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Ligand pentanal

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

1.1.1.71

1-pentanol + NAD(P)+ = pentanal + NAD(P)H + H+

-

-

1.1.3.13

n-pentanol + O2 = n-pentanal + H2O2

-

-

1.14.14.34

pentanesulfonate + FMNH2 + O2 = pentanal + FMN + sulfite + H2O

-

-

Substrate in Enzyme-catalyzed Reactions (94 results)

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Show Substrate (94 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

n-pentylaldehyde + NADH + H+ = n-pentanol + NAD+

285623

-

1.1.1.1

n-valeraldehyde + NADH + H+ = n-pentanol + NAD+

687850

-

1.1.1.1

pentanal + NAD+ = pentanone + NADH

285569, 285571, 285573, 285575, 285608, 285651, 285647, 285580, 285639, 285579, 285603

-

1.1.1.1

pentanal + NADH + H+ = 1-pentanol + NAD+

742472

-

1.1.1.1

pentanal + NADH = 1-pentanol + NAD+ + H+

667255

-

1.1.1.1

valeraldehyde + NADH = 1-pentanol + NAD+

722888

-

1.1.1.184

1-pentanal + NADPH = 1-pentanol + NADP+

347755

-

1.1.1.184

pentanal + NADPH + H+ = pentan-1-ol + NADP+

760819

-

1.1.1.184

valeraldehyde + NADPH + H+ = pentan-1-ol + NADP+

736122

-

1.1.1.2

pentanal + NADPH + H+ = pentan-1-ol + NADP+

737536

-

1.1.1.2

pentanal + NADPH + H+ = pentanol + NADP+

698623

-

1.1.1.2

pentanal + NADPH = 1-pentanol + NADP+

654493

-

1.1.1.2

pentanal + NADPH = pentanol + NADP+

286203, 286210, 286206

-

1.1.1.2

valeraldehyde + NADPH + H+ = ? + NADP+

698097

-

1.1.1.1

6 entries

1.1.1.184

3 entries

1.1.1.2

5 entries

1.1.1.202

valeraldehyde + NADH + H+ = pentan-1-ol + NAD+

740216

-

1.1.1.21

n-pentanal + NAD(P)H + H+ = n-pentanol + NAD(P)+

286248, 286238

-

1.1.1.265

pentanal + NADPH = pentanol + NADP+

246375, 286203

-

1.1.1.283

pentanal + NADPH + H+ = pentan-1-ol + NADP+

736122

-

1.1.1.283

valeraldehyde + NADPH + H+ = amyl alcohol + NADP+

736122

-

1.1.1.283

2 entries

1.1.1.307

valeraldehyde + NADPH + H+ = ?

286260

-

1.1.1.430

pentanal + NADH + H+ = ?

764945

-

1.1.1.431

pentanal + NADPH + H+ = ?

