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Ligand glycolaldehyde

Basic Ligand Information

Molecular Structure

Related pathways

Pathway Source

Pathways

BRENDA

6-hydroxymethyl-dihydropterin diphosphate biosynthesis, degradation of pentoses

KEGG

Folate biosynthesis, Glyoxylate and dicarboxylate metabolism, Microbial metabolism in diverse environments, Pentose and glucuronate interconversions, Vitamin B6 metabolism

MetaCyc

6-hydroxymethyl-dihydropterin diphosphate biosynthesis I, 6-hydroxymethyl-dihydropterin diphosphate biosynthesis II (Methanocaldococcus), 6-hydroxymethyl-dihydropterin diphosphate biosynthesis III (Chlamydia), D-arabinose degradation II, D-xylose degradation IV, D-xylose degradation to ethylene glycol (engineered), ethylene glycol degradation, L-arabinose degradation IV, L-ascorbate degradation IV, tetrahydromethanopterin biosynthesis more

Show all BRENDA pathways known for glycolaldehyde

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.265

glycolaldehyde + NADH + H+ = ethylene glycol + NAD+

763285

-

1.2.1.21

glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+

763597

-

4.1.2.25

6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde = 7,8-dihydroneopterin + 7,8-dihydromonapterin

747481, 746987, 748090

-

4.1.2.48

glycine + glycolaldehyde = L-4-hydroxythreonine

716291

-

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.81

7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde

-

-

1.4.3.8

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

-

-

4.1.2.25

7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde

-

-

4.1.2.25

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde

-

-

4.1.2.55

2-dehydro-3-deoxy-D-xylonate = pyruvate + glycolaldehyde

-

-

4.1.2.55

2-dehydro-3-deoxy-L-arabinonate = pyruvate + glycolaldehyde

-

-

4.1.2.25

2 entries

4.1.2.55

2 entries

Substrate in Enzyme-catalyzed Reactions (88 results)

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Show Substrate (88 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

glycolaldehyde + NADH + H+ = glycol + NAD+

739927, 763285

-

1.1.1.2

glycolaldehyde + NADPH = ethane-1,2-diol + NADP+

286184, 286181

-

1.1.1.21

glycoaldehyde + NADPH + H+ = ethylene glycol + NADP+

697266

-

1.1.1.21

glycoaldehyde + NADPH = ethylene glycol + NADP+

286238

-

1.1.1.21

glycolaldehyde + NADPH + H+ = ?

695881

-

1.1.1.21

3 entries

1.1.1.265

glycolaldehyde + NADH + H+ = ethylene glycol + NAD+

763285

-

1.1.1.4

glycolaldehyde + NADH + H+ = ? + NAD+

760423

-

1.1.1.71

glycoaldehyde + NADPH + H+ = ?

737536

-

1.1.1.72

glycolaldehyde + NADPH = ethyleneglycol + NADP+

287283, 287285

-

1.1.1.8

glycolaldehyde + NADH + H+ = ?

740076

-

1.1.1.8

glycolaldehyde + NADH + H+ = ? + NAD+

740076

-

1.1.1.8

glycolaldehyde + NADH + H+ = ethane-1,2-diol + NAD+

740579

-

1.1.1.8

glycolaldehyde + NADH = ?

