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Ligand glyceraldehyde

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for glyceraldehyde

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (7 results)

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

DL-glyceraldehyde + NADPH + H+ = DL-glycerol + NADP+

711903

-

1.1.1.21

DL-glyceraldehyde + NADPH + H+ = DL-glycerol + NADP+

711356, 713006, 713240, 711353, 713242, 711903

-

1.1.1.21

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

668222

-

1.1.1.21

glyceraldehyde + NADPH + H+ = glycerol + NADP+

738833

-

1.1.1.21

3 entries

1.1.1.265

glyceraldehyde + NAD(P)H = glycerol + NAD(P)+

246375

-

1.2.1.48

glyceraldehyde + NAD+ + H2O = ?

697840

-

1.2.7.5

glyceraldehyde + H2O + oxidized ferredoxin = glycerate + H+ + reduced ferredoxin

11938

-

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

1.1.1.202

glycerol + NAD+ = glyceraldehyde + NADH + H+

0

-

1.1.3.41

glycerol + O2 = glyceraldehyde + H2O2

0

-

1.1.3.B4

glycerol + O2 = glyceraldehyde + H2O2

0

-

Substrate in Enzyme-catalyzed Reactions (99 results)

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Show Substrate (99 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

DL-glyceraldehyde + H+ = glycerol + NAD+

667266

-

1.1.1.10

DL-glyceraldehyde + NADPH = dihydroxyacetone + NADP+

656049

-

1.1.1.112

DL-glyceraldehyde + NADH = glycerol + NAD+

285760

-

1.1.1.149

DL-glyceraldehyde + NADPH = glycerol + NADP+

286000, 286001

-

1.1.1.185

glyceraldehyde + NADPH + H+ = ?

286134

-

1.1.1.188

DL-glyceraldehyde + NADPH = DL-glycerol + NADP+

389454

-

1.1.1.189

DL-glyceraldehyde + NADPH + H+ = ?

389468

-

1.1.1.19

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

286143

-

1.1.1.2

DL-glyceraldehyde + NADPH + H+ = ? + NADP+

738838

-

1.1.1.2

DL-glyceraldehyde + NADPH + H+ = DL-glycerol + NADP+

711903

-

1.1.1.2

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

286168, 286181, 286199, 669787, 286196, 695864, 286200

-

1.1.1.2

glyceraldehyde + NADPH + H+ = glycerol + NADP+

286186, 286187

-

1.1.1.2

4 entries

1.1.1.20

glyceraldehyde + NADPH = ?

286222

-

1.1.1.202

glyceraldehyde + NADH + H+ = ? + NAD+

739886

-

1.1.1.21

DL-glyceraldehyde + NAD(P)H + H+ = glycerol + NAD(P)+

761025

-

1.1.1.21

DL-glyceraldehyde + NAD(P)H = glycerol + NAD(P)+

684768, 286221, 286241, 286253, 286254, 286261, 286262, 286263, 286247, 286250, 286256, 286255, 286258, 286238

-

1.1.1.21

DL-glyceraldehyde + NADPH + H+ = ?

738840

-

1.1.1.21

DL-glyceraldehyde + NADPH + H+ = DL-glycerol + NADP+

711356, 713006, 713240, 711353, 713242, 711458, 711903, 712014

-

1.1.1.21

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

668222, 669030, 695930, 696552, 696708, 697273, 667553, 667807, 669455, 697266, 699247, 699641, 667331, 696723, 696742, 737604, 737763, 738031, 738160, 700796, 669794, 738838, 739042

-

1.1.1.21

DL-glyceraldehyde + NADPH = glycerol + NAD(P)+

669455

-

1.1.1.21

DL-glyceraldehyde + NADPH = glycerol + NADP+

685200, 655525, 685547, 686528, 689107, 723017, 723337, 737604, 722192, 722285

-

1.1.1.21

glyceraldehyde + NADPH + H+ = glycerol + NADP+

667913, 668511, 667224, 667349, 667923, 667931, 738833

-

1.1.1.21

8 entries

1.1.1.265

glyceraldehyde + NAD(P)H = glycerol + NAD(P)+

246375

-

1.1.1.274

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

669104

-

1.1.1.283

DL-glyceraldehyde + NADPH = glycerol + NADP+

670170

-

1.1.1.307

DL-glyceraldehyde + NADH + H+ = glycerol + NAD+

696073

-

1.1.1.307

DL-glyceraldehyde + NADH + H+ = xylitol + NAD+

765123

-

1.1.1.307

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

286260, 696073

-

1.1.1.307

3 entries

1.1.1.365

DL-glyceraldehyde + NADPH + H+ = ?

724270, 724580

-

1.1.1.430

DL-glyceraldehyde + NADH + H+ = glycerol + NAD+

764945

-

1.1.1.431

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

699278, 764945

-

1.1.1.6

DL-glyceraldehyde + NAD+ = 3-hydroxypyruvaldehyde + NADH

636283, 636285, 636289, 636294

-

1.1.1.6

DL-glyceraldehyde + NADH = glycerol + NAD+

636297

-

1.1.1.6

2 entries

1.1.1.71

DL-glyceraldehyde + NADPH + H+ = ?

740291

-

1.1.1.72

DL-glyceraldehyde + NADPH + H+ = glycerol + NADP+

712771

-

1.1.1.76

glyceraldehyde + NADH + H+ = ?

737540

-

1.1.1.78

DL-glyceraldehyde + NAD+ = ?

207968, 207975

-

1.1.1.78

glyceraldehyde + NADH = glycerol + NAD+

207969

-

1.1.1.78

2 entries

1.1.2.8

glyceraldehyde + phenazine methosulfate = ? + reduced phenazine methosulfate

762829

-

1.1.3.9

glyceraldehyde + O2 = ? + H2O2

687852

-

1.1.99.12

DL-glyceraldehyde + acceptor = ? + reduced acceptor

287728

-

1.1.99.14

DL-glyceraldehyde + nitro blue tetrazolium = ? + reduced nitro blue tetrazolium

725738

-

1.1.99.28

DL-Glyceraldehyde + D-fructose = ?

10900

-

1.17.1.4

glyceraldehyde + 2,6-dichloroindophenol + H2O = ?

659210

-

1.2.1.12

DL-glyceraldehyde + phosphate + NAD+ = D-glyceroyl phosphate + NADH

287913

-

1.2.1.12

glyceraldehyde + NAD+ + H2O = glycerate + NADH + H+

688953

-

1.2.1.12

2 entries

1.2.1.20

DL-glyceraldehyde + NAD+ + H2O = glycerate + NADH

288126, 288125

-

1.2.1.21

DL-glyceraldehyde + NAD+ + H2O = 2,3-dihydroxypropanoic acid + NADH + H+

390211

-

1.2.1.22

DL-glyceraldehyde + NAD+ + H2O = glycerate + NADH

674270

-

1.2.1.24

glyceraldehyde + NAD+ + H2O = glycerate + NADH

674654

-

1.2.1.26

DL-glyceraldehyde + NADP+ + H2O = glycerate + NADPH + H+

719837, 715548

-

1.2.1.3

DL-glyceraldehyde + NAD+ + H2O = DL-glycerate + NADH + H+

722210

-

1.2.1.3

glyceraldehyde + NAD+ + H2O = glycerate + NADH

348683, 348721, 348700, 348707, 348708, 348723, 348702

-

1.2.1.3

glyceraldehyde + NAD+ + H2O = glycerate + NADH + H+

712435, 726464, 713308

-

1.2.1.4

glyceraldehyde + NADP+ + H2O = glycerate + NADPH + H+

723749, 739966

-

1.2.1.4

glyceraldehyde + NADP+ = glycerate + NADPH

437834

-

1.2.1.3

3 entries

1.2.1.4

2 entries

1.2.1.48

glyceraldehyde + NAD+ + H2O = ?

697840

-

1.2.1.5

DL-glyceraldehyde + NAD(P)+ + H2O = glycerate + NAD(P)H + H+

656571

-

1.2.1.5

glyceraldehyde + NAD(P)+ + H2O = glycerate + NAD(P)H + H+

654425

-

1.2.1.5

glyceraldehyde + NAD+ + H2O = glycerate + NADH + H+

348794

-

1.2.1.5

3 entries

1.2.1.69

DL-glyceraldehyde + NAD+ + H2O = DL-glycerate + NADH + H+

636460

-

1.2.1.8

DL-glyceraldehyde + NAD+ + H2O = glycerate + NADH + H+

656550

-

1.2.1.8

DL-glyceraldehyde + NADP+ + H2O = glycerate + NADPH + H+

656550

-

1.2.1.8

glyceraldehyde + NAD+ + H2O = glycerate + NADH

390352

-

1.2.1.8

3 entries

1.2.1.89

glyceraldehyde + NAD+ + H2O = glycerate + NADH + H+

736023

-

1.2.3.1

DL-glyceraldehyde + H2O + O2 = DL-glycerate + H2O2

656311, 654321

-

1.2.3.1

DL-glyceraldehyde + O2 + H2O = glycerate + H2O2

644705

-

1.2.3.1

glyceraldehyde + H2O + O2 = 2,3-dihydroxypropanoic acid + H2O2

390396

-

1.2.3.1

3 entries

1.2.3.15

DL-glyceraldehyde + H2O + O2 = ?

