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Ligand 4-nitrobenzaldehyde

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

1.1.1.184

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzylalcohol + NADP+

762501, 762087

-

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

1.1.3.7

4-nitrobenzyl alcohol + O2 = 4-nitrobenzaldehyde + H2O2

-

-

Substrate in Enzyme-catalyzed Reactions (92 results)

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Show Substrate (92 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

4-nitrobenzaldehyde + NADH + H+ = 4-nitrobenzyl alcohol + NAD+

678116, 721868

-

1.1.1.1

4-nitrobenzaldehyde + NADH + H+ = 4-nitrobenzylalcohol + NAD+

681763

-

1.1.1.1

p-nitrobenzaldehyde + NADH + H+ = p-nitrobenzyl alcohol + NAD+

691867

-

1.1.1.1

p-nitrobenzaldehyde + NADH = p-nitrobenzyl alcohol + NAD+

285603

-

1.1.1.1

4 entries

1.1.1.112

4-nitrobenzaldehyde + NAD(P)H = 4-nitrobenzyl alcohol + NAD(P)+

285758, 285759, 285760

-

1.1.1.145

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

389394

-

1.1.1.145

4-nitrobenzaldehyde + NADPH = ? + NADP+

684725

-

1.1.1.145

2 entries

1.1.1.146

4-nitrobenzaldehyde + NADPH + H+ = ?

740915

-

1.1.1.149

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

286000, 286001, 285998, 285999

-

1.1.1.153

p-nitrobenzaldehyde + NADPH = p-nitrobenzyl alcohol + NADP+

286031, 286021, 286028

-

1.1.1.184

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzyl alcohol + NADP+

347768, 740436, 760819

-

1.1.1.184

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzylalcohol + NADP+

762501, 762087

-

1.1.1.184

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

347762, 347758, 347749, 347763, 347770, 347776, 347755, 688959, 697262, 656548

-

1.1.1.184

4-nitrobenzaldehyde + NADPH = 4-nitrobenzylalcohol + NADP+

655067, 656568

-

1.1.1.188

4-nitrobenzaldehyde + NADPH + H+ = (4-nitrophenyl)methanol + NADP+

724961

-

1.1.1.188

4-nitrobenzaldehyde + NADPH = 4-nitrobenzalcohol + NADP+

389454

-

1.1.1.188

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

389448, 389452, 389453, 389454, 389446

-

1.1.1.184

4 entries

1.1.1.188

3 entries

1.1.1.189

4-nitrobenzaldehyde + NADPH = ?

347776

-

1.1.1.19

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

286139, 286143

-

1.1.1.2

p-nitrobenzaldehyde + NADPH = p-nitrobenzylalcohol + NADP+

286181, 286175, 286176, 286177, 286182, 286184, 286199, 286215, 286164, 286165, 286166, 286172, 286174, 286183, 286190, 286204, 288554, 286167, 286178, 286179, 286185, 286194, 286193, 286205, 286200, 286168

-

1.1.1.209

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

286234

-

1.1.1.21

4-nitrobenzaldehyde + NAD(P)H = 4-nitrobenzyl alcohol + NAD(P)+

286240, 286241, 286253, 286254, 286245, 286248, 286238

-

1.1.1.21

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzyl alcohol + NADP+

697266, 737763

-

1.1.1.21

4-nitrobenzaldehyde + NADPH + H+ = ?

737763

-

1.1.1.21

3 entries

1.1.1.213

4-nitrobenzaldehyde + NAD(P)H = (4-nitrophenyl)methanol + NAD(P)+

347982, 347988

-

1.1.1.220

4-nitrobenzaldehyde + NADPH = 4-nitrobenzylalcohol + NADP+

286310, 286309

-

1.1.1.231

4-nitrobenzaldehyde + NADP+ = 4-nitrobenzoate + NADPH

348016, 348013

-

1.1.1.274

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

669104

-

1.1.1.283

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzyl alcohol + NADP+

670170

-

1.1.1.317

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzoate + NADP+

716558

-

1.1.1.357

4-nitrobenzaldehyde + NAD(P)H + H+ = (4-nitrophenyl)methanol + NAD(P)+

722166

-

1.1.1.50

p-nitrobenzaldehyde + NAD(P)H = p-nitrobenzylalcohol + NAD(P)+

389547, 389546

-

1.1.1.53

4-nitrobenzaldehyde + NADPH = ?