685237, 740578

-

1.1.3.9

glycoaldehyde + O2 = glyoxal + H2O2

389862

-

1.1.3.9

glycolaldehyde + O2 = glyoxal + H2O2

687852, 712522

-

1.1.1.8

4 entries

1.1.3.9

2 entries

1.1.99.14

glycolaldehyde + nitro blue tetrazolium = ? + reduced nitro blue tetrazolium

725738

-

1.2.1.10

glycolaldehyde + CoA + NAD+ = hydroxyacetyl-CoA + NADH

390168

-

1.2.1.21

glycolaldehyde + NAD+ + H2O = glycolate + NADH

390212, 390211, 288131, 390210, 390214, 390215, 390213

-

1.2.1.21

glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+

763597

-

1.2.1.21

glycolaldehyde + NADP+ + H2O = glycolate + NADPH + H+

390211, 390213

-

1.2.1.22

glycoaldehyde + NAD+ + H2O = glycolate + NADH + H+

670833

-

1.2.1.22

glycolaldehyde + NAD+ + H2O = glycolate + NADH

288131, 288133, 674270

-

1.2.1.22

glycolaldehyde + NAD+ + H2O = glycolate + NADH + 2 H+

697876

-

1.2.1.21

3 entries

1.2.1.22

3 entries

1.2.1.24

glycoaldehyde + NAD+ + H2O = glycolate + NADH

674654

-

1.2.1.26

glycolaldehyde + NADP+ + H2O = glycolate + NADPH + H+

719837, 715548

-

1.2.1.3

glycolaldehyde + NAD+ + H2O = glycolate + NADH

348692, 348705, 348682, 348695, 348708, 675670, 348683, 348693

-

1.2.1.3

glycolaldehyde + NAD+ + H2O = glycolate + NADH + H+

722210

-

1.2.1.3

2 entries

1.2.1.4

glycolaldehyde + NADP+ + H2O = glycolate + NADPH + H+

437838

-

1.2.1.5

glycolaldehyde + NAD+ + H2O = glycolate + NADH + H+

722210

-

1.2.1.5

glycolaldehyde + NAD+ = glycolate + NADH

348793, 348794, 348795, 348792

-

1.2.1.5

glycolaldehyde + NADP+ + H2O = glycolate + NADPH + H+

348795, 348796

-

1.2.1.5

3 entries

1.2.1.69

glycoaldehyde + NAD+ + H2O = glycolate + NADH + H+

636460

-

1.2.1.76

glycolaldehyde + coenzyme A + NADP+ = ? + NADPH + H+

697694

-

1.2.1.8

glycolaldehyde + NAD+ + H2O = glycolate + NADH

390362, 390357

-

1.2.1.8

glycolaldehyde + NAD+ + H2O = glycolate + NADH + H+

656550

-

1.2.1.8

glycolaldehyde + NADP+ + H2O = glycolate + NADPH + H+

656550

-

1.2.1.8

3 entries

1.2.1.89

glycolaldehyde + NADP+ = glycolate + NADPH + H+

724216, 724992

-

1.2.3.1

glycoaldehyde + H2O + O2 = hydroxyacetic acid + H2O2

390396

-

1.2.3.1

glycolaldehyde + H2O + O2 = hydroxyacetic acid + H2O2

740776

-

1.2.3.15

glycolaldehyde + H2O + O2 = ?

739561

-

1.2.3.15

glycolaldehyde + H2O + O2 = hydroxyacetate + H2O2

738490

-

1.2.3.1

2 entries

1.2.3.15

2 entries

1.2.3.5

glycolaldehyde + O2 + H2O = ?

288397

-

1.2.5.2

glycolaldehyde + ferricyanide = hydroxyacetic acid + ferrocyanide + H+

731204

-

1.2.99.6

Glycolaldehyde + benzyl viologen = Glycolate + reduced benzyl viologen

11936

-

1.2.99.7

glycoaldehyde + H2O + benzylviologen = glycolate + reduced benzylviologen

11936

-

2.2.1.1

2 glycolaldehyde + ? = erythrulose + ?

776394

-

2.2.1.1

2-methoxyethanal + glycolaldehyde = (3S)-1,3-dihydroxy-4-methoxybutan-2-one

735938

-

2.2.1.1

beta-hydroxypyruvate + glycolaldehyde = L-erythrulose + CO2

691763, 692117, 696070, 696071

-

2.2.1.1

butanal + glycolaldehyde = (3S)-1,3-dihydroxyhexan-2-one

735938

-

2.2.1.1

glycolaldehyde + 2-oxobutanoate = ? + CO2

777044

-

2.2.1.1

glycolaldehyde + ? = ?

486023

-

2.2.1.1

glycolaldehyde + Fe(CN)6 + H2O = glycolic acid + ferrocyanide + ?

776394

-

2.2.1.1

glycolaldehyde + fructose 6-phosphate = ?

776394

-

2.2.1.1

glycolaldehyde + hydroxypyruvate = L-erythrulose + CO2

735415, 779303, 777044

-

2.2.1.1

glycolaldehyde + lithium hydroxypyruvate = L-erythrulose

778842

-

2.2.1.1

glycolaldehyde + pyruvate = 3,4-dihydroxy-2-butanone + CO2

756713, 777044

-

2.2.1.1

glycolaldehyde + ribose 5-phosphate = D-sedoheptulose 7-phosphate

776394

-

2.2.1.1

glycolaldehyde + xylulose 5-phosphate = ?

776394

-

2.2.1.1

hydroxypyruvate + glycolaldehyde = erythrulose + ?

658678

-

2.2.1.1

hydroxypyruvate + glycolaldehyde = L-erythrulose + ?

693289, 693291, 757041

-

2.2.1.1

lithium beta-hydroxypyruvate + glycolaldehyde = L-erythrulose + ?