739561, 738490

-

1.2.7.5

glyceraldehyde + H2O + 2 oxidized benzyl viologen = glycerate + 2 H+ + 2 reduced benzyl viologen

763075

-

1.2.7.5

glyceraldehyde + H2O + oxidized ferredoxin = glycerate + H+ + reduced ferredoxin

11938, 763266

-

1.2.7.5

glyceraldehyde + H2O + oxidized methyl viologen = glycerate + H+ + reduced methyl viologen

11938, 11935

-

1.2.7.5

3 entries

1.2.7.6

glyceraldehyde + H2O + oxidized ferredoxin = glycerate + H+ + reduced ferredoxin

763266

-

1.2.99.6

DL-glyceraldehyde + benzyl viologen = alpha,beta-dihydroxypropionic acid + reduced benzyl viologen

655482

-

1.2.99.6

Glyceraldehyde + benzyl viologen = Glycerate + reduced benzyl viologen

11935

-

1.2.99.6

Glyceraldehyde + methyl viologen = Glycerate + reduced methyl viologen

11938

-

1.2.99.6

3 entries

1.2.99.8

DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O = glycerate + reduced 2,6-dichlorophenolindophenol

719397

-

1.3.1.20

DL-glyceraldehyde + NADPH = ?

349240

-

2.2.1.1

DL-glyceraldehyde + ? = ?

486023

-

2.2.1.1

DL-glyceraldehyde + hydroxypyruvate = ? + CO2

735415

-

2.2.1.1

2 entries

2.2.1.2

dihydroxypropanone + DL-glyceraldehyde = D-fructose

719298

-

2.6.1.18

5-aminopentanoate + glyceraldehyde = 5-oxopentanoate + 1-amino-2,3-dihydroxypropane

737507

-

2.6.1.18

6-aminohexanoate + glyceraldehyde = 6-oxohexanoate + 1-amino-2,3-dihydroxypropane

737507

-

2.6.1.18

7-aminoheptanoate + glyceraldehyde = 7-oxoheptanoate + 1-amino-2,3-dihydroxypropane

737507

-

2.6.1.18

8-aminooctanoate + glyceraldehyde = 8-oxooctanoate + 1-amino-2,3-dihydroxypropane

737507

-

2.6.1.18

4 entries

2.6.1.62

2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine = ?

758685

-

2.7.1.28

ATP + glyceraldehyde = ADP + D-glyceraldehyde-3-phosphate

641262, 641261

-

2.7.1.29

ATP + DL-glyceraldehyde = ADP + DL-glyceraldehyde 3-phosphate

658036

-

2.7.1.29

ATP + DL-glyceraldehyde = ADP + glyceraldehyde 3-phosphate

641267, 641268

-

2.7.1.29

phosphoenolpyruvate + DL-glyceraldehyde = pyruvate + DL-glyceraldehyde 3-phosphate

658036

-

2.7.1.29

phospho-DhaM + glyceraldehyde = dephospho-DhaM + glyceraldehyde 2-phosphate

641272

-

2.7.1.29

4 entries

4.1.1.74

glyceraldehyde = ?

651291

-

4.1.2.17

dihydroxyacetone phosphate + DL-glyceraldehyde = L-tagatose 1-phosphate

727377

-

4.1.2.17

DL-glycerol 3-phosphate + DL-glyceraldehyde = D-psicose 1-phosphate

727377

-

4.1.2.17

glycerone phosphate + DL-glyceraldehyde = ?

652766

-

4.1.2.17

3 entries

4.1.2.20

pyruvate + glyceraldehyde = ?

716878

-

4.1.2.43

D-ribulose 5-phosphate + DL-glyceraldehyde = ?

690565

-

4.1.2.52

pyruvate + DL-glyceraldehyde = ?

702377

-

4.1.3.39

pyruvate + (R,S)-glyceraldehyde = ?

702377

-

Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

glycerol + NADP+ = DL-glyceraldehyde + NADPH + H+

0

-

1.1.1.202

glycerol + NAD+ = glyceraldehyde + NADH + H+

0

-

1.1.1.406

glycerol + NAD+ = DL-glyceraldehyde + NADH

389404

-

1.1.1.6

glycerol + NADP+ = glyceraldehyde + NADPH + H+

0

-

1.1.1.71

glycerol + NADP+ = glyceraldehyde + NADPH + H+

0

-

1.1.1.77

glycerol + NAD+ = DL-glyceraldehyde + NADH

0

-

1.1.3.13

glycerol + O2 = glyceraldehyde + H2O2

0

-

1.1.3.41

glycerol + O2 = glyceraldehyde + H2O2

0

-

1.1.3.B4

glycerol + O2 = glyceraldehyde + H2O2

0

-

1.1.9.1

glycerol + ferrocyanide = 2,3-dihydroxypropanal + ferricyanide

0

-

3.1.3.18

glyceraldehyde-3-phosphate + H2O = glyceraldehyde + phosphate

0

-

3.1.3.2

glyceraldehyde 3-phosphate + H2O = glyceraldehyde + phosphate

0

-

4.1.2.20

2-dehydro-3-deoxy-D-gluconate = pyruvate + glyceraldehyde

0

-

4.1.2.4

D-2-deoxyribose = glyceraldehyde + acetaldehyde

650530

-

4.1.2.4

L-Glyceraldehyde 3-phosphate + acetaldehyde = Glyceraldehyde + acetaldehyde

0

-

4.1.2.4

2 entries

4.3.1.9

D-glucosaminate = pyruvate + glyceraldehyde + NH3

650409

-

Inhibitor in Enzyme-catalyzed Reactions (15 results)

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Show Inhibitors (15 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.21

substrate inhibition

286243, 286250

-

1.2.1.22

substrate inhibition

288133

-

1.2.1.3

substrate inhibition

348721

-

1.2.1.47

1 mM causes 7% inhibition at 30°C

691376

-

1.2.1.8

-

390346

-

1.2.1.8

100 mM, 83% inhibition

390329

-

1.2.1.8

2 entries

1.2.1.9

competitive

657096

-

2.7.1.19

non competitive, 10 mM

641027

-

2.7.1.29

competitive

658036

-

4.1.2.17

-

727377

-

4.1.2.43

13% inhibition at 4 mM

691118

-

4.1.3.3

0% residual activity at 10 mM

33332

-

4.2.1.130

about 60% inhibition at 10 mM

740433

-

5.1.3.3

-

2364

-

6.3.2.26

-

440078

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (40 results)

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Show Turnover Number (40 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.10

0.52

-

pH 7.0, 25°C

656049

1.1.1.10

20

-

pH 7.0, 25°C

656049

1.1.1.10

21

-

pH 7.0, 25°C

656049

1.1.1.10

22

-

pH 7.0, 25°C

656049

1.1.1.10

24

-

pH 7.0, 25°C

656049

1.1.1.10

5 entries

1.1.1.149

0.215

-

+/-0.3

286001

1.1.1.21

-999

-

turnover number in mol per seconds for several mutants

286254

1.1.1.21

0.09

-

pH 7.0, 25°C, recombinant mutant W219E

667807

1.1.1.21

0.16

-

pH 7.0, 25°C, recombinant mutant R293A

667807

1.1.1.21

0.32

-

pH 7.0, 25°C, recombinant mutant W219A

667807

1.1.1.21

0.38

-

pH 7.0, 25°C, recombinant mutant R268A

667807

1.1.1.21

0.431

-

-

286221

1.1.1.21

0.5

-

pH 7.0, 25°C, recombinant wild-type enzyme

667807

1.1.1.21

0.54

-

pH 7.0, 25°C, recombinant mutant S226A

667807

1.1.1.21

0.583

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.21

0.673

-

recombinant from baculovirus system in Spodoptera frugiperda cells

286262

1.1.1.21

0.76

-

pH 6.2, 25°C, recombinant enzyme

667553

1.1.1.21

2

-

pH 7.0, 25°C, recombinant mutant S210A

667807

1.1.1.21

2.1

-

pH 7.0, 25°C, recombinant mutant S214A

667807

1.1.1.21

2.15

-

pH 7.0, 25°C, recombinant mutant DELTA214-219

667807

1.1.1.21

3.7

-

pH 7.0, 25°C, recombinant mutant G213S

667807

1.1.1.21

4

-

pH 7.0, 25°C, recombinant mutant C298A

667807

1.1.1.21

4.6

-

pH 7.0, 25°C, recombinant mutant G213P

667807

1.1.1.21

5.8

-

pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme

739042

1.1.1.21

155

-

-

286258

1.1.1.21

19 entries

1.1.1.283

0.52

-

1 mM

670170

1.1.1.430

14.1

-

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

764945

1.1.1.431

24.3

-

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

764945

1.2.1.12

4.35

-

recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C

688953

1.2.1.26

4.8

-

pH 7.5, 70°C

719837

1.2.1.3

0.92

-

in 50 mM Tris/HCl, at pH 8.0 and 80°C

722210

1.2.1.3

1.29

-

-

348708

1.2.1.4

1.2

-

at pH 8.8 and 60°C

739966

1.2.1.4

1.35

-

pH 8.4, 28°C, cosubstrate NADP+

723749

1.2.1.3

2 entries

1.2.1.4

2 entries

1.2.7.5

2.8

-

pH 8.4, 45°C, benzyl viologen as electron acceptor

11935

1.2.99.6

10.5

-

with benzyl viologen as cosubstrate, at 45°C

11935

2.2.1.2

0.54

-

mutant F178, pH 8.5, 30°C

719298

2.7.1.29

5.17

-

pH 7.5, 30°C

658036

4.1.2.52

5.6

-

Kcat(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C

702377

4.1.3.39

5.6

-

pH 8.0, 25°C

702377

K_M Value (128 results)

