

-

2.3.2.13

casein glutamine + pentylamine = casein N5-pentylglutamine + NH3

759209

-

2.3.2.13

cornifin-A glutamine + pentylamine = cornifin-A N5-pentylglutamine + NH3

758724

-

2.3.2.13

desmoplakin glutamine + pentylamine = desmoplakin N5-pentylglutamine + NH3

758724

-

2.3.2.13

epiplakin glutamine + pentylamine = epiplakin N5-pentylglutamine + NH3

758724

-

2.3.2.13

hornein glutamine + pentylamine = hornein N5-pentylglutamine + NH3

758724

-

2.3.2.13

involucrin glutamine + pentylamine = involucrin N5-pentylglutamine + NH3

758724

-

2.3.2.13

junction plakoglobin glutamine + pentylamine = junction plakoglobin N5-pentylglutamine + NH3

758724

-

2.3.2.13

kallikrein-10 glutamine + pentylamine = kallikrein-10 N5-pentylglutamine + NH3

758724

-

2.3.2.13

plasminogen activator inhibitor 2 glutamine + pentylamine = plasminogen activator inhibitor 2 N5-pentylglutamine + NH3

758724

-

2.3.2.13

protein S100A10 glutamine + pentylamine = protein S100A10 N5-pentylglutamine + NH3

758724

-

2.3.2.13

SPR2D glutamine + pentylamine = SPR2D N5-pentylglutamine + NH3

758724

-

2.3.2.13

YEQHKLPSSWPF + pentylamine = Y-N5-pentylglutaminyl-QHKLPSSWPF + NH3

758724

-

1.4.3.21

3 entries

1.4.3.22

2 entries

1.4.3.4

2 entries

1.4.9.1

2 entries

1.4.9.2

2 entries

2.3.2.13

13 entries

2.6.1.116

1-aminopentane + pyruvate = pentanal + L-alanine

753557

-

2.6.1.77

1-amylamine + pyruvate = pentanaldehyde + L-alanine

662781

-

3.4.22.8

benzoyl-Phe 4-guanidinephenyl ester + pentylamine = 4-guanidinephenol + benzoyl-Phe-pentylamide

652992

-

4.3.1.2

mesaconate + pentanamine = ?

730442, 729599

-

Product in Enzyme-catalyzed Reactions (8 results)

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Show Product (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.28

pentanal + NH3 + NADH + H+ = n-pentylamine + NAD+ + H2O

0

-

2.6.1.113

cadaverine + pyruvate = 1-aminopentane + alanine

0

-

2.6.1.77

taurine + pentanal = 2-sulfoacetaldehyde + pentylamine

0

-

3.10.1.2

N-(n-amyl)sulfamate + H2O = n-amylamine + sulfate

208293

-

3.5.1.53

N-amylurea + H2O = CO2 + NH3 + 1-n-pentanamine

209192

-

3.5.1.65

N5-n-pentyl-L-glutamine + H2O = L-glutamate + n-pentylamine

0

-

4.1.1.14

L-Norleucine = Pentylamine + CO2

0, 3968

-

4.1.1.57

L-norleucine = pentanamine + CO2

0

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.2.8

the alcohol oxidation activity of PpADH is strongly enhanced by pentylamine and the affinity for substrates is also improved by pentylamine as an activator, inhibitory at high concentrations

742110

-

1.1.5.5

best activating amine

740180

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.2.8

the alcohol oxidation activity of PpADH is strongly enhanced by pentylamine and the affinity for substrates is also improved by pentylamine as an activator, inhibitory at high concentrations

742110

-

1.4.3.10

-

395447

-

1.4.3.21

-

725733

-

2.5.1.16

-

661303

-

3.4.14.1

-

36134

-

3.4.21.50

-

36618

-

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

2.7.11.21

6ax4, 3D-view

3.4.21.4

1jir, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (15 results)

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Show Turnover Number (15 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.21

4.33

-

at pH 7.4, 37°C

726290

1.4.3.21

5.9

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

12.7

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

3 entries

1.4.3.22

142

-

-

391951

1.4.9.1

3.4

-

pH 7.5, 30°C, mutant enzyme betaI107V

656086

1.4.9.1

4.2

-

pH 7.5, 30°C, mutant enzyme betaI107N

656086

1.4.9.1

5.4

-

pH 7.5, 30°C, mutant enzyme alphaF55I

656086

1.4.9.1

17

-

pH 7.5, 30°C, wild-type enzyme

656086

1.4.9.1

20

-

pH 7.5, 30°C, mutant enzyme alphaF55A

656086

2.3.2.13

0.0065

-

pH 8.5, 4°C

759209

2.3.2.13

0.0096

-

pH 8.5, 22°C

759209

2.3.2.13

0.064

-

pH 8.5, 22°C

759209

2.6.1.116

0.18

-

pH 8.0, 30°C

753557

2.6.1.116

0.6

-

pH 8.0, 30°C

753557

2.6.1.116

1.1

-

pH 8.0, 30°C

753557

1.4.9.1

5 entries

2.3.2.13

3 entries

2.6.1.116

3 entries

K_M Value (17 results)