287106

-

1.1.1.53

p-nitrobenzaldehyde + NADPH = p-nitrobenzyl alcohol + NADP+

654932

-

1.1.1.53

2 entries

1.1.1.72

4-nitrobenzaldehyde + NADPH = 4-nitrobenzylalcohol + NADP+

287283

-

1.1.1.91

4-nitrobenzaldehyde + NADPH + H+ = 4-nitrobenzyl alcohol + NADP+

389598

-

1.1.1.91

4-nitrobenzaldehyde + NADPH = 4-nitrobenzyl alcohol + NADP+

724669

-

1.1.3.7

4-nitrobenzaldehyde + O2 = 4-nitrobenzoic acid

711137

-

1.1.3.7

4-nitrobenzaldehyde + O2 = 4-nitrobenzoic acid + H2O2

711137

-

1.11.2.1

4-nitrobenzaldehyde + H2O2 = 4-nitrobenzoic acid + H2O

711105

-

1.11.2.1

methyl 4-nitrobenzyl ether + H2O2 = 4-nitrobenzaldehyde + methanol + H2O

712389

-

1.1.1.91

2 entries

1.1.3.7

2 entries

1.11.2.1

2 entries

1.17.3.2

4-nitrobenzaldehyde + H2O + O2 = 4-nitrobenzoate + H2O2

673434

-

1.2.1.22

p-nitrobenzaldehyde + NAD+ + H2O = p-nitrobenzoate + NADH + H+

695015

-

1.2.1.24

4-nitrobenzaldehyde + NAD+ + H2O = 4-nitrobenzoate + NADH + H+

700082

-

1.2.1.24

p-nitrobenzaldehyde + NAD+ + H2O = p-nitrobenzoate + NADH

288171, 288152

-

1.2.1.3

p-nitrobenzaldehyde + NAD+ + H2O = p-nitrobenzoate + NADH

348694, 348695, 348715, 348703, 348704, 348708, 348712

-

1.2.1.3

p-nitrobenzaldehyde + NAD+ + H2O = p-nitrobenzoic acid + NADH

671512

-

1.2.1.24

2 entries

1.2.1.3

2 entries

1.2.1.32

4-nitrobenzaldehyde + NAD+ + H2O = 4-nitrobenzoate + NADH + H+

390259

-

1.2.1.4

4-nitrobenzaldehyde + NADP+ + H2O = 4-nitrobenzoate + NADPH + H+

712174

-

1.2.1.5

4-nitrobenzaldehyde + NAD+ + H2O = 4-nitrobenzoate + NADH + H+

348787

-

1.2.1.5

p-nitrobenzaldehyde + NADP+ + H2O = p-nitrobenzoate + NADPH + H+

685040

-

1.2.1.5

2 entries

1.2.1.65

4-nitrobenzaldehyde + NAD+ + H2O = 4-nitrobenzoate + NADH + 2 H+

741638

-

1.2.1.8

p-nitrobenzaldehyde + NAD+ + H2O = p-nitrobenzoate + NADH + H+

656550

-

1.2.1.8

p-nitrobenzaldehyde + NADP+ + H2O = p-nitrobenzoate + NADPH + H+

656550

-

1.2.1.8

2 entries

1.2.1.88

4-nitrobenzaldehyde + NAD+ + H2O = 4-nitrobenzoate + NADH + H+

392065

-

1.2.3.1

4-nitrobenzaldehyde + H2O + O2 = 4-nitrobenzoic acid + H2O2

660183

-

1.3.1.20

4-nitrobenzaldehyde + NAD(P)H = 4-nitrobenzylalcohol + NAD(P)+

349239, 349237, 349242, 349254, 349243

-

1.6.2.4

NADPH + H+ + 4-nitrobenzaldehyde = ?

288554

-

1.7.1.B3

p-nitrobenzaldehyde + NADPH + H+ = ? + NADP+

741786

-

2.1.2.1

D-alanine + 4-nitrobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-methyl-3-(4-nitrophenyl)propanoic acid

755784

-

2.1.2.1

D-serine + 4-nitrobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid

755784

-

2.1.2.1

glycine + 4-nitrobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid

755784

-

2.6.1.82

4-nitrobenzaldehyde + cadaverine = 4-nitrobenzylamine + piperideine + H2O

759219

-

2.6.1.82

4-nitrobenzaldehyde + isopropylamine = 4-nitrobenzylamine + acetone + H2O

759219

-

2.1.2.1

3 entries

2.6.1.82

2 entries

2.6.1.B16

(S)-(-)-1-phenyl-ethylamine + 4-nitrobenzaldehyde = 4-nitrobenzylamine + L-alanine

759320

-

3.4.22.3

1-methylpiperidin-4-one + 4-nitrobenzaldehyde = ?

734500

-

3.4.22.3

oxan-2-one + 4-nitrobenzaldehyde = ?

734500

-

3.4.22.3

oxan-3-one + 4-nitrobenzaldehyde = ?

734500

-

3.4.22.3

oxan-4-one + 4-nitrobenzaldehyde = ?

734500

-

3.4.22.3

tert-butyl 4-oxopiperidine-1-carboxylate + 4-nitrobenzaldehyde = tert-butyl 3-[hydroxy(4-nitrophenyl)methyl]-4-oxopiperidine-1-carboxylate

734500

-

3.4.22.3

thiolan-3-one + 4-nitrobenzaldehyde = ?