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Show KM Value (128 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.10

1.2

-

pH 7.0, 25°C

656049

1.1.1.10

1.4

-

pH 7.0, 25°C

656049

1.1.1.10

2.7

-

pH 7.0, 25°C

656049

1.1.1.10

5.1

-

pH 7.0, 25°C

656049

1.1.1.10

6

-

pH 7.0, 25°C

656049

1.1.1.10

5 entries

1.1.1.149

120

-

-

286001

1.1.1.185

0.026

-

enzyme form of pI 7.2, at pH 7.0 and 25°C

286134

1.1.1.185

0.026

-

pI 7.2 form

286134

1.1.1.185

0.029

-

enzyme form of pI 6.2, at pH 7.0 and 25°C

286134

1.1.1.185

0.029

-

pI 6.2 form

286134

1.1.1.185

0.566

-

enzyme form of pI 4.8, at pH 7.0 and 25°C

286134

1.1.1.185

0.566

-

pI 4.8 form

286134

1.1.1.188

0.143

-

-

389454

1.1.1.188

0.143

-

37°C, liver-type isozyme

389454

1.1.1.185

6 entries

1.1.1.188

2 entries

1.1.1.189

0.83

-

-

389468

1.1.1.19

1.671

-

-

286143

1.1.1.2

0.07

-

aldehyde reductase I, at pH 7.3 and 37°C

286187

1.1.1.2

0.07

-

AR I

286187

1.1.1.2

1.3

-

-

286174

1.1.1.2

1.5

-

-

286168, 286175

1.1.1.2

1.7

-

wild type enzyme, at pH 7.0 and 25°C

286199, 286200

1.1.1.2

1.7

-

wild-type aldehyde reductase

286199, 286200

1.1.1.2

1.8

-

aldehyde reductase, mutant V299C

286199

1.1.1.2

1.8

-

mutant enzyme V299C, at pH 7.0 and 25°C

286199

1.1.1.2

2.2

-

aldehyde reductase, mutant R311A

286200

1.1.1.2

2.2

-

mutant enzyme R311A, at pH 7.0 and 25°C

286200

1.1.1.2

2.3

-

aldehyde reductase, mutant R308A

286200

1.1.1.2

2.3

-

mutant enzyme R308A, at pH 7.0 and 25°C

286200

1.1.1.2

2.94

-

aldehyde reductase II

286181

1.1.1.2

2.94

-

aldehyde reductase II, at pH 7.0 and 37°C

286181

1.1.1.2

4.67

-

enzyme from inner medulla, at pH 6.2 and 25°C

286196

1.1.1.2

4.67

-

inner medulla enzyme

286196

1.1.1.2

4.68

-

cortex enzyme

286196

1.1.1.2

4.68

-

enzyme from brain cortex, at pH 6.2 and 25°C

286196

1.1.1.2

5.92

-

enzyme from outer medulla, at pH 6.2 and 25°C

286196

1.1.1.2

5.92

-

outer medulla enzyme

286196

1.1.1.2

6.67

-

aldehyde reductase II, at pH 7.0 and 37°C

286187

1.1.1.2

6.67

-

AR II

286187

1.1.1.2

7.59

-

aldehyde reductase II

286186

1.1.1.2

8.35

-

-

286192

1.1.1.2

11.5

-

aldehyde reductase, mutant I298C

286199

1.1.1.2

11.5

-

mutant enzyme I298C, at pH 7.0 and 25°C

286199

1.1.1.2

12.5

-

aldehyde reductase I

286181

1.1.1.2

12.5

-

aldehyde reductase I, at pH 7.3 and 37°C

286181

1.1.1.2

33

-

aldehyde reductase, mutant I298A

286199

1.1.1.2

33

-

mutant enzyme I298A, at pH 7.0 and 25°C

286199

1.1.1.2

76

-

aldehyde reductase, mutant H112Q

286199

1.1.1.2

76

-

mutant enzyme H112Q, at pH 7.0 and 25°C

286199

1.1.1.202

26

-

-

389498

1.1.1.202

29

-

-

389498

1.1.1.21

0.02

-

-

286254

1.1.1.21

0.02

-

pH 7.0, 25°C, recombinant mutant R293A

667807

1.1.1.21

0.02

-

pH 7.0, 25°C, recombinant mutant W219A

667807

1.1.1.21

0.02

-

pH 7.0, 25°C, recombinant mutant W219E

667807

1.1.1.21

0.02

-

pH 7.0, 25°C, recombinant wild-type enzyme

667807

1.1.1.21

0.025

-

-

286221, 286241

1.1.1.21

0.03

-

-

286247

1.1.1.21

0.03

-

pH 7.0, 25°C, recombinant mutant S226A

667807

1.1.1.21

0.046

-

-

286261

1.1.1.21

0.047

-

recombinant from E. coli

286261

1.1.1.21

0.05

-

pH 7.0, 25°C, recombinant mutant R268A

667807

1.1.1.21

0.071

-

pH 6.0, 25°C, healthy heart

669455

1.1.1.21

0.08

-

-

286261

1.1.1.21

0.0835

-

pH 6.0, 25°C, ischemic heart

669455

1.1.1.21

0.0836

-

pH 6.0, 25°C, healthy heart, in presence of DTT

669455

1.1.1.21

0.092

-

pH 6.2, 25°C, recombinant enzyme

667553

1.1.1.21

0.0934

-

pH 6.0, 25°C, ischemic heart, in presence of DTT

669455

1.1.1.21

0.0973

-

presence of peroxynitrite, pH 7.0, 37°C

669455

1.1.1.21

0.11

-

pH 7.0, 25°C, recombinant mutant S210A

667807

1.1.1.21

0.12

-

recombinant from E. coli

286261

1.1.1.21

0.124

-

pH 7.0, 37°C

669455

1.1.1.21

0.13

-

pH 7.0, 25°C, recombinant mutant S214A

667807

1.1.1.21

0.1734

-

presence of dimedone, pH 7.0, 37°C

669455

1.1.1.21

0.19

-

pH 6.2, 25°C, enzyme from ischemic heart

655525

1.1.1.21

0.2

-

pH 6.2, 25°C, enzyme from normal heart

655525

1.1.1.21

0.42

-

pH 7.0, 25°C, recombinant mutant G213S

667807

1.1.1.21

0.4287

-

presence of peroxynitrite and dimedone, pH 7.0, 37°C

669455

1.1.1.21

0.5

-

pH 7.0, 25°C, recombinant mutant DELTA214-219

667807

1.1.1.21

0.51

-

-

286186

1.1.1.21

0.585

-

isoform ALR2, pH 6.2, 30°C

685547

1.1.1.21

0.6

-

pH 7.0, 25°C, recombinant mutant C298A

667807

1.1.1.21

1.1

-

pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme

739042

1.1.1.21

2

-

-

286258

1.1.1.21

2

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.21

3.4

-

-

286238

1.1.1.21

3.7

-

pH 7.0, 25°C, recombinant mutant G213P

667807

1.1.1.21

4

-

in 50 mM sodium phosphate at pH 7.0 and 30°C

700796

1.1.1.21

6

-

pH 7.0, 25°C, recombinant detagged enzyme

738031

1.1.1.21

12

-

mutant H110Q

286254

1.1.1.21

64

-

mutant Y48S

286254

1.1.1.21

71

-

mutant Y48H

286254

1.1.1.21

84

-

mutant H110A

286254

1.1.1.21

730.2

-

-

286255

1.1.1.2

32 entries

1.1.1.202

2 entries

1.1.1.21

43 entries

1.1.1.283

0.56

-

1 mM

670170

1.1.1.365

6

-

in 100 mM sodium phosphate (pH 7.0), at 22°C

724270

1.1.1.430

2.43

-

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

764945

1.1.1.431

1.14

-

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

764945

1.1.3.9

7.5

-

-

687852

1.2.1.12

0.1

-

enzyme form E8.5, pH 7

287913

1.2.1.12

0.2

-

recombinant enzyme, at 25°C

688953

1.2.1.3

0.17

-

D-glyceraldehyde, L-glyceraldehyde, DL-glyceraldehyde

348723

1.2.1.3

0.205

-

-

348683

1.2.1.3

0.39

-

-

348708

1.2.1.3

0.595

-

wild type isoform ALDH1A1, in 100 mM sodium diphosphate (pH 9.5), at 25°C

726464

1.2.1.3

7.374

-

pH and temperature not specified in the publication

712435

1.2.1.3

8.51

-

in 50 mM Tris/HCl, at pH 8.0 and 80°C

722210

1.2.1.4

0.65

-

pH 8.4, 28°C, cosubstrate NADP+

723749

1.2.1.4

15

-

at pH 8.8 and 60°C

739966

1.2.1.8

11

-

pH 7.7, coenzyme NADP+

656550

1.2.1.8

48

-

pH 7.7, coenzyme NAD+

656550

1.2.1.12

2 entries

1.2.1.3

6 entries

1.2.1.4

2 entries

1.2.1.8

2 entries

1.2.3.1

0.31

-

37°C, pH 7.0

644705

1.2.7.5

0.2

-

pH 8.4, 45°C, benzyl viologen as electron acceptor

11935

1.2.7.5

1

-

pH 8.4, 65°C, with methyl viologen as electron acceptor

11938

1.2.99.6

0.016

-

-

655482

1.2.99.6

0.196

-

with benzyl viologen as cosubstrate, at 45°C

11935

1.2.7.5

2 entries

1.2.99.6

2 entries

1.2.99.8

0.09

-

80°C, pH 6.7

719397

2.2.1.1

10

-

-

486023

2.2.1.2

120

-

mutant F178, pH 8.5, 30°C

719298

2.7.1.28

0.01

-

pH 7.0, 22°C

641262

2.7.1.29

0.024

-

pH 7.5, 30°C

641268

2.7.1.29

0.18

-

pH 7.5, 30°C

658036

2.7.1.29

2 entries

4.1.1.74

0.042

-

70°C, pH 8.0

651291

4.1.2.17

0.743

-

pH not specified in the publication, temperature not specified in the publication

727377

4.1.2.17

7.8

-

wild-type

652766

4.1.2.17

8.2

-

N25T mutant

652766

4.1.2.17

23.1

-

N25L mutant

652766

4.1.2.17

4 entries

4.1.2.52

88.6

-

Km(app) with pyruvate as carbonyl donor, pH 8.0 and 25°C

702377

4.1.3.39

88.6

-

pH 8.0, 25°C

702377

K_i Value (6 results)

top print hide

Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.8

7.4

-

-

390329

1.2.1.9

1.05

-

-

657096

2.7.1.19

19

20