764945

-

1.1.1.71

pentanal + NADPH + H+ = 1-pentanol + NAD(P)+

737536

-

1.1.1.72

n-pentanal + NADPH + H+ = n-pentanol + NADP+

287287, 287283

-

1.1.1.91

pentanal + NADPH = pentanol + NADP+

724669

-

1.1.1.B3

n-valeraldehyde + NADH + H+ = ? + NAD+

685643

-

1.1.1.B3

valeraldehyde + NADH + H+ = n-pentanol + NAD+

684588

-

1.1.1.B3

2 entries

1.1.99.20

pentanal + acceptor + H2O = pentanoic acid + reduced acceptor

389904

-

1.2.1.10

pentaldehyde + CoA + NAD+ = pentyl-CoA + NADH + H+

724341

-

1.2.1.10

valeraldehyde + CoA + NAD+ = valeryl-CoA + NADH

286052, 390166

-

1.2.1.10

valerylaldehyde + CoA + NAD+ = valeryl-CoA + NADH + H+

742936

-

1.2.1.10

3 entries

1.2.1.12

valeraldehyde + phosphate + NAD+ = pentanoyl phosphate + NADH

287913

-

1.2.1.16

pentanal + NAD+ + H2O = pentanoate + NADH + 2 H+

685387

-

1.2.1.16

pentanal + NAD+ + H2O = pentanoate + NADH + H+

685387

-

1.2.1.16

2 entries

1.2.1.19

valeraldehyde + NAD+ + H2O = valerate + NADH + H+

288081, 288069

-

1.2.1.20

valeraldehyde + NAD+ + H2O = valeric acid + NADH + H+

288125

-

1.2.1.24

n-pentanal + NAD+ + H2O = n-pentanoate + NADH + H+

692615, 700082

-

1.2.1.24

pentanal + NAD(P)+ + H2O = pentanoate + NAD(P)H + H+

692620

-

1.2.1.24

pentanaldehyde + NAD+ + H2O = pentanoate + NADH

674654

-

1.2.1.26

valeraldehyde + NAD(P)+ + H2O = n-pentanoate + NAD(P)H + H+

693021

-

1.2.1.26

valeraldehyde + NAD+ = valerate + NADH + H+

763713

-

1.2.1.3

pentanal + NAD+ + H2O = pentanoate + NADH

348694, 348682, 348707, 348706

-

1.2.1.3

pentanaldehyde + NAD+ + H2O = pentanoate + NADH + H+

741416

-

1.2.1.3

valeraldehyde + NAD+ + H2O = valerate + NADH + H+

690591, 711536

-

1.2.1.4

pentanal + NADP+ = pentanoate + NADPH

348681, 348725, 437830, 437834

-

1.2.1.4

valeraldehyde + NADP+ + H2O = pentanoate + NADPH + H+

712174

-

1.2.1.47

pentanal + NAD+ = pentanoate + NADH

288255

-

1.2.1.47

valeraldehyde + NAD+ + H2O = valerate + NADH + H+

762831

-

1.2.1.5

n-pentanal + NAD+ + H2O = n-pentanoate + NADH + H+

348786, 348793, 348794, 348792, 348796, 348798

-

1.2.1.5

n-pentanal + NADP+ + H2O = n-pentanoate + NADPH + H+

671511

-

1.2.1.5

valeraldehyde + NAD(P)+ + H2O = valerate + NAD(P)H + H+

654425, 656571

-

1.2.1.5

valeraldehyde + NAD+ = valerate + NADH + H+

725948

-

1.2.1.5

valeraldehyde + NADP+ + H2O = valerate + NADPH + H+

688414

-

1.2.1.5

valeraldehyde + NADP+ = valerate + NADPH + H+

725948

-

1.2.1.24

3 entries

1.2.1.26

2 entries

1.2.1.3

3 entries

1.2.1.4

2 entries

1.2.1.47

2 entries

1.2.1.5

6 entries

1.2.1.76

valeraldehyde + coenzyme A + NADP+ = n-valeryl-CoA + NADPH + H+

697694

-

1.2.1.77

valeraldehyde + NADP+ + H2O = valerate + NADPH + H+

688414

-

1.2.1.79

n-pentanal + NADP+ + H2O = n-pentanoate + NADPH + H+

690736

-

1.2.1.8

valeraldehyde + NAD+ + H2O = valerate + NADH + H+

656550

-

1.2.1.8

valeraldehyde + NADP+ + H2O = valerate + NADPH + H+

656550

-

1.2.1.8

2 entries

1.2.1.87

pentaldehyde + CoA + NAD+ = pentanoyl-CoA + NADH + H+

721615

-

1.2.1.99

valeraldehyde + NAD+ + H2O = pentanoate + NADH + H+

690591, 711536

-

1.2.3.1

n-pentanal + H2O + O2 = n-pentanoic acid + H2O2

677264

-

1.2.3.1

n-valeraldehyde + O2 + H2O = valerate + H2O2

644705

-

1.2.3.1

pentanal + H2O + O2 = pentanoic acid + H2O2

763618, 763546

-

1.2.3.1

valeraldehyde + H2O + O2 = valerate + H2O2

654321, 656311

-

1.2.3.1

valeraldehyde + H2O + O2 = valeric acid + H2O2

390405, 699045

-

1.2.5.2

pentanal + 2 ferricyanide + H2O = pentanoate + 2 ferrocyanide + 2 H+

389961, 684539

-

1.2.5.2

pentanal + a quinone + H2O = pentanoate + a quinol

288472

-

1.2.5.2

valeraldehyde + ferricyanide = pentanoic acid + ferrocyanide + H+

731204

-

1.2.3.1

5 entries

1.2.5.2

3 entries

1.2.99.6

Pentanal + benzyl viologen = Pentanoate + reduced benzyl viologen

11936

-

1.2.99.7

pentanal + H2O + benzylviologen = pentanoate + reduced benzylviologen

11936

-

1.4.1.28

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

763489

-

2.2.1.1

3-hydroxypyruvate + n-pentanal = 1,3-dihydroxy-2-heptanone + CO2

756467

-

2.2.1.1

pentanal + 2-oxohexanoic acid = 6-hydroxydecan-5-one + CO2

756713

-

2.2.1.1

pentanal + pyruvate = 2-hydroxyhexanal + CO2

756713

-

2.2.1.1

3 entries

2.6.1.77

taurine + pentanal = 2-sulfoacetaldehyde + pentylamine

737516

-

4.1.1.43

phenylpyruvate + pentanal = 3-hydroxy-1-phenyl-2-heptanone

653954

-

4.1.1.7

n-pentanal = (R)-6-hydroxydecan-5-one

679656

-

4.1.2.10

HCN + pentanal = (R)-2-hydroxy-hexanenitrile

663423

-

4.1.2.13

2 pentanaldehyde = 5,6,7,8-tetradeoxy-D-threo-2-octulose

727267

-

4.1.2.38

2 valeraldehyde = (R)-6-hydroxy-5-decanone

748404

-

4.1.2.38

n-pentanal = (R)-6-hydroxydecan-5-one

679656

-

4.1.2.38

2 entries

4.1.2.43

D-ribulose 5-phosphate + valeraldehyde = ?