734500

-

3.4.23.1

4-nitrobenzaldehyde + 1,3-dihydroxypropan-2-one = (3R,4S)-1,3,4-trihydroxy-4-(4-nitrophenyl)butan-2-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + 1-(benzyloxy)propan-2-one = (3R,4S)-3-(benzyloxy)-4-hydroxy-4-(4-nitrophenyl)butan-2-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + 1-hydroxypropan-2-one = (3R,4S)-3,4-dihydroxy-4-(4-nitrophenyl)butan-2-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + 1-methoxypropan-2-one = (3R,4S)-4-hydroxy-3-methoxy-4-(4-nitrophenyl)butan-2-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + cyclohexanone = (2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclohexan-1-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + cyclopentanone = (2S)-2-[(R)-hydroxy(4-nitrophenyl)methyl]cyclopentan-1-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + oxan-4-one = (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]oxan-4-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + propan-2-one = (4R)-4-hydroxy-4-(4-nitrophenyl)butan-2-one

755572

-

3.4.23.1

4-nitrobenzaldehyde + tert-butyl 4-oxopiperidine-1-carboxylate = tert-butyl (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]-4-oxopiperidine-1-carboxylate

755572

-

3.4.23.1

4-nitrobenzaldehyde + thian-4-one = (3S)-3-[(R)-hydroxy(4-nitrophenyl)methyl]thian-4-one

755572

-

4.1.2.10

4-nitrobenzaldehyde + HCN = (R)-4-nitromandelonitrile

727240

-

4.1.2.10

cyanide + 4-nitrobenzaldehyde = (R)-4-nitromandelonitrile

747398

-

4.1.2.10

HCN + 4-nitrobenzaldehyde = (R)-2-hydroxy-2-(4-nitrophenyl)acetonitrile

663423

-

4.1.2.42

4-nitrobenzaldehyde + glycine = D-4-nitrophenylserine

682892

-

4.1.2.42

glycine + 4-nitrobenzaldehyde = (2R,3S)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid + (2R,3R)-2-amino-3-hydroxy-3-(4-nitrophenyl)propanoic acid

665293

-

4.1.2.42

glycine + 4-nitrobenzaldehyde = (betaS)-beta-hydroxy-4-nitro-D-phenylalanine

691309

-

4.1.2.42

glycine + 4-nitrobenzaldehyde = D-3-(4-nitrophenyl)serine

747468

-

3.4.22.3

6 entries

3.4.23.1

10 entries

4.1.2.10

3 entries

4.1.2.42

4 entries

4.1.2.45

4-nitrobenzaldehyde + pyruvate = 4-(4-nitrophenyl)-2-oxobut-3-enoate + H2O

726697

-

4.2.1.84

4-nitrobenzaldehyde + HCN + H2O = ? + H2O

654314

-

4.2.1.B27

4-nitrobenzaldehyde + nitromethane = 2-nitro-1-(4-nitrophenyl)ethanol

733949

-

7.1.1.2

NADH + H+ + 4-nitrobenzaldehyde = NAD+ + ?

714281

-

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

4-nitrobenzyl alcohol + NAD+ = 4-nitrobenzaldehyde + NADH + H+

-

-

1.1.1.50

p-nitrobenzylalcohol + NAD+ = p-nitrobenzaldehyde + NADH

389546

-

1.1.3.7

4-nitrobenzyl alcohol + O2 = 4-nitrobenzaldehyde + H2O2

-

-

1.1.3.9

4-nitrobenzyl alcohol + O2 = 4-nitrobenzaldehyde + H2O2

389850

-

1.11.2.1

1-(methoxymethyl)-4-nitrobenzene + H2O2 = 4-nitrobenzaldehyde + methanol + H2O

-

-

1.11.2.1

4-nitrobenzyl alcohol + H2O2 = 4-nitrobenzaldehyde + H2O

-

-

1.11.2.1

methyl 4-nitrobenzyl ether + H2O2 = 4-nitrobenzaldehyde + methanol + H2O

-

-

1.11.2.1

3 entries

1.14.99.21

(1E)-2-methyl-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-1-en-1-yl 4-nitrobenzoate + O2 = 4-(2,6,6-trimethylcyclohex-1-en-1-yl)butan-2-one + CO2 + 4-nitrobenzaldehyde

-

-

1.4.3.4

p-nitrobenzylamine + H2O + O2 = 4-nitrobenzaldehyde + NH3 + H2O2

-

-

4.1.1.7

p-nitrobenzoylformate = p-nitrobenzaldehyde + CO2

-

-

4.1.1.74

4-nitro-benzoylformic acid = 4-nitrobenzaldehyde + CO2

651152

-

4.1.2.47

(1S)-2-nitro-1-(4-nitrophenyl)ethanol = 4-nitrobenzaldehyde + CH3NO2

-

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.188

competitive inhibition of PGD2 but not of PGH2 reduction

389454

-

1.1.1.21

at concentration above 2 mM substrate inhibition

286250

-

1.2.1.24

1 mM, 20% inhibition

288166

-

1.2.1.3

substrate inhibition

348694

-

1.2.1.3

substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition

348704

-

1.2.1.3

2 entries

1.2.1.65

substrate inhibition

741638

-

3D Structure of Enzyme-Ligand-Complex (PDB) (25 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (25 entries)