pH 7.9, 20°C

641027

2.7.1.29

0.15

-

pH 7.5, 30°C

658036

2.7.1.29

0.6

-

pH 7.5, 30°C

658036

2.7.1.29

2 entries

4.1.2.17

0.01

-

direction of aldol condensation, pH not specified in the publication, temperature not specified in the publication

727377

References & Links

Literature References (190)

top print hide

Show Reference (190 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2364

4945113

The enzymatically catalyzed mutarotation. The mechanism of action of mutarotase (aldose 1-epimerase) from Escherichia coli

1971

Hucho, F.; Wallenfels, K.

Eur. J. Biochem.

23

489-496

10900

3745122

Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production

1986

Zachariou, M.; Scopes, R.K.

J. Bacteriol.

167

863-869

11935

7642503

Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1

1995

Heider, J.; Ma, K.; Adams, M.W.W.

J. Bacteriol.

177

4757-4764

11938

1907273

The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway

1991

Mukund, S.; Adams, M.W.W.

J. Biol. Chem.

266

14208-14216

33332

1646603

Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli

1991

Aisaka, K.; Igarashi, A.; Yamaguchi, K.; Uwajima, T.

Biochem. J.

276

541-546

207968

14323585

The metabolism of lactaldehyde: VII. The oxidation of D-lactaldehyde in rat liver

1965

Ting, S.M.; Miller, O.N.; Sellinger, O.Z.

Biochim. Biophys. Acta

97

407-415

207969

6386056

Purification and partial characterization of a methylglyoxal reductase from goat liver

1984

Ray, M.; Ray, S.

Biochim. Biophys. Acta

802

119-127

207975

-

Purification and partial characterization of NADH-dependent methylglyoxal-reducing enzyme from porcine liver

1988

Kato, H.; Miyauchi, Y.; Nishimura, T.; Liang, Z.Q.

Agric. Biol. Chem.

52

2641-2642

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

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

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

286134

7018582

Purification and some properties of L-glycol dehydrogenase from hens muscle

1981

Bernardo, A.; Burgos, J.; Martin, R.

Biochim. Biophys. Acta

659

189-198

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

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

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

286181

6753936

Purification and properties of human liver aldehyde reductases

1982

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

Biochim. Biophys. Acta

707

105-114

286186

3922304

Purification and properties of aldose reductase and aldehyde reductase II from human erythrocyte

1985

Das, B.; Srivastava, S.K.

Arch. Biochem. Biophys.

238

670-679

286187

3890957

Purification and properties of aldehyde reductases from human placenta

1985

Das, B.; Srivastava, S.K.

Biochim. Biophys. Acta

840

324-333

286192

2500152

Characterization of aldose reductase and aldehyde reductase from rat testis

1989

Kawasaki, N.; Tanimoto, T.; Tanaka, A.

Biochim. Biophys. Acta

996

30-36

286196

1907200

Localization, isolation and properties of three NADPH-dependent aldehyde reducing enzymes from dog kidney

1991

Ohta, M.; Tanimoto, T.; Tanaka, A.

Biochim. Biophys. Acta

1078

395-403

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

286221

1901806

Purification and characterization of human testis aldose and aldehyde reductase

1991

Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.

Int. J. Biochem.

23

421-428

286222

6706910

Enzymatic determination of free glucoronic acid with glucuronolactone reductase. I. isolation and purification of glucoronolactone reductase from rat kidney

1984

Hayashi, S.; Watanabe, M.; Kimura, A.

J. Biochem.

95

223-232

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

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

286243

4458

Physical and kinetic properties of homogenous bovine lens aldose reductase

1976

Sheaff, C.M.; Doughty, C.C.

J. Biol. Chem.

251

2696-2702

286247

14275148

Isolation and properties of lens aldose reductase

1965

Hayman, S.; Kinoshita, J.H.

J. Biol. Chem.

240

877-882

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

286255

12223702

Characterization and purification of an aldose from the acidophilic and thermophilic red algae Galdiera sulphuraria

1997

Gross, W.; Seipold, P.; Schnarrenberger, C.

Plant Physiol.

114

231-236

286256

7626055

Alpha-crystallin-like molecular chaperone against the thermal denaturation of lens aldose reductase: the effect of divalent metal ions

1995

Marini, I.; Bucchioni, L.; Voltarelli, M.; Del Corso, A.; Mura, U.

Biochem. Biophys. Res. Commun.

212

413-420

286258

11306077

Structural and functional properties of alsode xylose reductase from the D-xylose-metabolizing Candida tenuis

2001

Nidetzky, B.; Mayr, P.; Neuhauser, W.; Puchberger, M.

Chem. Biol. Interact.

130-132

583-595

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

286261

7484387

Purification and characterization of recombinant human placental and rat lens aldose reductases expressed in Escherichia coli

1995

Sato, S.; Old, S.; Carper, D.; Kador, P.F.

Adv. Exp. Med. Biol.

5

259-268

286262

1905957

Purification and characterization of the recombinant human aldose reductase expressed in baculovirus system

1991

Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera, T.; Tanimoto, T.

Biochim. Biophys. Acta

1078

171-178

286263

7961617

Purification and properties of six aldo-keto reductases from rat adrenal gland

1994

Inazu, N.; Nagashima, Y.; Satoh, T.; Fujii, T.

J. Biochem.

115

991-999

287728

27392874

Isolation and Characterization of a 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

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

288133

3308886

Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12

1987

Baldoma, L.; Aguilar, J.

J. Biol. Chem.

262

13991-13996

348683

224930

Purification and partial characterization of aldehyde dehydrogenase from human erythrocytes

1979

Inoue, K.; Nishimukai, H.; Yamasawa, K.

Biochim. Biophys. Acta

569

117-123

348700

2719636

Purification of aldehyde dehydrogenase from rat liver mitochondria by alpha-cyanocinnamate affinity chromatography

1989

Poole, R.C.; Halestrap, A.P.

Biochem. J.

259

105-110

348702

2930466

Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase

1989

Kitson, T.M.

Biochem. J.

257

573-578

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

348708

6651766

Bovine lens aldehyde dehydrogenase. Kinetics and mechanism

1983

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

Biochem. J.

215

361-368

348721

170276

Human liver aldehyde dehydrogenase. Kinetics of aldehyde oxidation

1975

Sidhu, R.S.; Blair, A.H.

J. Biol. Chem.

250

7899-7904

348723

627210

Purification and characterization of aldehyde dehydrogenase from bovine liver

1978

Leicht, W.; Heinz, F.; Freimueller, B.

Eur. J. Biochem.

83

189-196

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

349240

2690827

Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities

1989

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

Biochem. J.

264

403-407

389404

7551050

Enzyme evolution in Rhodobacter sphaeroides: Selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme

1995

Schneider, K.H.; Jäkel, G.; Hoffmann, R.; Giffhorn, F.

Microbiology

141

1865-1873

389454

1605628

Purification and characterization of prostaglandin F synthase from bovine liver

1992

Chen, L.Y.; Watanabe, K.; Hayaishi, O.

Arch. Biochem. Biophys.