690565

-

4.1.2.47

cyanide + pentanal = (2S)-2-hydroxyhexanenitrile

5153

-

4.1.2.47

HCN + pentanal = 2-hydroxyhexanenitrile

650926

-

4.1.2.49

glycine + valeraldehyde = (2S,3R/3S)-2-amino-3-hydroxyheptanoic acid

770834

-

4.1.2.49

glycine + valeraldehyde = (2S,3R/S)-2-amino-3-hydroxyheptanoic acid

770834

-

4.1.2.47

2 entries

4.1.2.49

2 entries

4.1.2.52

pyruvate + pentaldehyde = ?

702377

-

4.1.2.63

pentanal + formyl-CoA = 2-hydroxyhexanoyl-CoA

774545

-

4.1.3.39

pentaldehyde + pyruvate = 4-hydroxy-2-oxooctanoate

714244

-

4.1.3.39

pyruvate + pentaldehyde = ?

702377

-

4.1.3.39

2 entries

4.1.3.43

pyruvate + pentaldehyde = ?

702377, 714244, 722458

-

4.1.99.5

pentanal + O2 + 2 NADH + 2 H+ = butane + formate + H2O + 2 NAD+

727312

-

5.3.2.6

pentanal + [(Z)-2-nitroethenyl]benzene = (2R)-2-[(1S)-2-nitro-1-phenylethyl]pentanal

727314

-

Product in Enzyme-catalyzed Reactions (82 results)

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Show Product (82 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

1-pentanol + NAD+ = 1-pentanal + NADH + H+

-

-

1.1.1.1

pentanol + NAD+ = n-pentanal + NADH

-

-

1.1.1.1

1-pentanol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.1

n-pentanol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.1

pentan-1-ol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.1

pentanol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.1

pentanol + NAD+ = valeraldehyde + NADH + H+

-

-

1.1.1.1

7 entries

1.1.1.192

n-pentanol + NAD+ + H2O = n-pentanal + NADH

-

-

1.1.1.2

1-pentanol + NADP+ = n-pentanal + NADPH

-

-

1.1.1.2

1-pentanol + NADP+ = n-pentanal + NADPH + H+

-

-

1.1.1.2

1-pentanol + NADP+ = pentanal + NADPH

-

-

1.1.1.2

1-pentanol + NADP+ = pentanal + NADPH + H+

-

-

1.1.1.2

pentan-1-ol + NADP+ = pentanal + NADPH + H+

-

-

1.1.1.2

pentanol + NADP+ = pentanal + NADPH

-

-

1.1.1.2

pentanol + NADP+ = pentanal + NADPH + H+

-

-

1.1.1.2

7 entries

1.1.1.245

1-pentanol + NAD+ = n-pentanal + NADH

-

-

1.1.1.306

1-pentanol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.71

pentan-1-ol + NADP+ = pentaldehyde + NADPH + H+

-

-

1.1.1.71

1-pentanol + NAD(P)+ = pentanal + NAD(P)H + H+

-

-

1.1.1.71

1-pentanol + NAD+ = pentanal + NADH + H+

-

-

1.1.1.71

1-pentanol + NADP+ = pentanal + NADPH + H+

-

-

1.1.1.71

pentan-1-ol + NADP+ = pentanal + NADPH

287280, 287277, -

-

1.1.1.71

5 entries

1.1.1.73

n-pentanol + NAD+ = n-pentanal + NADH

-

-

1.1.1.91

n-pentanol + NADP+ = n-pentanal + NADPH

-

-

1.1.1.B3

pentan-1-ol + NADP+ = pentanal + NADPH + H+

-

-

1.1.2.7

pentanol + 2,6-dichlorophenolindophenol = pentaldehyde + reduced 2,6-dichlorophenolindophenol

-

-

1.1.2.7

pentanol + 2 oxidized cytochrome cL = pentanal + 2 reduced cytochrome cL

-

-

1.1.2.7

2 entries

1.1.2.9

1-pentanol + ferricytochrome c = pentanal + ferrocytochrome c + H+

-

-

1.1.3.13

1-pentanol + O2 = n-pentanal + H2O2

-

-

1.1.3.13

n-pentanol + O2 = n-pentanal + H2O2

-

-

1.1.3.13

1-pentanol + O2 = pentanal + H2O2

-

-

1.1.3.13

pentan-1-ol + O2 = pentanal + H2O2

-

-

1.1.3.13

1-pentanol + O2 = pentanaldehyde + H2O2

-

-

1.1.3.13

5 entries

1.1.3.18

1-pentanol + O2 = n-pentanal + H2O2

-

-

1.1.5.11

1-pentanol + a quinone = pentanal + a quinol

-

-

1.1.5.5

n-pentanol + ferricyanide = n-pentanal + ferrocyanide

-

-

1.1.5.5

1-pentanol + ubiquinone = pentanal + ubiquinol

-

-

1.1.5.5

1-pentanol + 2,6-dichlorophenolindophenol = pentanaldehyde + reduced 2,6-dichlorophenolindophenol

-

-

1.1.9.1

1-pentanol + ferricyanide = pentanal + ferrocyanide

-

-

1.1.9.1

1-pentanol + ferrocyanide = pentanal + ferricyanide

-

-

1.1.9.1

1-pentanol + N,N,N',N'-tetramethyl-p-phenylenediamine = pentanal + ?