EC NUMBER

ENZYME 3D STRUCTURE

3.1.1.3

4flf, 3D-view

3.1.1.3

4glb, 3D-view

3.1.1.3

4kjx, 3D-view

3.1.1.3

4n8s, 3D-view

3.1.1.3

4s0x, 3D-view

3.1.1.3

4flf, 3D-view

3.1.1.3

4glb, 3D-view

3.1.1.3

4kjx, 3D-view

3.1.1.3

4n8s, 3D-view

3.1.1.3

4s0x, 3D-view

3.1.1.3

4flf, 3D-view

3.1.1.3

4glb, 3D-view

3.1.1.3

4kjx, 3D-view

3.1.1.3

4n8s, 3D-view

3.1.1.3

4s0x, 3D-view

3.1.1.3

4flf, 3D-view

3.1.1.3

4glb, 3D-view

3.1.1.3

4kjx, 3D-view

3.1.1.3

4n8s, 3D-view

3.1.1.3

4s0x, 3D-view

3.1.1.3

4flf, 3D-view

3.1.1.3

4glb, 3D-view

3.1.1.3

4kjx, 3D-view

3.1.1.3

4n8s, 3D-view

3.1.1.3

4s0x, 3D-view

3.1.1.3

25 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (24 results)

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Show Turnover Number (24 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

4.6

-

in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C

681763

1.1.1.1

4.6

-

native enzyme, at 55°C

678116

1.1.1.1

2 entries

1.1.1.145

16.7

-

pH 7.4, 25°C

684725

1.1.1.149

5.91

-

+/-33.4

286001

1.1.1.184

0.0098

-

pH 6.5, 25°C

688959

1.1.1.184

0.0283

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

0.3

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

1.087

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

3.48

-

pH 6.5, 25°C

740436

1.1.1.2

9.5

-

-

286168

1.1.1.2

22

-

-

286165

1.1.1.184

5 entries

1.1.1.2

2 entries

1.1.1.21

0.57

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.283

1.24

-

1 mM

670170

1.1.1.317

8.26

-

pH 8.5, 37°C

716558

1.1.1.50

1.08

-

-

389547

1.1.3.7

1.21

-

mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0

711137

1.1.3.7

1.633

-

wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0

711137

1.2.1.3

0.23

-

-

348708

1.2.1.3

7.17

-

enzyme ALDH-2

348694

1.1.3.7

2 entries

1.2.1.3

2 entries

1.2.1.65

59

-

pH 8.0, temperature not specified in the publication

741638

1.3.1.20

11.3

-

-

349237

1.7.1.B3

30

-

pH 7.0, 25°C

741786

4.2.1.B27

0.35

-

30°C, pH not specified in the publication

733949

4.2.1.B27

0.45

-

40°C, pH not specified in the publication

733949

4.2.1.B27

2 entries

K_M Value (98 results)

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Show KM Value (98 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.145