296

17-26

389468

8529651

Prostaglandin-E2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20.alpha-hydroxysteroid dehydrogenase activity

1995

Wintergalen, N.; Thole, H.H.; Galla, H.J.; Schlegel, W.

Eur. J. Biochem.

234

264-270

389498

1622279

1,3-Propanediol:NAD+ oxidoreductases of Lactobacillus brevis and Lactobacillus buchneri

1992

Veiga-da-Cunha, M.; Foster, M.A.

Appl. Environ. Microbiol.

58

2005-2010

390211

-

Glycoladehyde dehydrogenase, an enzyme related to vitamin B6 biosynthesis, from Bacillus subtilis

1979

Morita, H.; Yamamoto, K.; Tani, Y.; Ogata, K.; Yamada, H.

Agric. Biol. Chem.

43

317-323

390329

2194570

Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli

1990

Falkenberg, P.; Strom, A.R.

Biochim. Biophys. Acta

1034

253-259

390346

13192104

The oxidation of betaine aldehyde be betaine aldehyde dehydrogenase

1954

Rothschild, H.A.; Barron, E.S.

J. Biol. Chem.

209

511-523

390352

9734333

Porcine kidney betaine aldehyde dehydrogenase: purification and properties

1998

Guzman-Partida, A.M.; Valenzuela-Soto, E.M.

Comp. Biochem. Physiol. B

119

485-491

390396

4051501

Guinea pig liver aldehyde oxidase as a sulfoxide reductase: its purification and characterization

1985

Yoshihara, S.; Tatsumi, K.

Arch. Biochem. Biophys.

242

213-224

437834

-

Purification and properties of five NADP-dependent aldehyde dehydrogenases from Acetobacter aceti

1980

Muraoka, H.; Watabe, Y.; Ogasawara, N.; Takahashi, H.

J. Ferment. Technol.

58

501-507

440078

-

Regulation of ACV synthetase activity in the beta-lactam biosynthetic pathway by carbon sources and their metabolites

1992

Zhang, J.; Demain, A.L.

Arch. Microbiol.

158

364-369

486023

7607225

Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains

1995

Sprenger, G.A.; Schoerken, U.; Sprenger, G.; Sahm, H.

Eur. J. Biochem.

230

525-532

636283

-

Purification and properties of glycerol:NAD+ 2-oxidoreductase (glycerol dehydrogenase) from Schizosaccharomyces pombe

1985

Marshall, J.H.; May, J.W.; Sloan, J.

J. Gen. Microbiol.

131

1581-1588

636285

-

Purification and properties of glycerol dehydrogenase from Candida valida

1984

Gärtner, G.; Kopperschläger, G.

J. Gen. Microbiol.

130

3225-3233

636289

-

Glycerol dehydrogenase from Cellulomonas sp. NT 3060: purification and characterization

1982

Yamada H.; Nagao, A.; Nishise, H.; Tani, Y.

Agric. Biol. Chem.

46

2333-2339

636294

-

Glycerol dehydrogenase from Aerobacter aerogenes

1955

Burton, R.M.

Methods Enzymol.

1

397-400

636297

11412332

Separation and characterization of the 1,3-propanediol and glycerol dehydrogenase activities from Clostridium butyricum E5 wild-type and mutant D

2001

Malaoui, H.; Marczak, R.

J. Appl. Microbiol.

90

1006-1014

636460

11571203

Isolation of an aldehyde dehydrogenase involved in the oxidation of fluoroacetaldehyde to fluoroacetate in Streptomyces cattleya

2001

Murphy, C.D.; Moss, S.J.; O'Hagan, D.

Appl. Environ. Microbiol.

67

4919-4921

641027

182116

Inhibition of spinach phosphoribulokinase by DL-glyceraldehyde

1976

Slabas, A.R.; Walker, D.A.

Biochem. J.

153

613-619

641261

13093749

Le metabolisme du fructose-1-phosphate dans le foie

1953

Hers, H.G.; Kusaka, T.

Biochim. Biophys. Acta

11

427-437

641262

5823111

Enzymes involved in fructose metabolism in lir and the glyceraldehyde metabolic crossroads

1969

Sillero, M.A.G.; Sols, A.

Eur. J. Biochem.

10

345-350

641267

2177824

Triokinase from Candida boidinii KD1

1990

Bystrykh, L.V.; de Koning, W.; Harder, W.

Methods Enzymol.

188

445-451

641268

2177825

Glycerone kinase from Candida methylica

1990

Hofmann, K.H.; Babel, W.

Methods Enzymol.

188

451-455

641272

12813127

A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase

2003

Siebold, C.; Garcia-Alles, L.F.; Erni, B.; Baumann, U.

Proc. Natl. Acad. Sci. USA

100

8188-8192

644705

14659539

Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690

2003

Uchida, H.; Kondo, D.; Yamashita, A.; Nagaosa, Y.; Sakurai, T.; Fujii, Y.; Fujishiro, K.; Aisaka, K.; Uwajima, T.

FEMS Microbiol. Lett.

229

31-36

650409

12686150

The D-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens exhibits thioredoxin reductase activity

2003

Iwamoto, R.; Amano, C.; Ikehara, K.; Ushida, N.

Biochim. Biophys. Acta

1647

310-314

650530

12467706

Structure-based mutagenesis approaches toward expanding the substrate specificity of D-2-deoxyribose-5-phosphate aldolase

2003

DeSantis, G.; Liu, J.; Clark, D.P.; Heine, A.; Wilson, I.A.; Wong, C.H.

Bioorg. Med. Chem.

11

43-52

651291

11801253

A novel bifunctional molybdo-enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. strain 7

2002

Wakagi, T.; Fukuda, E.; Ogawa, Y.; Kino, H.; Matsuzawa, H.

FEBS Lett.

510

196-200

652766

-

Mutagenic characterization of a conserved functional amino acid in fuculose-1-phosphate aldolase from Methanococcus jannaschii, a hyperthermophilic archaea

2001

Yoon, H.S.; Kwon, S.J.; Han, M.S.; Yu, Y.G.; Yoon, M.Y.

J. Microbiol. Biotechnol.

11

709-711

654321

15657722

Characterization and potential application of purified aldehyde oxidase from Pseudomonas stutzeri IFO12695

2005

Uchida, H.; Fukuda, T.; Satoh, Y.; Okamura, Y.; Toriyama, A.; Yamashita, A.; Aisaka, K.; Sakurai, T.; Nagaosa, Y.; Uwajima, T.

Appl. Microbiol. Biotechnol.

68

53-56

654425

12419301

Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties

2002

Yamanaka, Y.; Kazuoka, T.; Yoshida, M.; Yamanaka, K.; Oikawa, T.; Soda, K.

Biochem. Biophys. Res. Commun.

298

632-637

655482

14686934

Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum. Isolation, characterization and molecular analysis

2004

Rauh, D.; Graentzdoerffer, A.; Granderath, K.; Andreesen, J.R.; Pich, A.

Eur. J. Biochem.

271

212-219

655525

11772943

Aldose reductase activation is a key component of myocardial response to ischemia

2002

Hwang, Y.C.; Sato, S.; Tsai, J.Y.; Yan, S.; Bakr, S.; Zhang, H.; Oates, P.J.; Ramasamy, R.

FASEB J.

16

243-245

656049

11882650

Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney

2002

Nakagawa, J.; Ishikura, S.; Asami, J.; Isaji, T.; Usami, N.; Hara, A.; Sakurai, T.; Tsuritani, K.; Oda, K.; Takahashi, M.; Yoshimoto, M.; Otsuka, N.; Kitamura, K.

J. Biol. Chem.

277

17888-17891

656311

16233281

Production of aldehyde oxidases by microorganisms and their enzymatic properties

2002

Yasuhara, A.; Akiba-Goto, M.; Fujishiro, K.; Uchida, H.; Uwajima, T.; Aisaka, K.

J. Biosci. Bioeng.

94

124-129

656550

15381418

Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase

2004

Gruez, A.; Roig-Zamboni, V.; Grisel, S.; Salomoni, A.; Valencia, C.; Campanacci, V.; Tegoni, M.; Cambillau, C.

J. Mol. Biol.

343

29-41

656571

-

Paradoxical thermostable enzymes from psychrophile: molecular characterization and potentiality for biotechnological application

2003

Oikawa, T.; Kazuoka, T.; Soda, K.

J. Mol. Catal. B

23

65-70

657096

-

On the interaction of substrate analogues with non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves

2002

Iglesias, A.A.; Vicario, L.R.; Gomez-Casati, D.F.; Sesma, J.I.; Gomez-Casati, M.E.; Bustos, D.M.; Podesta, F.E.

Plant Sci.

162

689-696

658036

15476397

Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism

2004

Garcia-Alles, L.F.; Siebold, C.; Nyffeler, T.L.; Flukiger-Bruhwiler, K.; Schneider, P.; Burgi, H.B.; Baumann, U.; Erni, B.

Biochemistry

43

13037-13045

659210

12670960

Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans

2003

Leimkuhler, S.; Hodson, R.; George, G.N.; Rajagopalan, K.V.