-

-

1.1.5.5

3 entries

1.1.9.1

3 entries

1.1.99.12

1-pentanol + acceptor = n-pentanal + reduced acceptor

287728

-

1.13.12.16

pentane-1-nitronate + Cu(0) + N,N,N',N'-tetramethylethylenediamine + O2 = pentaldehyde + (NO2)CuN,N,N',N'-tetramethylethylenediamine

-

-

1.13.12.16

pentyl-1-nitronate + O2 = NO2- + pentanal

-

-

1.13.12.16

1-nitropentane + O2 = pentanaldehyde + HNO2

-

-

1.13.12.16

1-nitropentane + O2 = pentanaldehyde + nitrite

-

-

1.13.12.16

4 entries

1.14.11.17

pentanesulfonic acid + 2-oxoglutarate + O2 = sulfite + pentanal + succinate + CO2

-

-

1.14.11.77

pentyl sulfate + 2-oxoglutarate + O2 = pentanal + succinate + CO2 + sulfate

-

-

1.14.14.34

pentanesulfonate + FMNH2 + O2 = pentanal + FMN + sulfite + H2O

-

-

1.14.14.5

pentanesulfonate + FMNH2 + O2 = pentaldehyde + FMN + sulfite + H2O

-

-

1.14.14.5

pentanesulfonic acid + FMNH2 + O2 = pentaldehyde + FMN + sulfite + H2O

438770, -

-

1.14.14.5

2 entries

1.14.18.3

pentane + duroquinol + O2 = 2-pentanol + pentanal + duroquinone + H2O

-

-

1.2.98.1

1-pentanol + p-nitroso-N,N-dimethylaniline = n-pentanal + reduced p-nitroso-N,N-dimethylaniline

390495, 390488

-

1.3.1.48

trans-2-pentenal + NADPH = pentanal + NADP+

390830

-

1.3.1.74

(2E)-pentenal + NAD(P)H = n-pentanal + NAD(P)+

-

-

1.3.1.74

trans-2-pentenal + NADPH = pentanal + NADP+

-

-

1.4.3.21

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

-

-

1.4.3.21

amylamine + H2O + O2 = pentanal + NH3 + H2O2

-

-

1.4.3.21

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

-

-

1.4.3.22

aminopentane + H2O + O2 = pentanal + NH3 + H2O2

391951

-

1.4.3.22

pentylamine + H2O + O2 = pentanal + NH3 + H2O2

-

-

1.3.1.74

2 entries

1.4.3.21

3 entries

1.4.3.22

2 entries

1.4.3.4

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

-

-

1.4.9.1

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

-

-

1.4.9.1

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

-

-

1.4.9.1

2 entries

1.4.9.2

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

-

-

1.6.5.5

2-pentenal + NADPH = pentanal + NADP+

-

-

1.7.3.1

1-nitropentane + O2 = pentanaldehyde + HNO2

-

-

2.6.1.116

1-aminopentane + pyruvate = pentanal + L-alanine

-

-

2.6.1.77

1-amylamine + pyruvate = pentanaldehyde + L-alanine

-

-

4.1.1.1

2-oxohexanoic acid = n-pentanal + CO2

-

-

4.1.1.1

2-ketohexanoic acid = pentanal + CO2

-

-

4.1.1.1

2-oxohexanoic acid = pentanal + CO2

-

-

4.1.1.1

2-oxomethylvalerate = pentanal + CO2

-

-

4.1.1.43

2-ketohexanoic acid = pentanal + CO2

-

-

4.1.1.43

2-Oxohexanoate = Pentanal + CO2

-

-

4.1.1.7

2-ketohexanoate = valeraldehyde + CO2

-

-

4.1.1.7

2-oxohexanoate = valeraldehyde + CO2

-

-

4.1.1.7

2-oxohexanoic acid = valeraldehyde + CO2

-

-

4.1.1.72

4-methyl-2-oxopentanoate = 4-methylbutanal + CO2

-

-

4.1.1.72

2-oxohexanoate = n-pentanal + CO2

-

-

4.1.1.72

2-oxohexanoic acid = pentanal + CO2

-

-

4.1.1.72

2-oxomethylvalerate = pentanal + CO2

-

-

4.1.1.1

4 entries

4.1.1.43

2 entries

4.1.1.7

3 entries

4.1.1.72

4 entries

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.265

presence of NADPH, Ki: 3.9 mM, presence of NADH, Ki: 13.9 mM

286203

-

1.13.12.16

competitive inhibitor with respect to ethylnitronate as substrate

696605

-

1.2.1.20

-

288126

-

1.2.1.24

-

288166

-

1.2.1.3

substrate inhibition

348707

-

1.2.1.3

-

741416

-

1.2.1.3

2 entries

1.2.1.46

substrate n-butanol

288247

-

1.2.1.5

extremely strong substrate inhibition

348798

-

1.2.5.2

substrate inhibition

389961

-

3.4.22.B69

-

773052

-

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

2.7.1.37

1REK, 3D-view

3.2.1.17

1YKZ, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (41 results)