1.966

-

-

389394

1.1.1.145

13

-

pH 7.4, 25°C

684725

1.1.1.149

0.221

0.254

-

285999

1.1.1.149

0.34

-

-

285998

1.1.1.149

0.3811

-

+/-0.0605

286001

1.1.1.145

2 entries

1.1.1.149

3 entries

1.1.1.153

0.43

-

-

286021

1.1.1.184

0.12

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

0.13

-

pH 6.5, 25°C

688959

1.1.1.184

0.2

-

pH 6.0, 25°C, recombinant enzyme

656568

1.1.1.184

0.338

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

0.354

-

at 100 mM sodium phosphate buffer, pH 6.5, 0.065 mM NADPH, 25°C

697262

1.1.1.184

0.44

-

pH 6.5, 25°C

740436

1.1.1.184

0.45

-

-

347776

1.1.1.184

0.64

-

recombinant protein purified from E. coli

347768

1.1.1.184

1.1

-

-

347770

1.1.1.184

1.3

1.6

Km depending on enzyme form

347763

1.1.1.184

1.6

2

Km depending on enzyme form

347749

1.1.1.188

0.0008

-

-

389446

1.1.1.188

0.0008

-

liver enzyme

389453

1.1.1.188

0.0083

-

lung enzyme

389453

1.1.1.188

0.0143

-

-

389454

1.1.1.188

0.0143

-

37°C, liver-type isozyme

389454

1.1.1.188

0.0774

-

-

389448

1.1.1.188

0.125

-

lung enzyme

389460

1.1.1.184

11 entries

1.1.1.188

7 entries

1.1.1.189

0.45

-

-

347776

1.1.1.19

0.133

-

-

286143

1.1.1.19

0.35

-

-

286139

1.1.1.2

0.0013

-

low-Km reductase

286166

1.1.1.2

0.0026

-

low-Km reductase

286215

1.1.1.2

0.004

-

low-Km aldehyde reductase

286166

1.1.1.2

0.0053

-

-

286205

1.1.1.2

0.006

-

-

286164

1.1.1.2

0.0084

-

AR3

286178

1.1.1.2

0.029

-

aldehyde reductase I

286181

1.1.1.2

0.034

-

AR2

286181

1.1.1.2

0.041

-

high-Km reductase

286215

1.1.1.2

0.044

-

-

286190

1.1.1.2

0.071

-

AR1

286178

1.1.1.2

0.08

-

-

286175

1.1.1.2

0.12

-

-

286204

1.1.1.2

0.129

-

G2

286178

1.1.1.2

0.15

-

-

286168

1.1.1.2

0.16

-

wild-type aldehyde reductase

286199, 286200

1.1.1.2

0.169

-

aldehyde reductase II

286181

1.1.1.2

0.2

-

enzyme from kidney, brain or liver

286183

1.1.1.2

0.23

-

-

286174

1.1.1.2

0.25

-

aldehyde reductase, mutant R308A

286200

1.1.1.2

0.25

-

high-Km aldehyde reductase

286166

1.1.1.2

0.262

-

AR4

286178

1.1.1.2

0.27

-

-

286172

1.1.1.2

0.29

-

high-Km aldehyde reductase

286166

1.1.1.2

0.31

-

-

288554

1.1.1.2

0.35

-

-

286165

1.1.1.2

0.38

-

aldehyde reductase, mutant V299C

286199

1.1.1.2

0.38

-

mutant R311A

286200

1.1.1.2

0.8

-

-

286193

1.1.1.2

1.1

-

AR3

286181

1.1.1.2

1.2

-

-

286190

1.1.1.2

1.2

-

aldehyde reductase, mutant I298C

286199

1.1.1.2

1.2

-

AR1

286184

1.1.1.2

2.8

-

aldehyde reductase, mutant I298A

286199

1.1.1.2

5.9

-

aldehyde reductase, mutant H112Q

286199

1.1.1.21

0.002

-

-

286241

1.1.1.21

0.003

-

-

286238

1.1.1.21

0.003

-

4-hydroxyphenylglycolaldehyde

286241

1.1.1.21

0.0035

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.21

0.007

-

-

286253

1.1.1.19

2 entries

1.1.1.2

35 entries

1.1.1.21

5 entries

1.1.1.213

0.163

0.211

-

347988

1.1.1.220

0.1

-

-

286309

1.1.1.231

0.0667

-

-

348013

1.1.1.283

0.85

-

1 mM

670170

1.1.1.317

0.28

-

pH 8.5, 37°C

716558

1.1.1.357

1

-

pH 7.0, temperature not specified in the publication, NAD(P)H

722166

1.1.1.357

1.09

-

pH 7.0, temperature not specified in the publication, NAD(P)H

722166

1.1.1.357

2 entries

1.1.1.50

0.087

-

NADPH, detection spectrophotometrically

389547

1.1.1.91

0.04

-

-

389598

1.1.3.7

2

-

mutant enzyme Y92F, wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0

711137

1.1.3.7

5

-

wild type enzyme, at 24°C, 0.1 M sodium phosphate buffer, pH 6.0

711137

1.1.3.7

2 entries

1.17.3.2

0.011

-

pH 7.0

673434

1.2.1.24

0.033

-

-

288171

1.2.1.24

0.156

-

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

700082

1.2.1.24

0.1612

-

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

700082

1.2.1.3

0.000007

-

enzyme ALDH-2

348694

1.2.1.3

0.0001

-

native enzyme

348695

1.2.1.3

0.0004

-

mutant enzyme S74A

348695

1.2.1.3

0.0034

-

-

348708

1.2.1.3

0.018

-

isoenzyme ALDH-II

348715

1.2.1.3

0.056

-

membrane-bound isoenzyme ALDH

348715

1.2.1.3

2

-

isoenzyme ALDH-I

348715

1.2.1.24

3 entries

1.2.1.3

7 entries

1.2.1.32

0.31

-

-

390259

1.2.1.65

0.011

-

pH 8.0, temperature not specified in the publication

741638

1.2.1.8

0.5

-

pH 7.7, coenzyme NAD+

656550

1.2.1.88

0.27

-

isoform A

392065

1.3.1.20

3.3

-

-

349237

1.6.2.4

0.31

-

-

288554

1.7.1.B3

0.17

-

pH 7.0, 25°C

741786

4.2.1.B27

0.62

-

40°C, pH not specified in the publication

733949

4.2.1.B27

0.72

-

30°C, pH not specified in the publication

733949

4.2.1.B27

2 entries

K_i Value (2 results)

top print hide

Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.188

0.023

-

37°C, liver-type isozyme, versus prostaglandin D2

389454

1.2.1.65

0.126

-

pH 8.0, temperature not specified in the publication

741638

References & Links

Literature References (147)

top print hide

Show Reference (147 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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

285758

2674111

Monkey liver indanol dehydrogenase. Purification, properties, and kinetic mechanism

1989

Hara, A.; Mouri, K.; Nakagawa, M.; Nakamura, M.; Nakayama, T.; Matsuura, K.; Saweda, H.

J. Biochem.

106

126-132

285759

2559080

3(20)alpha-hydroxysteroi dehydrogenase activity of monkey liver indanol dehydrogenase

1989

Hara, A.; Nakagawa, M.; Taniguchi, H.; Saweda, H.

J. Biochem.

106

900-903

285760

3527067

Isolation of multiple forms of indanol dehydrogenase associated with 17-beta-hydroxysteroid dehydrogenase activity from male rabbit

1986

Hara, A.; Kariya, K.; Nakamura, M.; Nakayama, T.; Saweda, H.