J. Biol. Chem.

278

20802-20811

667224

15998238

Zofenoprilat-glutathione mixed disulfide as a specific S-thiolating agent of bovine lens aldose reductase

2005

Dal Monte, M.; Del Corso, A.; Moschini, R.; Cappiello, M.; Amodeo, P.; Mura, U.

Antioxid. Redox Signal.

7

841-848

667266

16391048

Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase uperfamily

2006

Machielsen, R.; Uria, A.R.; Kengen, S.W.; van der Oost, J.

Appl. Environ. Microbiol.

72

233-238

667331

16615933

Chaperone-like activity of alpha-crystallin toward aldose reductase oxidatively stressed by copper ion

2006

Moschini, R.; Marini, I.; Malerba, M.; Cappiello, M.; Del Corso, A.; Mura, U.

Arch. Biochem. Biophys.

453

13-17

667349

16528793

Curcumin analogs as potent aldose reductase inhibitors

2006

Du, Z.Y.; Bao, Y.D.; Liu, Z.; Qiao, W.; Ma, L.; Huang, Z.S.; Gu, L.Q.; Chan, A.S.

Arch. Pharm.

339

123-128

667553

16226225

Fibrates inhibit aldose reductase activity in the forward and reverse reactions

2005

Balendiran, G.K.; Rajkumar, B.

Biochem. Pharmacol.

70

1653-1663

667807

15769597

The structure of Apo R268A human aldose reductase: Hinges and latches that control the kinetic mechanism

2005

Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison, D.H.

Biochim. Biophys. Acta

1748

201-212

667913

17083960

Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes

2006

Brownlee, J.M.; Carlson, E.; Milne, A.C.; Pape, E.; Harrison, D.H.

Bioorg. Chem.

34

424-444

667923

15781392

Structure-activity relationships and molecular modelling of 5-arylidene-2,4-thiazolidinediones active as aldose reductase inhibitors

2005

Maccari, R.; Ottana, R.; Curinga, C.; Vigorita, M.G.; Rakowitz, D.; Steindl, T.; Langer, T.

Bioorg. Med. Chem.

13

2809-2823

667931

16202614

In vitro aldose reductase inhibitory activity of 5-benzyl-2,4-thiazolidinediones

2006

Rakowitz, D.; Maccari, R.; Ottana, R.; Vigorita, M.G.

Bioorg. Med. Chem.

14

567-574

668222

15928807

Phorbol ester up-regulates aldose reductase expression in A549 cells: a potential role for aldose reductase in cell cycle modulation

2005

Kang, E.S.; Kim, H.J.; Paek, K.S.; Jang, H.S.; Chang, K.C.; Lee, J.H.; Nishinaka, T.; Yabe-Nishimura, C.; Seo, H.G.

Cell. Mol. Life Sci.

62

1146-1155

668511

15967436

Regulation of lens aldose reductase activity by nitric oxide

2005

Srivastava, S.; Tammali, R.; Chandra, D.; Greer, D.A.; Ramana, K.V.; Bhatnagar, A.; Srivastava, S.K.

Exp. Eye Res.

81

664-672

669030

16939321

Inhibitory effects of Zingiber officinale Roscoe derived components on aldose reductase activity in vitro and in vivo

2006

Kato, A.; Higuchi, Y.; Goto, H.; Kizu, H.; Okamoto, T.; Asano, N.; Hollinshead, J.; Nash, R.J.; Adachi, I.

J. Agric. Food Chem.

54

6640-6644

669104

16077126

Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases

2005

Ko, J.; Kim, I.; Yoo, S.; Min, B.; Kim, K.; Park, C.

J. Bacteriol.

187

5782-5789

669455

16567803

Redox activation of aldose reductase in the ischemic heart

2006

Kaiserova, K.; Srivastava, S.; Hoetker, J.D.; Awe, S.O.; Tang, X.L.; Cai, J.; Bhatnagar, A.

J. Biol. Chem.

281

15110-15120

669787

16107153

Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity

2005

El-Kabbani, O.; Carbone, V.; Darmanin, C.; Oka, M.; Mitschler, A.; Podjarny, A.; Schulze-Briese, C.; Chung, R.P.

J. Med. Chem.

48

5536-5542

669794

16250648

Naphtho[1,2-d]isothiazole acetic acid derivatives as a novel class of selective aldose reductase inhibitors

2005

Da Settimo, F.; Primofiore, G.; La Motta, C.; Sartini, S.; Taliani, S.; Simorini, F.; Marini, A.M.; Lavecchia, A.; Novellino, E.; Boldrini, E.

J. Med. Chem.

48

6897-6907

670170

16804176

Methylglyoxal detoxification by an aldo-keto reductase in the cyanobacterium Synechococcus sp. PCC 7002

2006

Xu, D.; Liu, X.; Guo, C.; Zhao, J.

Microbiology

152

2013-2021

674270

16585745

Identification of lactaldehyde dehydrogenase in Methanocaldococcus jannaschii and its involvement in production of lactate for F420 biosynthesis

2006

Grochowski, L.L.; Xu, H.; White, R.H.

J. Bacteriol.

188

2836-2844

674654

16835232

A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism

2006

Watanabe, S.; Kodaki, T.; Makino, K.

J. Biol. Chem.

281

28876-28888

684768

17351966

Novel aldose reductase inhibitors derived from 6-[[(diphenylmethylene)amino]oxy]hexanoic acid

2007

Rakowitz, D.; Piccolruaz, G.; Pirker, C.; Matuszczak, B.

Arch. Pharm.

340

202-208

685200

18205401

Electrostatic fields near the active site of human aldose reductase: 1. New inhibitors and vibrational stark effect measurements

2008

Webb, L.J.; Boxer, S.G.

Biochemistry

47

1588-1598

685547

18395454

Carboxymethylated pyridoindole antioxidants as aldose reductase inhibitors: Synthesis, activity, partitioning, and molecular modeling

2008

Stefek, M.; Snirc, V.; Djoubissie, P.O.; Majekova, M.; Demopoulos, V.; Rackova, L.; Bezakova, Z.; Karasu, C.; Carbone, V.; El-Kabbani, O.

Bioorg. Med. Chem.

16

4908-4920

686528

18313804

Synthesis and aldose reductase inhibitory activity of some new chromonyl-2,4-thiazolidinediones

2008

Bozdag-Duendar, O.; Evranos, B.; Das-Evcimen, N.; Sarikaya, M.; Ertan, R.

Eur. J. Med. Chem.

43

2412-2417

687852

17884657

Purification and characterization of a novel alcohol oxidase from Paenibacillus sp. AIU 311

2007

Isobe, K.; Kato, A.; Sasaki, Y.; Suzuki, S.; Kataoka, M.; Ogawa, J.; Iwasaki, A.; Hasegawa, J.; Shimizu, S.

J. Biosci. Bioeng.

104

124-128

688953

17619949

Cloning, gene expression and characterization of a novel bacterial NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Neisseria meningitidis strain Z2491

2007

Fourrat, L.; Iddar, A.; Valverde, F.; Serrano, A.; Soukri, A.

Mol. Cell. Biochem.

305

209-219

689107

17851441

Synthesis and activity of a new series of (Z)-3-phenyl-2-benzoylpropenoic acid derivatives as aldose reductase inhibitors

2007

Wang, S.; Yan, J.; Hao, D.; Niu, X.; Cheng, M.

Molecules

12

885-895

690565

-

Catalytic properties and substrate specificity of 3-hexulose phosphate synthase from Methylomonas M15

1991

Beisswenger, R.; Kula, M.R.

Appl. Microbiol. Biotechnol.

34

604-607

691118

564713

3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics

1978

Kato, N.; Ohashi, H.; Tani, Y.; Ogata, K.

Biochim. Biophys. Acta

523

236-244

691376

18175913

4-N-trimethylaminobutyraldehyde dehydrogenase: purification and characterization of an enzyme from Pseudomonas sp. 13CM

2008

Hassan, M.; Okada, M.; Ichiyanagi, T.; Mori, N.

Biosci. Biotechnol. Biochem.

72

155-162

695864

18782556

Structure of aldehyde reductase in ternary complex with coenzyme and the potent 20alpha-hydroxysteroid dehydrogenase inhibitor 3,5-dichlorosalicylic acid: implications for inhibitor binding and selectivity

2008

Carbone, V.; Chung, R.; Endo, S.; Hara, A.; El-Kabbani, O.

Arch. Biochem. Biophys.

479

82-87

695930

19023536

Inhibitory activities of the alkaloids from Coptidis Rhizoma against aldose reductase

2008

Jung, H.A.; Yoon, N.Y.; Bae, H.J.; Min, B.S.; Choi, J.S.

Arch. Pharm. Res.

31

1405-1412

696073

3921014

Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis

1985

Verduyn, C.; van Kleef, R.; Frank, J.; Schreuder, H.; van Dijken, J.P.; Scheffers, W.A.

Biochem. J.

226

669-677

696552

18670102

Inhibitory effect of the compounds isolated from Rhus verniciflua on aldose reductase and advanced glycation endproducts

2008

Lee, E.H.; Song, D.G.; Lee, J.Y.; Pan, C.H.; Um, B.H.; Jung, S.H.

Biol. Pharm. Bull.