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Show KM Value (17 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.21

0.11

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

0.16

-

isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

1.4.3.21

5.71

-

at pH 7.4, 37°C

726290

1.4.3.21

3 entries

1.4.3.22

0.35

-

-

391951

1.4.3.4

0.5

-

at pH 7.0 and 37°C

724603

1.4.3.4

20

-

-

394577

1.4.9.1

0.004

-

pH 7.5, 30°C, mutant enzyme betaI107N

654866, 656086

1.4.9.1

0.047

-

pH 7.5, 30°C, mutant enzyme alphaF55A

654866, 656086

1.4.9.1

0.13

-

pH 7.5, 30°C, mutant enzyme betaI107V

654866, 656086

1.4.9.1

0.25

-

pH 7.5, 30°C, mutant enzyme alphaF55I

654866, 656086

1.4.9.1

2.5

-

pH 7.5, 30°C, wild-type enzyme

654866, 656086

2.3.2.13

0.00288

-

pH 8.5, 4°C

759209

2.3.2.13

0.0029

-

pH 8.5, 22°C

759209

2.3.2.13

0.0203

-

pH 8.5, 22°C

759209

2.6.1.116

5.7

-

pH 8.0, 30°C

753557

2.6.1.116

7.2

-

pH 8.0, 30°C

753557

2.6.1.116

8.5

-

pH 8.0, 30°C

753557

1.4.3.4

2 entries

1.4.9.1

5 entries

2.3.2.13

3 entries

2.6.1.116

3 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

1.1.2.8

37.6

-

pH 9.0, temperature not specified in the publication

742110

1.4.3.10

0.24

-

-

395447

1.4.3.21

3.1

-

isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

725733

References & Links

Literature References (29)

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Show Reference (29 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3968

-

Leucin-carboxylase aus marinen Rhodophyceae: Vorkommen, Verbreitung und einige Eigenschaften

1972

Hartmann, T.

Phytochemistry

11

1327-1336

36134

1238111

The mechanism of action of dipeptidyl aminopeptidase. Inhibition by amino acid derivatives and amines; activation by aromatic compounds

1975

Metrione, R.M.; MacGeorge, N.L.

Biochemistry

14

5249-5252

36618

7845202

Lysyl endopeptidase of Achromobacter lyticus

1994

Sakiyama, F.; Masaki, T.

Methods Enzymol.

244

126-137

208293

4209783

Partial purification and some properties of cyclamate sulfamatase

1974

Niimura, T.; Tokiedo, T.; Yamaha, T.

J. Biochem.

75

407-417

209192

-

Substrate utilization by grape N-carbamoylputrescine amidohydrolase: the final enzyme in putrescine biosynthesis

1997

Mendum, M.L.; Adams D.O.

Am. J. Enol. Vitic.

48

137-144

391951

7727530

Amine oxidases from Aspergillus niger: identification of a novel flavin-dependent enzyme

1995

Schilling, B.; Lerch, K.

Biochim. Biophys. Acta

1243

529-537

394577

4434991

Kinetics of the interaction between pig-plasma benzylamine oxidase and various monoamines

1974

Lindström, A.; Olsson, B.; Petterson, G.; Szymanska, J.

Eur. J. Biochem.

47

99-105

395447

1260033

Mechanism of action of putrescine oxidase. Binding characteristics of the active site of putrescine oxidase from Micrococcus rubens

1976

Swain, W.F.; Desa, R.J.

Biochim. Biophys. Acta

429

331-341

396571

-

Crystallization and properties of amine dehydrogenase from Pseudomonas sp.

1988

Shinagawa, E.; Matsushita, K.; Nakashima, K.; Adachi, O.; Ameyama, M.

Agric. Biol. Chem.

52

2255-2263

652992

10750491

Investigations on the enzyme specificity of clostripain: a new efficient biocatalyst for the synthesis of peptide isosteres

2000

Gunther, R.; Stein, A.; Bordusa, F.

J. Org. Chem.

65

1672-1679

654866

12686138

Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55

2003

Davidson, V.L.

Biochim. Biophys. Acta

1647

230-233

655062

15388968

Purification and characterization of aromatic amine dehydrogenase from Alcaligenes xylosoxidans

2004

Kondo, T.; Kondo, E.; Maki, H.; Yasumoto, K.; Takagi, K.; Kano, K.; Ikeda, T.

Biosci. Biotechnol. Biochem.