Arch. Biochem. Biophys.

249

225-236

285998

8280099

Purification and characterization of a novel dimeric 20alpha-hydroxysteroid dehydrogenase from Tetrahymena pyriformis

1994

Inazu, A.; Sato, K.; Nakayama, T.; Deyashiki, Y.; Hara, A.; Nozawa, Y.

Biochem. J.

297

195-200

285999

7484385

Substrate specificity and kinetic mechanism of Tetrahymena 20alpha-hydroxysteroid dehydrogenase

1995

Hara, A.; Inazu, A.; Deyashiki, Y.; Nozawa, Y.

Adv. Exp. Med. Biol.

372

249-258

286000

8977402

Expression, purification and characterization of the rat luteal 20alpha-hydroxysteroid dehydrogenase

1997

Mao, J.; Duan, R.W.; Zhong, L.; Gibori, G.; Azhar, S.

Endocrinology

138

182-190

286001

10417353

Characterization of homogeneous recombinant rat ovarian 20alpha-hydroxysteroid dehydrogenase: fluorescent properties and inhibition profile

1999

Ma, H.; Penning, T.M.

Biochem. J.

341

853-859

286021

3904835

Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes

1985

Sueoka, T.; Katoh, S.

Biochim. Biophys. Acta

843

193-198

286028

11306098

Role of the conserved Ser-Tyr-Lys triad of the SDR family in sepiapterin reductase

2001

Fujimoto, K.; Hara, M.; Yamada, H.; Sakurai, M.; Inaba, A.; Tomomura, A.; Katoh, S.

Chem. Biol. Interact.

130-132

825-832

286031

-

Isolation and characterization of sepiapterin reductase from Drosophila melanogaster

1993

Yoon, K.H.; Cha, K.W.; Park, S.I.; Yim, J.J.

Pteridines

4

43-50

286139

6755181

Aldehyde reductase (L-hexonate: NADP dehydrogenase) from pig kidney

1982

Flynn, T.G.; Cromlish, J.A.; Davidson, W.S.

Methods Enzymol.

89

501-506

286143

15991

Resolution and partial characterization of two aldehyde reductases of mammalian liver

1977

Tulsiani, D.R.P.; Touster, O.

J. Biol. Chem.

252

2545-2550

286164

4393513

Purification and characterization of a reduced nicotinamide adenine dinucleotide phosphate-linked aldehyde reductase from brain

1970

Tabakoff, B.; Erwin, G.

J. Biol. Chem.

245

3263-3268

286165

4402936

Triphosphopyridine nucleotide-linked aldehyde reductase I. Purification and properties of the enzyme from pig kidney cortex

1972

Bosron, W.F.; Prairie, R.L.

J. Biol. Chem.

217

4480-4485

286166

4146452

The characterization of two reduced nicotinamide-adenine dinucleotide phosphate-linked aldehyde reductases from pig brain

1972

Turner, A.J.; Tipton, K.F.

Biochem. J.

130

765-772

286167

235531

Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney. Amino acid composition, reactivity of cysteinyl residues, and stereochemistry of D-glyceraldehyde reduction

1975

Flynn, T.G.; Shires, J.; Walton, D.J.

J. Biol. Chem.

250

2933-2940

286168

16919

Purification and properties of NADPH-dependent aldehyde reductase from human liver

1977

Wermuth, B.; Muench, J.D.B.; von Wartburg, J.P.

J. Biol. Chem.

252

3821-3828

286172

6989609

Purification and some properties of aldehyde reductases from pig liver

1980

Branlant, G.M; Biellmann, J.F.

Eur. J. Biochem.

105

611-621

286174

7448191

Isolation and characterization of rat liver aldehyde reductase

1980

Turner, A.J.; Hryszko, J.

Biochim. Biophys. Acta

613

256-265

286175

6798966

Purification of the high-Km aldehyde reductase from rat brain and liver and from ox brain

1981

Rivett, A.J.; Smith, I.L.; Tipton, K.F.

Biochem. J.

197

473-481

286176

6749832

Kinetic mechanisms in the reduction of aldehydes and ketones catalyzed by rabbit liver aldehyde reductases and hydroxysteroid dehydrogenases

1982

Sawada, H.; Hara, A.; Nakayama, T.; Hayashibara, M.

J. Biochem.

92

185-191

286177

6814444

Aldehyde reductases: Monomeric NADPH-dependent oxidoreductases with multifunctional potential

1982

Flynn, T.G.

Biochem. Pharmacol.

31

2705-2712

286178

6753832

Purification and characterization of the multiple forms of aldehyde reductase in ox kidney

1982

Daly, A.K.; Mantle, T.J.

Biochem. J.

205

373-380

286179

6814425

The kinetic mechanism of the major form of ox kidney aldehyde reductase with D-glucuronic acid

1982

Daly, A.K.; Mantle, T.J.

Biochem. J.

205

381-388

286181

6753936

Purification and properties of human liver aldehyde reductases

1982

Petrash, J.M.; Srivastava, S.K.