696918

-

2.2.1.1

propanal + glycolaldehyde = (3S)-1,3-dihydroxypentan-2-one

735938, 756629

-

2.2.1.3

D-xylulose 5-phosphate + glycolaldehyde = glyceraldehyde 3-phosphate + 1,3,5-trihydroxypentane-2-one

486048, 486051

-

2.2.1.3

glycolaldehyde + D-xylulose 5-phosphate = glyceraldehyde 3-phosphate + 1,3-dihydroxypentane-2-one

486057

-

2.2.1.1

17 entries

2.2.1.3

2 entries

2.2.1.7

pyruvate + glycolaldehyde = 1-deoxy-L-erythrulose + CO2

659734

-

2.2.1.8

L-threonine + glycolaldehyde = acetaldehyde + 4-hydroxyl-L-threonine

755884

-

2.5.1.54

phosphoenolpyruvate + glycolaldehyde = (S)-2-oxo-4,5-dihydroxypentanoate + phosphate

639780

-

2.6.1.77

taurine + glycolaldehyde = 2-sulfoacetaldehyde + ?

737516

-

4.1.1.1

beta-hydroxypyruvate + glycolaldehyde = 1,3,4-trihydroxy-2-butanone

678579

-

4.1.1.8

glycolaldehyde + formyl-CoA = glyceryl-CoA

768566

-

4.1.2.14

pyruvate + glycoaldehyde = ?

650823, 586786

-

4.1.2.17

L-glycerol 3-phosphate + glycoaldehyde = D-ribulose 1-phosphate

727788

-

4.1.2.17

Glycerone phosphate + glycolaldehyde = D-Ribulose 1-phosphate

5049, 5047, 5048

-

4.1.2.17

2 entries

4.1.2.19

Glycerone phosphate + glycolaldehyde = L-Xylulose 1-phosphate

5049, 5071, 5066

-

4.1.2.20

pyruvate + glycolaldehyde = 2-oxo-4,5-dihydroxy-L-pentanoic acid

5078, 4971

-

4.1.2.25

6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde = 7,8-dihydroneopterin + 7,8-dihydromonapterin

727676, 747481, 746987, 748090

-

4.1.2.43

D-ribulose 5-phosphate + glycolaldehyde = 4-heptulose 7-phosphate

690311

-

4.1.2.43

D-ribulose 5-phosphate + glycolaldehyde = ?

694004, 690565

-

4.1.2.43

2 entries

4.1.2.48

glycine + glycolaldehyde = L-4-hydroxythreonine

716291

-

4.1.2.52

pyruvate + glycolaldehyde = ?

702377

-

4.1.2.54

pyruvate + glycolaldehyde = ?

722654

-

4.1.2.55

pyruvate + glycolaldehyde = 2-dehydro-3-deoxy-D-xylonate

715548, 718771

-

4.1.2.55

pyruvate + glycolaldehyde = 2-dehydro-3-deoxy-L-arabinonate

715548, 718771

-

4.1.2.55

pyruvate + glycolaldehyde = ?

718713

-

4.1.3.39

pyruvate + glycolaldehyde = 4,5-dihydroxy-2-oxo-pentanoic acid

702377

-

4.1.3.39

pyruvate + glycolaldehyde = ?

702377

-

4.1.2.55

3 entries

4.1.3.39

2 entries

4.1.3.43

pyruvate + glycolaldehyde = ?

702377

-

5.3.1.1

glycolaldehyde = ?

702315, 727027

-

Product in Enzyme-catalyzed Reactions (38 results)

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Show Product (38 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.156

1,2-ethanediol + NADP+ = hydroxyacetaldehyde + NADPH

286042

-

1.1.1.283

glyoxal + NADPH = glycolaldehyde + NADP+

207971, 207974

-

1.1.1.6

ethanediol + NAD+ = glycolaldehyde + NADH

636283, 636289

-

1.1.1.6

1,2-ethanediol + NAD+ = hydroxyacetaldehyde + NADH + H+

-

-

1.1.1.6

2 entries

1.1.1.77

ethylene glycol + NAD+ = glycolaldehyde + NADH + H+

-

-

1.1.1.78

glyoxal + NADH = glycolaldehyde + NAD+

207975

-

1.1.9.1

1,2-ethanediol + ferricyanide = hydroxyacetaldehyde + ferrocyanide

-

-

1.11.1.14

guaiacyl glycerol-beta-guaiacyl ether + H2O2 = vanillin + guaiacol + 2-hydroxyacetaldehyde + H2O

-

-

1.11.1.14

1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = vanillin + hydroxyacetaldehyde + guaiacol