68

1921-1928

656086

11733518

Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase

2002

Wang, Y.; Sun, D.; Davidson, V.L.

J. Biol. Chem.

277

4119-4122

656323

16233600

A thermostable histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007

2004

Sekiguchi, Y.; Makita, H.; Yamamura, A.; Matsumoto, K.

J. Biosci. Bioeng.

97

104-110

661303

15340214

Mammalian spermidine synthase--identification of cysteine residues and investigation of the putrescine binding site

2004

Goda, H.; Watanabe, T.; Takeda, N.; Kobayashi, M.; Wada, M.; Hosoda, H.; Shirahata, A.; Samejima, K.

Biol. Pharm. Bull.

27

1327-1332

662781

15184574

Phototrophic utilization of taurine by the purple nonsulfur bacteria Rhodopseudomonas palustris and Rhodobacter sphaeroides

2004

Novak, R.T.; Gritzer, R.F.; Leadbetter, E.R.; Godchaux, W.

Microbiology

150

1881-1891

684685

17548046

N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: a kinetic and spectroscopic study

2007

Di Paolo, M.L.; Pesce, C.; Lunelli, M.; Scarpa, M.; Rigo, A.

Arch. Biochem. Biophys.

465

50-60

714515

27315927

Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas putida

1998

Adachi, O.; Kubota, T.; Hacisalihoglu, A.; Toyama, H.; Shinagawa, E.; Duine, J.; Matsushita, K.

Biosci. Biotechnol. Biochem.

62

469-478

724603

23924738

Purification and molecular analysis of a monoamine oxidase isolated from Narcissus tazetta

2013

Cui, Z.; Zhang, Y.; Inoue, H.; Yogo, S.; Hirasawa, E.

Biosci. Biotechnol. Biochem.

77

1728-1733

725733

-

Identification, functional expression and kinetic analysis of two primary amine oxidases from Rhodococcus opacus

2012

Foster, A.; Barnes, N.; Speight, R.; Keane, M.

J. Mol. Catal. B

74

73-82

726290

22238597

Implication for functions of the ectopic adipocyte copper amine oxidase (AOC3) from purified enzyme and cell-based kinetic studies

2012

Shen, S.H.; Wertz, D.L.; Klinman, J.P.

PLoS ONE

7

e29270

729599

-

Enantioselective Synthesis of N-Substituted Aspartic Acids Using an Engineered Variant of Methylaspartate Ammonia Lyase

2013

PuthanVeetil, V.; Raj, H.; DeVilliers, M.; Tepper, P.; Dekker, F.; Quax, W.; Poelarends, G.

ChemCatChem

5

1325-1327

730442

22614383

Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids

2012

Raj, H.; Szymanski, W.; de Villiers, J.; Rozeboom, H.J.; Veetil, V.P.; Reis, C.R.; de Villiers, M.; Dekker, F.J.; de Wildeman, S.; Quax, W.J.; Thunnissen, A.M.; Feringa, B.L.; Janssen, D.B.; Poelarends, G.J.

Nat. Chem.

4

478-484

740180

25229857

Effect of amines as activators on the alcohol-oxidizing activity of pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase

2014

Takeda, K.; Ishida, T.; Igarashi, K.; Samejima, M.; Nakamura, N.; Ohno, H.

Biosci. Biotechnol. Biochem.

78

1195-1198

742110

25229857

Effect of amines as activators on the alcohol-oxidizing activity of pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase

2014

Takeda, K.; Ishida, T.; Igarashi, K.; Samejima, M.; Nakamura, N.; Ohno, H.

Biosci. Biotechnol. Biochem.

78

1195-1198

742933

25468423

Characterization of two amine oxidases from Aspergillus carbonarius AIU 205

2015

Sugawara, A.; Matsui, D.; Yamada, M.; Asano, Y.; Isobe, K.

J. Biosci. Bioeng.

119

629-635

753557

31162815

Biochemical properties of a Pseudomonas aminotransferase involved in caprolactam metabolism

2019

Palacio, C.M.; Rozeboom, H.J.; Lanfranchi, E.; Meng, Q.; Otzen, M.; Janssen, D.B.

FEBS J.

286

4086-4102

758724

27416753

Analysis on transglutaminase 1 and its substrates using specific substrate peptide in cultured keratinocytes

2016

Yamane, M.; Sugimura, K.; Kawasaki, H.; Tatsukawa, H.; Hitomi, K.

Biochem. Biophys. Res. Commun.

478

343-348

759209

29960064

Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus

2018

Sirikharin, R.; Soederhaell, I.; Soederhaell, K.

Fish Shellfish Immunol.

80

546-549

Links to other databases for 1-aminopentane

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Show Links (1 entry)

ChEBI

PubChem