Biochim. Biophys. Acta

707

105-114

286182

6404249

Tissue distribution of mammalian aldose reductase and related enzymes

1983

Markus, H.B.; Raducha, M.; Harris, H.

Biochem. Med.

29

31-45

286183

6416297

Purification and properties of an NADPH-linked aldehyde reductase from rat kidney

1983

Takahashi, N.; Saito, T.; Tomita, K.

Biochim. Biophys. Acta

748

444-452

286184

6343086

Isolation and characterization of multiforms of aldehyde reductase in chicken kidney

1983

Hara, A.; Deyashiki, Y.; Nakayama, T.; Sawada, H.

Eur. J. Biochem.

133

207-214

286185

6339239

The kinetics and mechanism of pig-liver aldehyde reductase. Comparative studies with pyridine-3-aldehyde and p-carboxybenzaldehyde

1983

Magnien, A.; Branlant, G.

Eur. J. Biochem.

131

375-381

286190

3593233

Kinetic mechanism of sheep liver NADPH-dependent aldehyde reductase

1987

De Jongh, K.S.; Schofield, P.J.; Edwards, M.R.

Biochem. J.

242

143-150

286193

2663637

The NADP-linked aldehyde reductase from Trypanosoma cruzi subcellular localization and some properties

1989

Arauzo, S.; Cazzulo, J.J.

FEMS Microbiol. Lett.

58

283-286

286194

-

A novel NADPH-dependent aldehyde reductase, catalyzing asymmetric reduction of beta-keto acid esters, from Sporobolomyces salmonicolor: purification and characterization

1990

Yamada, H.; Shimizu, S.; Kataoka, M.; Sakai, H.; Miyoshi, T.

FEMS Microbiol. Lett.

70

45-48

286199

7669785

Mechanism of human aldehyde reductase: characterization of the active site pocket

1995

Barski, O.A.; Gabbay, K.H.; Grimshaw, C.E.; Bohren, K.M.

Biochemistry

34

11264-11275

286200

8916913

The C-terminal loop of aldehyde reductase determines the substrate and inhibitor specificity

1996

Barski, O.A.; Gabbay, K.H.; Bohren, K.M.

Biochemistry

35

14276-14280

286204

9693960

Mitochondrial aldehyde reductase: identification and characterization in rat liver and kidney cortex

1998

Udovikova, E.A.; Wojtczak, L.

Int. J. Biochem. Cell Biol.

30

597-608

286205

9952458

Purification and characterization of a NADPH-dependent aldehyde reductase from mung bean that detoxifies eutypine, a toxin from Eutypa lata1

1999

Colrat, S.; Latche, A.; Guis, M.; Pech, J.C.; Bouzayen, M.; Fallot, J.; Roustan, J.P.

Plant Physiol.

119

621-626

286215

45199

Purification from human brain and some properties of two NADPH-linked aldehyde reductases which reduce succinic semialdehyde to 4-hydroxybutyrate

1979

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

J. Neurochem.

33

1169-1175

286234

2691507

Identification of two dihydrodiol dehydrogenases associated with 3(17)alpha-hydoxysteroid dehydrogenase activity in mouse kidney

1989

Nakagawa, M.; Tsukuda, F.; Nakayama, T.; Matsuura, K.; Hara, A.; Sawada, H.

J. Biochem.

106

633-638

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

286240

6815419

Aldose reductase from human tissues

1982

Wermuth, B.; von Wartburg, J.P.

Methods Enzymol.

89

181-186

286241

6814912

Purification and characterization of human-brain aldose reductase

1982

Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.

Eur. J. Biochem.

127

279-284

286245

6402510

Purification and characterization of two aldose reductase isoenzymes from rabbit muscle

1983

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

J. Biol. Chem.

258

3416-3424

286248

4216364

Purification and properties of calf liver aldose reductase

1974

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

Biochim. Biophys. Acta

370

358-368

286250

6426471

Bovine lens aldehyde reductase (aldose reductase)

1984

Halder, A.B.; Crabbe, M.J.C.

Biochem. J.

219

33-39

286253

1815509

Purification and characterization of aldose reductase and aldehyde reductase from human kidney

1991

Ansari, N.H.; Bhatnagar, A.; Liu, S.; Srivastava, S.K.

Biochem. Int.

25

755-765

286254

8117659

Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme

1994

Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe, D.; Petsko, G.A.; Gabbay, K.H.

Biochemistry

33

2021-2032

286309

2656673

The biosynthesis of tetrahydrobiopterin in rat brain. Purification and characterization of 6-pyruvoyl tetrahydropterin (2-oxo)reductase

1989

Milstien, S.; Kaufman, S.

J. Biol. Chem.

264

8066-8073

286310

2511841

Human liver 6-pyruvoyl tetrahydropterin reductase is biochemically and immunologically indistinguishable from aldose reductase

1989

Steinerstauch, P.; Wermuth, B.; Leimbacher, W.; Curtius, H.C.

Biochem. Biophys. Res. Commun.