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Show Turnover Number (41 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

418

-

pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae

722888

1.1.1.1

432

-

pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans

722888

1.1.1.1

528

-

pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha

722888

1.1.1.2

49.2

-

pH 7.0, temperature not specified in the publication

737536

1.1.1.2

159

-

-

698623

1.1.1.2

159.1

-

in 30 mM Tris-HCl (pH 8.0)

698623

1.1.1.2

378

-

pH 7.0, 25°C

654493

1.1.1.2

11920

-

pH 7.0, 25°C

654493

1.1.1.1

3 entries

1.1.1.2

5 entries

1.1.1.202

1

-

pH 7.0, 37°C

740216

1.1.1.265

56.6

-

presence of NADPH

286203

1.1.1.265

81.6

-

presence of NADH

286203

1.1.1.265

2 entries

1.1.1.430

5.9

-

pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH

764945

1.1.1.431

20.7

-

pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH

764945

1.1.1.71

6.96

-

substrates NADH and pentanal, pH 5.5, 30°C

761529

1.2.1.10

13

-

mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)

724341

1.2.1.26

2.1

-

-

693021

1.2.1.3

5.44

-

at pH 8.0 and 21°C

741416

1.2.1.3

8.17

-

enzyme form ALDH-1, pH 9.5

348694

1.2.1.3

22.8

-

enzyme form ALDH-2, pH 9.5

348694

1.2.1.3

26.24

-

with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C

690591

1.2.1.5

19.41

-

with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C

725948

1.2.1.5

30.99

-

with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C

725948

1.2.1.3

4 entries

1.2.1.5

2 entries

1.2.1.77

5.16

-

in 50 mM Tris-HCl (pH 7.5), at 25°C

688414

1.2.1.99

26.24

-

pH 8.0, 37°C, cofactor: NAD+

690591

1.2.1.99

29.61

-

pH 8.0, 45°C

711536

1.2.3.1

0.45

-

mutant V1016I, pH 8.0, 37°C

763618

1.2.3.1

0.64

-

pH 8, 37°C

763618

1.2.3.1

0.92

-

mutant M1088V, pH 8.0, 37°C

763618

1.2.3.1

1.11

-

mutant V1016F, pH 8.0, 37°C

763618

1.2.3.1

1.28

-

mutant I1018K, pH 8.0, 37°C

763618

1.2.3.1

1.53

-

pH 8, 37°C

763618

1.2.3.1

2.65

-

mutant I1018S, pH 8.0, 37°C

763618

1.2.3.1

2.79

-

wild-type, pH 8.0, 37°C

763618

1.2.3.1

4.34

-

pH 8, 37°C

763618

1.2.3.1

7.98

-

mutant M1088T, pH 8.0, 37°C

763618

1.2.1.99

2 entries

1.2.3.1

10 entries

4.1.2.63

2

-

pH 7.4, 37°C, wild-type enzyme

774545

4.1.3.39

0.13

-

L87A/L89A mutant protein, pH 8.0, 25°C

714244

4.1.3.39

0.58

-

L89A mutant protein, pH 8.0, 25°C

714244

4.1.3.43

0.13

-

L87A/L89A variant of BphI, app. kcat-value, pH 8.0, 25°C

714244

4.1.3.43

0.14

-

Y290F variant of BphI, app. kcat-value, steady-state kinetic parameter, pH 8.0, 25°C

722458

4.1.3.43

0.58

-

L89A variant of BphI, app. kcat-value, pH 8.0, 25°C

714244

4.1.3.39

2 entries

4.1.3.43

3 entries

K_M Value (69 results)

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Show KM Value (69 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.1

0.17

-

pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae

722888

1.1.1.1

0.28

-

pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans

722888

1.1.1.1

2

-

pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha

722888

1.1.1.1

10.3

-

33°C, pH 8

684612

1.1.1.2

0.049

-

pH 7.0, 25°C

654493

1.1.1.2

0.06

-

pH 7.0, 25°C

654493

1.1.1.2

0.07

-

-

286206

1.1.1.2

0.075

-

-

698623

1.1.1.2

0.075

-

in 30 mM Tris-HCl (pH 8.0)

698623

1.1.1.2

0.16

-

coenzyme NADPH

286203

1.1.1.2

0.4

-

pH 7.0, temperature not specified in the publication

737536

1.1.1.2

3.01

-

coenzyme NADH

286203

1.1.1.1

4 entries

1.1.1.2

8 entries

1.1.1.202

2.16

-

pH 7.0, 37°C

740216

1.1.1.21

0.087

-

-

286238

1.1.1.265

0.16

-

presence of NADPH

286203

1.1.1.265

3.01

-

presence of NADH

286203

1.1.1.265

2 entries

1.1.1.430

14.7

-

pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH

764945

1.1.1.431

3.9

-

pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH

764945

1.1.1.71

0.09

-

substrates NADH and pentanal, pH 5.5, 30°C

761529

1.2.1.10

1.5

-

-

390166

1.2.1.10

8.2

-

mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)