31

1626-1630

696708

18976928

Inhibition of aldose reductase from cataracted eye lenses by finger millet (Eleusine coracana) polyphenols

2008

Chethan, S.; Dharmesh, S.M.; Malleshi, N.G.

Bioorg. Med. Chem.

16

10085-10090

696723

18492610

Synthesis, induced-fit docking investigations, and in vitro aldose reductase inhibitory activity of non-carboxylic acid containing 2,4-thiazolidinedione derivatives

2008

Maccari, R.; Ottana, R.; Ciurleo, R.; Rakowitz, D.; Matuszczak, B.; Laggner, C.; Langer, T.

Bioorg. Med. Chem.

16

5840-5852

696742

19121944

Correlation of binding constants and molecular modelling of inhibitors in the active sites of aldose reductase and aldehyde reductase

2009

Carbone, V.; Zhao, H.T.; Chung, R.; Endo, S.; Hara, A.; El-Kabbani, O.

Bioorg. Med. Chem.

17

1244-1250

697266

18845131

Characterization of a rat NADPH-dependent aldo-keto reductase (AKR1B13) induced by oxidative stress

2009

Endo, S.; Matsunaga, T.; Mamiya, H.; Hara, A.; Kitade, Y.; Tajima, K.; El-Kabbani, O.

Chem. Biol. Interact.

178

151-157

697273

19061876

Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation

2009

Baba, S.P.; Wetzelberger, K.; Hoetker, J.D.; Bhatnagar, A.

Chem. Biol. Interact.

178

250-258

697840

19787414

Gene cloning and characterization of an aldehyde dehydrogenase from long-chain alkane-degrading Geobacillus thermoleovorans B23

2009

Kato, T.; Miyanaga, A.; Kanaya, S.; Morikawa, M.

Extremophiles

14

33-39

699247

19555177

Aldose reductase inhibitors from Litchi chinensis Sonn

2009

Lee, S.J.; Park, W.H.; Park, S.D.; Moon, H.I.

J. Enzyme Inhib. Med. Chem.

24

957-959

699278

-

Purification, characterization and structure analysis of NADPH-dependent D-xylose reductases from Candida tropicalis

1995

Yokoyama, S.-I.; Suzuki, T.; Kawai, K.; Horitsu, H.; Takamizawa, K.

J. Ferment. Bioeng.

79

217-223

699641

19670875

Inhibitors of aldose reductase and formation of advanced glycation end-products in moutan cortex (Paeonia suffruticosa)

2009

Ha, D.T.; Ngoc, T.M.; Lee, I.; Lee, Y.M.; Kim, J.S.; Jung, H.; Lee, S.; Na, M.; Bae, K.

J. Nat. Prod.

72

1465-1470

700796

19056286

Structural and kinetic characterization of a maize aldose reductase

2009

de Sousa, S.M.; Rosselli, L.K.; Kiyota, E.; da Silva, J.C.; Souza, G.H.; Peroni, L.A.; Stach-Machado, D.R.; Eberlin, M.N.; Souza, A.P.; Koch, K.E.; Arruda, P.; Torriani, I.L.; Yunes, J.A.

Plant Physiol. Biochem.

47

98-104

702377

20364820

Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling

2010

Wang, W.; Baker, P.; Seah, S.Y.

Biochemistry

49

3774-3782

711353

20823582

Inhibition of aldose reductase and xylose-induced lens opacity by puerariafuran from the roots of Pueraria lobata

2010

Kim, N.H.; Kim, Y.S.; Lee, Y.M.; Jang, D.S.; Kim, J.S.

Biol. Pharm. Bull.

33

1605-1609

711356

20460778

Aldose reductase inhibitory compounds from Glycyrrhiza uralensis

2010

Lee, Y.S.; Kim, S.H.; Jung, S.H.; Kim, J.K.; Pan, C.H.; Lim, S.S.

Biol. Pharm. Bull.

33

917-921

711458

20452228

Identification of new non-carboxylic acid containing inhibitors of aldose reductase

2010

Maccari, R.; Ciurleo, R.; Giglio, M.; Cappiello, M.; Moschini, R.; Corso, A.D.; Mura, U.; Ottana, R.

Bioorg. Med. Chem.

18

4049-4055

711903

20036445

Structure of aldehyde reductase in ternary complex with a 5-arylidene-2,4-thiazolidinedione aldose reductase inhibitor

2010

Carbone, V.; Giglio, M.; Chung, R.; Huyton, T.; Adams, J.; Maccari, R.; Ottana, R.; Hara, A.; El-Kabbani, O.

Eur. J. Med. Chem.

45

1140-1145

712014

19850041

Inhibition of aldose reductase by dietary antioxidant curcumin: mechanism of inhibition, specificity and significance

2009

Muthenna, P.; Suryanarayana, P.; Gunda, S.K.; Petrash, J.M.; Reddy, G.B.

FEBS Lett.

583

3637-3642

712435

20207735

Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress

2010

Brocker, C.; Lassen, N.; Estey, T.; Pappa, A.; Cantore, M.; Orlova, V.V.; Chavakis, T.; Kavanagh, K.L.; Oppermann, U.; Vasiliou, V.

J. Biol. Chem.

285

18452-18463

712771

20887732

The Three-Dimensional Structure of AKR11B4, a Glycerol Dehydrogenase from Gluconobacter oxydans, Reveals a Tryptophan Residue as an Accelerator of Reaction Turnover

2010

Richter, N.; Breicha, K.; Hummel, W.; Niefind, K.

J. Mol. Biol.

404

353-362

713006

20354121

Inhibition of aldose reductase prevents growth factor-induced G1-S phase transition through the AKT/phosphoinositide 3-kinase/E2F-1 pathway in human colon cancer cells

2010

Ramana, K.V.; Tammali, R.; Srivastava, S.K.

Mol. Cancer Ther.

9

813-824

713240

17498942

Inhibitory effect of rhetsinine isolated from Evodia rutaecarpa on aldose reductase activity

2009

Kato, A.; Yasuko, H.; Goto, H.; Hollinshead, J.; Nash, R.; Adachi, I.

Phytomedicine

16

258-261

713242

19373770

Inhibitory effect of total lignan from fructus Arctii on aldose reductase

2010

Xu, Z.; Yang, H.; Zhou, M.; Feng, Y.; Jia, W.

Phytother. Res.

24

472-473

713308

19052152

Rice aldehyde dehydrogenase7 is needed for seed maturation and viability

2009

Shin, J.; Kim, S.; An, G.

Plant Physiol.

149

905-915

715548

20736170

Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius

2010

Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.

J. Biol. Chem.

285

33701-33709

716878

21294156

Identification of biochemical and putative biological role of a xenolog from Escherichia coli using structural analysis

2011

Bhaskar, V.; Kumar, M.; Manicka, S.; Tripathi, S.; Venkatraman, A.; Krishnaswamy, S.

Proteins

79

1132-1142

719298

21290439

Broadening deoxysugar glycodiversity: natural and engineered transaldolases unlock a complementary substrate space

2011

Rale, M.; Schneider, S.; Sprenger, G.A.; Samland, A.K.; Fessner, W.D.

Chemistry

17

2623-2632

719397

10095793

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme - an aldehyde oxidoreductase

1999

Kardinahl, S.; Schmidt, C.L.; Hansen, T.; Anemueller, S.; Petersen, A.; Schaefer, G.

Eur. J. Biochem.

260

540-548

719837

16849334

Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment

2006

Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.

J. Biol. Chem.

281

27378-27388

722192

22436396

Progresses in the pursuit of aldose reductase inhibitors: the structure-based lead optimization step

2012

Ramunno, A.; Cosconati, S.; Sartini, S.; Maglio, V.; Angiuoli, S.; La Pietra, V.; Di Maro, S.; Giustiniano, M.; La Motta, C.; Da Settimo, F.; Marinelli, L.; Novellino, E.

Eur. J. Med. Chem.

51

216-226

722210

23224332

Molecular characterization of a thermostable aldehyde dehydrogenase (ALDH) from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7

2013

Liu, T.; Hao, L.; Wang, R.; Liu, B.

Extremophiles

17

181-190

722285

22155003

The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase

2012

Zheng, X.; Zhang, L.; Zhai, J.; Chen, Y.; Luo, H.; Hu, X.

FEBS Lett.

586

55-59

723017

23456234

Structures of acylated sucroses and an acylated flavonol glycoside and inhibitory effects of constituents on aldose reductase from the flower buds of Prunus mume

2013

Nakamura, S.; Fujimoto, K.; Matsumoto, T.; Ohta, T.; Ogawa, K.; Tamura, H.; Matsuda, H.; Yoshikawa, M.

J. Nat. Med.

67

799-806

723337

23160889

Molecular cloning and characterization of Schistosoma japonicum aldose reductase

2013

Liu, J.; Wang, J.; Wang, S.; Xu, B.; Liu, X.; Wang, X.; Hu, W.

Parasitol. Res.

112

549-558

723749

23063486

Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1

2013

Mihasan, M.; Stefan, M.; Hritcu, L.; Artenie, V.; Brandsch, R.

Res. Microbiol.

164

22-30

724270

16101307

Identification in the mold Hypocrea jecorina of the first fungal D-galacturonic acid reductase

2005

Kuorelahti, S.; Kalkkinen, N.; Penttilä, M.; Londesborough, J.; Richard, P.