164

1130-1136

287106

1377683

Pig testicular 20beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity

1992

Tanaka, M.; Ohno, S.; Adachi, S.; Nakajin, S.; Shinoda, M.; Nagahama, Y.

J. Biol. Chem.

267

13451-13455

287283

7144572

Glycerol dehydrogenase from rabbit muscle

1982

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

Methods Enzymol.

89

237-242

288152

3190233

Human brain high Km aldehyde dehydrogenase: purification, characterization, and identification as NAD+-dependent succinic semialdehyde dehydrogenase

1988

Ryzlak, M.T.; Pietruszko, R.

Arch. Biochem. Biophys.

266

386-396

288166

19091

Purification and properties of rat brain succinic semialdehyde dehydrogenase

1977

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

Biochimie

59

257-268

288171

-

Purification and properties of succinic semialdehyde dehydrogenase from Lumbricus rubellus

1994

Koh, Y.S.; Joo, C.N.; Choi, S.Y.; Kim, D.S.

Korean Biochem. J.

27

75-79

288554

3084464

Characterization of microsomal NADPH-dependent aldehyde reductase from rat brain

1986

Takahashi, N.; Saito, T.; Goda, Y.; Tomita, K.

J. Biochem.

99

513-519

347749

7005231

Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase

1981

Wermuth, B.

J. Biol. Chem.

256

1206-1213

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

347758

6439186

Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver

1984

Usui, S.; Hara, A.; Nakayama, T.; Sawada, H.

Biochem. J.

223

697-705

347762

1338044

Characterization of multiple forms of carbonyl reductase from chicken liver

1993

Nishinaka, T.; Kinoshita, Y.; Terada, N.; Terada, T.; Mizoguchi, T.; Nishihara, T.

Enzyme

46

221-228

347763

1540623

Carbonyl reductase from human testis: purification and comparison with carbonyl reductase from human brain and rat testis

1992

Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.

Biochim. Biophys. Acta

1116

50-56

347768

8779568

Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product

1996

Kita, K.; Matsuzaki, K.; Hashimoto, T.; Yanase, H.; Kato, N.; Chung, M.C.; Kataoka, M.; Shimizu, S.

Appl. Environ. Microbiol.

62

2303-2310

347770

7990149

Expression, crystallization and preliminary crystallographic analysis of human carbonyl reductase

1994

Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.; Gabbay, K.H.

J. Mol. Biol.

244

659-664

347776

1597188

Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney. Identity with human carbonyl reductase

1992

Schieber, A.; Frank, R.W.; Ghisla, S.

Eur. J. Biochem.

206

491-502

347982

6435601

Purification and properties of a 3alpha-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs

1984

Penning, T.M.; Mukharji, I.; Barrows, S.; Talalay, P.

Biochem. J.

222

601-611

347988

8939970

Characterization of the substrate binding site in rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase. The roles of tryptophans in ligand binding and protein fluorescence

1996

Jez, J.M.; Schlegel, B.P.; Penning, T.M.

J. Biol. Chem.

271

30190-30198

348013

7061415

The purification and characterization of a prostacyclin dehydrogenase from rabbit kidney

1982

Korff, J.M.; Jarabak, J.

J. Biol. Chem.

257

2177-2181

348016

11306100

Characterization of multiple Chinese hamster carbonyl reductases

2001

Terada, T.; Sugihara, Y.; Nakamura, K.; Sato, R.; Sakuma, S.; Fujimoto, Y.; Fujita, T.; Inazu, N.; Maeda, M.

Chem. Biol. Interact.

130-132

847-861

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

348695

8043582

Involvement of Serine 74 in the Enzyme-Coenzyme Interaction of Rat Liver Mitochondrial Aldehyde Dehydrogenase

1994

Rout, U.K.; Weiner, H.

Biochemistry

33

8955-8961

348703

-

Pre-steady-state kinetics of aldehyde oxidation by pig liver cytosolic aldehyde dehydrogenase

1988

Hill, J.P.; Dickinson, F.M.

Biochem. Soc. Trans.

16

856-857

348704

-

Steady-state kinetics of aldehyde by pig liver cytosolic aldehyde dehydrogenase

1988

Hill, J.P.; Dickinson, F.M.

Biochem. Soc. Trans.

16

857-858

348708

6651766

Bovine lens aldehyde dehydrogenase. Kinetics and mechanism

1983

Ting, H.H.; Crabbe, M.J.C.

Biochem. J.

215

361-368

348712

223840

Purification and properties of sheep-liver aldehyde dehydrogenases

1979

MacGibbon, A.K.H.; Motion, R.L.

Eur. J. Biochem.

96

585-595

348715

-

Purification and characterization of the rat liver mitochondrial aldehyde dehydrogenase

1991

Han, I.O.; Joo, C.N.

Hanguk Saenghwahakhoe Chi

24

353-360

348787

2802624

Characterization of rat cornea aldehyde dehydrogenase

1989

Evces, S.; Lindahl, R.

Arch. Biochem. Biophys.

274

518-524

349237

2697716

Dimeric dihydrodiol dehydrogenase in monkey kidney. Substrate specificity, stereospecificity of hydrogen transfer, and distribution

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