724341

1.2.1.19

0.004

-

constant substrate 1 mM NAD+

288081

1.2.1.19

0.013

-

-

288069

1.2.1.24

0.025

-

-

692620

1.2.1.24

0.0287

-

in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C

700082

1.2.1.24

0.057

-

-

692615

1.2.1.24

0.0827

-

-

692620

1.2.1.24

0.096

-

in 100 mM Na2HPO4/NaH2PO4 buffer, 1 mM dithiothreitol, at pH 8.5 and 22°C

700082

1.2.1.10

2 entries

1.2.1.19

2 entries

1.2.1.24

5 entries

1.2.1.26

0.145

-

-

693021

1.2.1.3

0.000034

-

enzyme form ALDH-2, pH 9.5

348694

1.2.1.3

0.00016

-

enzyme form ALDH-1, pH 9.5

348694

1.2.1.3

0.0007

-

-

348682

1.2.1.3

0.006

-

-

348707

1.2.1.3

0.14

-

recombinant enzyme, in 50 mM potassium phosphate buffer, at pH 8.0 and 45°C

711536

1.2.1.3

0.24

-

with NAD+ as cofactor, in 50 mM potassium phosphate buffer (pH 8.0), at 37°C

690591

1.2.1.3

2.2

-

at pH 8.0 and 21°C

741416

1.2.1.4

0.435

-

-

348681, 348725

1.2.1.4

0.92

-

-

437830

1.2.1.47

0.01

-

-

288255

1.2.1.47

0.035

-

pH 7.5, temperature not specified in the publication

762831

1.2.1.5

0.0001

-

isoenzyme F1

348792, 348796

1.2.1.5

0.12

-

with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C

725948

1.2.1.5

0.3

-

-

688414

1.2.1.5

0.34

-

with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C

725948

1.2.1.3

7 entries

1.2.1.4

2 entries

1.2.1.47

2 entries

1.2.1.5

4 entries

1.2.1.77

0.3

-

in 50 mM Tris-HCl (pH 7.5), at 25°C

688414

1.2.1.8

0.2

-

pH 7.7, coenzyme NAD+

656550

1.2.1.8

4.1

-

pH 7.7, coenzyme NADP+

656550

1.2.1.99

0.14

-

pH 8.0, 45°C

711536

1.2.1.99

0.24

-

pH 8.0, 37°C, cofactor: NAD+

690591

1.2.3.1

0.0011

-

30°C, pH 7.0

699045

1.2.3.1

0.0134

-

mutant I1018K, pH 8.0, 37°C

763618

1.2.3.1

0.0134

-

mutant I1018S, pH 8.0, 37°C

763618

1.2.3.1

0.0157

-

pH 8, 37°C

763618

1.2.3.1

0.0284

-

mutant M1088V, pH 8.0, 37°C

763618

1.2.3.1

0.0293

-

mutant V1016I, pH 8.0, 37°C

763618

1.2.3.1

0.0483

-

wild-type, pH 8.0, 37°C

763618

1.2.3.1

0.057

-

mutant M1088T, pH 8.0, 37°C

763618

1.2.3.1

0.0692

-

pH 8, 37°C

763618

1.2.3.1

0.1356

-

pH 8, 37°C

763618

1.2.3.1

0.18

-

37°C, pH 7.0

644705

1.2.3.1

1.5

-

pH 7.0, 30°C

677264

1.2.3.1

5.566

-

mutant V1016F, pH 8.0, 37°C

763618

1.2.1.8

2 entries

1.2.1.99

2 entries

1.2.3.1

13 entries

1.2.5.2

0.061

-

pH 8.2

389961

4.1.2.63

0.4

-

pH 7.4, 37°C, wild-type enzyme

774545

4.1.3.39

24.8

-

L89A mutant protein, pH 8.0, 25°C

714244

4.1.3.39

33.3

-

L87A/L89A mutant protein, pH 8.0, 25°C

714244

4.1.3.43

24.8

-

L89A variant of BphI, app. Km-value, pH 8.0, 25°C

714244

4.1.3.43

33.3

-

L87A/L89A variant of BphI, app. Km-value, pH 8.0, 25°C

714244

4.1.3.43

80.5

-

Y290F variant of BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C

722458

4.1.3.39

2 entries

4.1.3.43

3 entries

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

1.13.12.16

58

-

pH 7.4, 30°C

696605

1.2.1.3

0.54

-

-

348707

1.2.1.3

12.61

-

at pH 8.0 and 21°C

741416

1.2.1.3

2 entries

1.2.1.46

1.9

-

substrate n-butanol

288247

1.2.5.2

0.33

-

pH 8.2

389961

References & Links

Literature References (136)

top print hide

Show Reference (136 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5153

-

The first recombinent hydroxynitrile lyase in the synthesis of (S)-cyanohydrins

1996

Foerster, S.; Roos, J.; Effenberger, F.; Wajant, H.; Sprauer, A.

Angew. Chem. Int. Ed. Engl.

35

437-439

11936

7592385

Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas

1995

Hensgens, C.M.H.; Hagen, W.R.; Hansen, T.A.