Biochemistry

44

11234-11240

724580

17090924

Functional characterization of D-galacturonic acid reductase, a key enzyme of the ascorbate biosynthesis pathway, from Euglena gracilis

2006

Ishikawa, T.; Masumoto, I.; Iwasa, N.; Nishikawa, H.; Sawa, Y.; Shibata, H.; Nakamura, A.; Yabuta, Y.; Shigeoka, S.

Biosci. Biotechnol. Biochem.

70

2720-2726

725738

-

Characterization and application of a glycolate dehydrogenase from Trichoderma harzianum AIU 353

2012

Isobe, K.; Watabe, S.; Yamada, M.

J. Mol. Catal. B

83

94-99

726464

23444097

New insights into the half-of-the-sites reactivity of human aldehyde dehydrogenase 1A1

2013

Yoval-Sanchez, B.; Pardo, J.P.; Rodriguez-Zavala, J.S.

Proteins

81

1330-1339

727377

22418259

Kinetic mechanism of fuculose-1-phosphate aldolase from the hyperthermophilic archaeon Methanococcus jannaschii

2012

Park, H.C.; Park, J.S.; Choi, J.D.; Dabrowski, M.; Atkins, W.M.; Yoon, M.Y.

Enzyme Microb. Technol.

50

209-214

735415

-

Thermostable transketolase from Geobacillus stearothermophilus: Characterization and catalytic properties

2013

Abdoul-Zabar, J.; Sorel, I.; Helaine, V.; Charmantray, F.; Devamani, T.; Yi, D.; De Berardinis, V.; Louis, D.; Marliere, P.; Fessner, W.; Hecquet, L.

Adv. Synth. Catal.

355

116-128

736023

24034429

Improvement of thermostable aldehyde dehydrogenase by directed evolution for application in Synthetic Cascade Biomanufacturing

2013

Steffler, F.; Guterl, J.K.; Sieber, V.

Enzyme Microb. Technol.

53

307-314

737507

27107110

A beta-alanine batabolism pathway containing a highly promiscuous omega-transaminase in the 12-aminododecanate-degrading Pseudomonas sp. strain AAC

2016

Wilding, M.; Peat, T.S.; Newman, J.; Scott, C.

Appl. Environ. Microbiol.

82

3846-3856

737540

25363556

Promiscuous activity of (S,S)-butanediol dehydrogenase is responsible for glycerol production from 1,3-dihydroxyacetone in Corynebacterium glutamicum under oxygen-deprived conditions

2015

Jojima, T.; Igari, T.; Moteki, Y.; Suda, M.; Yukawa, H.; Inui, M.

Appl. Microbiol. Biotechnol.

99

1427-1433

737604

25528584

L-Idose: an attractive substrate alternative to D-glucose for measuring aldose reductase activity

2015

Balestri, F.; Cappiello, M.; Moschini, R.; Rotondo, R.; Buggiani, I.; Pelosi, P.; Mura, U.; Del-Corso, A.

Biochem. Biophys. Res. Commun.

456

891-895

737763

26215787

Modulation of aldose reductase activity by aldose hemiacetals

2015

Balestri, F.; Cappiello, M.; Moschini, R.; Rotondo, R.; Abate, M.; Del-Corso, A.; Mura, U.

Biochim. Biophys. Acta

1850

2329-2339

738031

23295227

X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP+ and the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity

2013

Ruiz, F.X.; Cousido-Siah, A.; Mitschler, A.; Farres, J.; Pares, X.; Podjarny, A.

Chem. Biol. Interact.

202

178-185

738160

27639366

Design and synthesis of chiral 2H-chromene-N-imidazolo-amino acid conjugates as aldose reductase inhibitors

2016

Gopinath, G.; Sankeshi, V.; Perugu, S.; Alaparthi, M.D.; Bandaru, S.; Pasala, V.K.; Chittineni, P.R.; Krupadanam, G.L.; Sagurthi, S.R.

Eur. J. Med. Chem.

124

750-762

738490

3553159

Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium

1987

Kersten, P.J.; Kirk, T.K.

J. Bacteriol.

169

2195-2201

738833

24341381

Design of an amide N-glycoside derivative of beta-glucogallin: a stable, potent, and specific inhibitor of aldose reductase

2014

Li, L.; Chang, K.C.; Zhou, Y.; Shieh, B.; Ponder, J.; Abraham, A.D.; Ali, H.; Snow, A.; Petrash, J.M.; LaBarbera, D.V.

J. Med. Chem.

57

71-77

738838

25602762

Design and synthesis of potent and multifunctional aldose reductase inhibitors based on quinoxalinones

2015

Qin, X.; Hao, X.; Han, H.; Zhu, S.; Yang, Y.; Wu, B.; Hussain, S.; Parveen, S.; Jing, C.; Ma, B.; Zhu, C.

J. Med. Chem.

58

1254-1267

738840

25695864

Identification of novel aldose reductase inhibitors based on carboxymethylated mercaptotriazinoindole scaffold

2015

Stefek, M.; Soltesova Prnova, M.; Majekova, M.; Rechlin, C.; Heine, A.; Klebe, G.

J. Med. Chem.

58

2649-2657

739042

24939578

Structural characterization and functional validation of aldose reductase from the resurrection plant Xerophyta viscosa

2014

Singh, P.; Sarin, N.B.

Mol. Biotechnol.

56

971-978

739561

11607073

Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase

1990

Kersten, P.J.

Proc. Natl. Acad. Sci. USA

87

2936-2940

739886

26961082

Expression and characterization of a novel 1,3-propanediol dehydrogenase from Lactobacillus brevis

2016

Qi, X.; Yun, J.; Qi, Y.; Zhang, H.; Wang, F.; Guo, Q.; Cao, Z.

Appl. Biochem. Biotechnol.

179

959-972

739966

27956891

NADP-dependent aldehyde dehydrogenase from archaeon Pyrobaculum sp.1860: structural and functional features

2016

Bezsudnova, E.Y.; Petrova, T.E.; Artemova, N.V.; Boyko, K.M.; Shabalin, I.G.; Rakitina, T.V.; Polyakov, K.M.; Popov, V.O.

Archaea

2016

9127857

740291

25451588

Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3)

2015

Lundova, T.; Zemanova, L.; Malcekova, B.; Skarka, A.; Stambergova, H.; Havrankova, J.; Safr, M.; Wsol, V.

Chem. Biol. Interact.

234

178-187

740433

25283443

Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures

2014

Choi, D.; Kim, J.; Ha, S.; Kwon, K.; Kim, E.H.; Lee, H.Y.; Ryu, K.S.; Park, C.

FEBS J.

281

5447-5462

758685

30178202

Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and alpha-diketones

2018

Bezsudnova, E.Y.; Stekhanova, T.N.; Popinako, A.V.; Rakitina, T.V.; Nikolaeva, A.Y.; Boyko, K.M.; Popov, V.O.

Appl. Microbiol. Biotechnol.

102

9621-9633

761025

28259841

Enhancing activity and selectivity in a series of pyrrol-1-yl-1-hydroxypyrazole-based aldose reductase inhibitors The case of trifluoroacetylation

2017

Papastavrou, N.; Chatzopoulou, M.; Ballekova, J.; Cappiello, M.; Moschini, R.; Balestri, F.; Patsilinakos, A.; Ragno, R.; Stefek, M.; Nicolaou, I.

Eur. J. Med. Chem.

130

328-335

762829

33686415

Characterization of a cryptic, pyrroloquinoline quinone-dependent dehydrogenase of Gluconobacter sp. strain CHM43

2021

Nguyen, T.; Naoki, K.; Kataoka, N.; Matsutani, M.; Ano, Y.; Adachi, O.; Matsushita, K.; Yakushi, T.

Biosci. Biotechnol. Biochem.

85

998-1004

763075

30766522

Characterization of an aldehyde oxidoreductase from the mesophilic bacterium Aromatoleum aromaticum EbN1, a member of a new subfamily of tungsten-containing enzymes

2019

Arndt, F.; Schmitt, G.; Winiarska, A.; Saft, M.; Seubert, A.; Kahnt, J.; Heider, J.

Front. Microbiol.

10

71

763266

31097544

The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis

2019

Scott, I.M.; Rubinstein, G.M.; Poole, F.L.; Lipscomb, G.L.; Schut, G.J.; Williams-Rhaesa, A.M.; Stevenson, D.M.; Amador-Noguez, D.; Kelly, R.M.; Adams, M.W.W.

J. Biol. Chem.

294

9995-10005

764945

14690376

Multiple forms of xylose reductase in Candida intermedia comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies

2003

Nidetzky, B.; Brueggler, K.; Kratzer, R.; Mayr, P.

J. Agric. Food Chem.

51

7930-7935

765123

16232468

Expression of xyrA gene encoding for D-xylose reductase of Candida tropicalis and production of xylitol in Escherichia coli

1999

Suzuki, T.; Yokoyama, S.; Kinoshita, Y.; Yamada, H.; Hatsu, M.; Takamizawa, K.; Kawai, K.

J. Biosci. Bioeng.

87

280-284