J. Bacteriol.

177

6195-6200

246375

-

Purificationa nd characterization of yeast 3-methyl butanal reductases involved in the removal of wort carbonyls during fermentation

1997

Van Nedervelde, L.; Verlingen, V.; Philipp, D.; Debourg, A.

Proc. Congr. Eur. Brew. Conv.

26

447-454

285569

6397223

Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: pi-ADH

1984

Ditlow, C.C.; Holmquist, B.; Morelock, M.M.; Vallee, B.L.

Biochemistry

23

6363-6368

285571

6375718

Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: chi-ADH

1984

Wagner, F.W.; Pares, X.; Holmquist, B.; Vallee, B.L.

Biochemistry

23

2193-2199

285573

836289

Isolation and characterization of an anodic form of human liver alcohol dehydrogenase

1977

Bosron, W.F.; Li, T.K.

Biochem. Biophys. Res. Commun.

74

85-91

285575

2819035

Purification and steady-state kinetic characterization of human liver beta 3 beta 3 alcohol dehydrogenase

1989

Burnell, J.C.; Li, T.K.; Bosron, W.F.

Biochemistry

28

6810-6815

285579

7011375

Simian liver alcohol dehydrogenase: isolation and characterization of isoenzymes from Saimiri sciureus

1981

Dafeldecker, W.P.; Pares, X.; Vallee, B.L.; Bosron, W.F.; Li, T.K.

Biochemistry

20

856-861

285580

7030395

Simian liver alcohol dehydrogenase: isolation and characterization of isoenzymes from Macaca mulatta

1981

Dafeldecker, W.P.; Meadow, P.E.; Pares, X.; Vallee, B.L.

Biochemistry

20

6729-6734

285603

6360682

Purification and molecular properties of mouse alcohol dehydrogenase isozymes

1983

Algar, E.M.; Seeley, T.L.; Holmes, R.S.

Eur. J. Biochem.

137

139-147

285608

7876099

Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity copared with liver isozymes

1995

Kedishvili, N.Y.; Bosron, W.F.; Stone, C.L.; Hurley, T.D.; Peggs, C.F.; Thomasson, H.R.; Popov, K.M.; Carr, L.G.; Edenberg, H.J.; Li, T.K.

J. Biol. Chem.

270

3625-3630

285623

-

Purification of two alcohol dehydrogenases from Zymomonas mobilis and their properties

1985

Kinoshita, S.; Kakizono, T.; Kadota, K.; Das, K.; Taguchi, H.

Appl. Microbiol. Biotechnol.

22

249-254

285639

-

Purification and properties of an alcohol dehydrogenase from Sporotrichum pulverulentum

1986

Rudge, J.; Bickerstaff, G.F.

Enzyme Microb. Technol.

8

120-124

285647

8532667

Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity

1995

Weinhold, E.G.; Benner, S.A.

Protein Eng.

8

457-461

285651

2099148

Identification of a human stomach alcohol dehydrogenase with distinctive kinetic properties

1990

Yin, S.J.; Wang, M.F.; Liao, C.S.; Chen, C.M.; Wu, C.W.

Biochem. Int.

22

829-835

286052

-

Solubilization and partial characterization of particulate dehydrogenases from Clostridium kluyveri

1974

Hillmer, P.; Gottschalk, G.

Biochim. Biophys. Acta

334

12-23

286203

9327572

Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae

1997

Van Iersel, M.F.; Eppink, M.H.; van Berkel, W.J.; Rombouts, F.M.; Abee, T.

Appl. Environ. Microbiol.

63

4079-4082

286206

10473548

Structural and enzymatic properties of a gastric NADP(H)-dependent and retinal-active alcohol dehydrogenase

1999

Peralba, J.M.; Cederlund, E.; Crosas, B.; Moreno, A.; Julia, P.; Martinez, S.E.; Persson, B.; Farr s, J.; Pares, X.; Jornvall, H.

J. Biol. Chem.

274

26021-26026

286210

11097895

Thermostable NADP(+)-dependent medium-chain alcohol dehydrogenase from Acinetobacter sp. strain M-1: purification and characterization and gene expression in Escherichia coli

2000

Tani, A.; Sakai, Y.; Ishige, T.; Kato, N.

Appl. Environ. Microbiol.

66

5231-5235

286238

16664750

Purification and properties of an NADPH-aldose reductase (aldehyde reductase) from Euonymus japonica leaves

1986

Negm, F.B.

Plant Physiol.

80

972-977

286248

4216364

Purification and properties of calf liver aldose reductase

1974

Attwood, M.A.; Doughty, C.C.

Biochim. Biophys. Acta

370

358-368

286260

9307017

NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis

1997

Neuhauser, W.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.

Biochem. J.

326

683-692

287277

8162187

NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae

1994

Wales, M.R.; Fewson, C.A.

Microbiology

140

173-183

287280

-

Purification and properties of alcohol dehydrogenase from Leuconostoc mesenteroides

1974

Hatanaka, A.; Kajiwara, T.; Tomohiro, S.

Agric. Biol. Chem.

38

1819-1833

287283

7144572

Glycerol dehydrogenase from rabbit muscle

1982

Flynn, T.G.; Cromlish, J.A.

Methods Enzymol.

89

237-242

287287

16742532

The kinetics and reaction mechanism of the nicotinamide-adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle

1967

Toews, C.J.

Biochem. J.

105

1067-1073

287728

-

Isolation and characterization of an new quinoprotein dehydrogenase, L-sorbose/L-sorbosone dehydrogenase

1999

Asakura, A.; Hoshino, T.

Biosci. Biotechnol. Biochem.

63

46-53

287913

3370218

Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain

1988

Ryzlak, M.T.; Pietruszko, R.

Biochim. Biophys. Acta

954

309-324

288069

-

4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenase for arginine degradation in Pseudomonas putida

1986

Yorifuji, T.; Koike, K.; Sakurai, T.; Yokoyama, K.

Agric. Biol. Chem.

50

2009-2016

288081

7584606

Purification and kinetic characterization of gamma-aminobutyraldehyde dehydrogenase from rat liver

1995

Testore, G.; Colombatto, S.; Silvagno, F.; Bedino, S.

Int. J. Biochem. Cell Biol.

27

1201-1210

288125

-

Factors influencing growth on L-lysine by Pseudomonas

1971

Chang, Y.F.; Adams, E.

Methods Enzymol.

17B

166-171

288126

914857

Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism

1977

Chang, Y.F.; Adams, E.

J. Biol. Chem.

252

7979-7986

288166

19091

Purification and properties of rat brain succinic semialdehyde dehydrogenase

1977

Cash, C.; Ciesielski, L.; Maitre, M.; Mandel, P.

Biochimie

59

257-268

288247

-

Substrate specificity of formaldehyde dehydrogenase from Pseudomonas putida

1984

Ogushi, S.; Ando, M.; Tsuru, D.

Agric. Biol. Chem.

48

597-601

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

288472

-

A pyridine nucleotide-independent aldehyde dehydrogenase involved in the alkane oxidation of Acetobacter rancens

1984

Hommel, R.; Kleber, H.P.

FEMS Microbiol. Lett.

22

139-142

347755

1731616

Purification and characterization of pig lung carbonyl reductase

1992

Oritani, H.; Deyashiki, Y.; Nakayama, T.; Hara, A.; Sawada, H.; Matsuura, K.; Bunai, Y.; Ohya, I.

Arch. Biochem. Biophys.

292

539-547

348681

6292666

Aldehyde dehydrogenases from Pseudomonas aeruginosa

1982

Vandecasteele, J.P.; Guerrillot, L.

Methods Enzymol.

89

484-490

348682

10852

Localization and characteristics of rat liver mitochondrial aldehyde dehydrogenases

1976

Siew, C.; Deitrich, R.A.

Arch. Biochem. Biophys.

176

638-649

348694

8605195

Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes

1996

Klyosov, A.A.

Biochemistry

35

4457-4467

348706

3756202

Purification of aldehyde dehydrogenase reconstitutively active in fatty alcohol oxidation from rabbit intestinal microsomes

1986

Ichihara, K.; Noda, Y.; Tanaka, C.; Kusunose, M.

Biochim. Biophys. Acta

878

419-425

348707

2322424

Initial characterization of aldehyde dehydrogenase from rat testis cytosol

1990

Bedino, S.; Testore, G.; Obert, F.

Biol. Chem. Hoppe-Seyler

371

95-101

348725

22435

Purification and characterization of two aldehyde dehydrogenases from Pseudomonas aeruginosa

1977

Guerrillot, L.; Vandecasteele, J.P.

Eur. J. Biochem.

81

185-192

348786

3355167

Purification and characterization of aldehyde dehydrogenase from rat liver mitochondria

1988

Senior, d.J.; Tasi, C.S.

Arch. Biochem. Biophys.

262

211-220

348792

7144584

Isozymes of aldehyde dehydrogenase from horse liver

1982

Eckfeldt, J.H.; Yonetani, T.

Methods Enzymol.

89

474-479

348793

6755180

Aldehyde dehydrogenase from bakers yeast

1982

Tamaki, N.; Hama, T.

Methods Enzymol.

89

469-473

348794

19457

Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae

1977

Tamaki, N.; Nakamura, M.; Kimura, K.; Hama, T.

J. Biochem.

82

73-79

348796

1244351

Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes

1976

Eckfeldt, J.; Mope, L.; Takio, K.; Yonetani, T.

J. Biol. Chem.

251

236-240

348798

11717302

NAD(P)-dependent aldehyde dehydrogenase induced during growth of Ralstonia eutropha strain Bo on tetrahydrofurfuryl alcohol

2001

Schraeder, T.; Zernt, G.; Andreesen, J.R.

J. Bacteriol.

183

7408-7411

389904

-

Identification of the prosthetic group and further characterization of a novel enzyme, polyethylne glycol dehydrogenase

1985

Kawai, F.; Yamanaka, H.; Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.

Agric. Biol. Chem.

49

1071-1076

389961

11222593

Catalytic and molecular properties of the quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase from Ralstonia eutropha strain Bo

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