-

-

1.11.1.14

2 entries

1.13.11.81

7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde

-

-

1.13.12.16

1-hydroxyethyl-2-nitronate + O2 = glycoaldehyde + HNO2

-

-

1.13.12.16

2-nitroethanol + O2 = glycoaldehyde + HNO2

-

-

1.13.12.16

2 entries

1.14.14.34

isethionate + FMNH2 + O2 = hydroxyacetaldehyde + FMN + sulfite + H2O

-

-

1.4.3.21

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

-

-

1.4.3.4

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

-

-

1.4.3.8

ethanolamine + H2O + O2 = glycolaldehyde + NH3 + H2O2

-

-

2.2.1.1

2 D-xylulose 5-phosphate = glyceraldehyde 3-phosphate + glycolaldehyde

-

-

2.2.1.1

D-ribose-5-phosphate + L-erythrulose = D-sedoheptulose 7-phosphate + glycolaldehyde

-

-

2.2.1.1

L-erythrulose + D-ribose = D-seduheptulose + glycolaldehyde

-

-

2.2.1.1

L-erythrulose + D-ribose-5-phosphate = D-sedoheptulose 7-phosphate + glycolaldehyde

-

-

2.2.1.1

L-erythrulose + L-threose = L-sorbose + glycolaldehyde

-

-

2.2.1.1

5 entries

3.2.1.58

periodate-oxidized and reduced laminarin = glycerol + glycoaldehyde + D-glucose

136646, -

-

4.1.1.1

3-Hydroxypyruvate = Glycolaldehyde + CO2

114290, -

-

4.1.1.1

beta-hydroxypyruvate = glycolaldehyde + ?

-

-

4.1.1.1

2 entries

4.1.1.40

Hydroxypyruvate = Glycolaldehyde + CO2

4542, 4543

-

4.1.2.17

D-ribose 1-phosphate = glycerone phosphate + glycolaldehyde

-

-

4.1.2.18

2-Keto-3-deoxy-D-xylonate = Pyruvate + glycolaldehyde

5063

-

4.1.2.18

2-Keto-3-deoxy-L-arabonate = Pyruvate + glycolaldehyde

5057, 5059, -

-

4.1.2.18

2 entries

4.1.2.19

Xylulose 1-phosphate = Glycerone phosphate + glycoaldehyde

-

-

4.1.2.25

2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde

5110, 5109, 5104, 5107, 5105, 5106, 5108, 5103

-

4.1.2.25

7,8-dihydromonapterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde

-

-

4.1.2.25

7,8-dihydroneopterin = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde

-

-

4.1.2.25

7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde

652042, 653544, 652283, -

-

4.1.2.25

4 entries

4.1.2.28

2-dehydro-3-deoxy-D-pentonate = pyruvate + glycolaldehyde

5123

-

4.1.2.4

Glyceraldehyde phosphate + acetaldehyde = Hydroxyacetaldehyde + glyceraldehyde 3-phosphate

-

-

4.1.2.48

L-4-hydroxythreonine = glycine + glycolaldehyde

-

-

4.1.2.55

2-dehydro-3-deoxy-D-xylonate = pyruvate + glycolaldehyde

-

-

4.1.2.55

2-dehydro-3-deoxy-L-arabinonate = pyruvate + glycolaldehyde

-

-

4.1.2.55

2 entries

Inhibitor in Enzyme-catalyzed Reactions (11 results)

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Show Inhibitors (11 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

slight inhibition

763285

-

1.2.1.21

substrate inhibition

390213

-

1.2.1.22

substrate inhibition

288133

-

2.2.1.1

-

691763

-

2.3.3.12

-

488128

-

2.6.1.16

weak

639912

-

4.1.2.43

49% inhibition at 4 mM

691118

-

4.1.3.16

competitive, Ki for 2-keto-4-hydroxybutyrate cleavage: 2.7 mM, Ki for 2-keto-4-hydroxyglutarate cleavage: 2.4 mM

5238

-

4.2.1.130

about 60% inhibition at 10 mM

740433

-

4.2.1.28

inactivates

5623

-

5.1.3.4

-

2396

-

3D Structure of Enzyme-Ligand-Complex (PDB) (2 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (2 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.2.4.2

6KMA, 3D-view

4.1.1.47

8I07, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (21 results)

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Show Turnover Number (21 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.1

15.44

-

pH 7.0, 30°C, with NADH

763285

1.1.1.1

18.65

-

pH 7.0, 30°C

739927

1.1.1.21

0.2

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.21

0.58

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

1.1.1.1

2 entries

1.1.1.21

2 entries

1.1.1.265

15.44

-

pH 7.0, 30°C

763285

1.1.1.4

7.39

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B

760423

1.1.1.4

9.43

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B

760423

1.1.1.4

37.32

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y

760423

1.1.1.4

53.46

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y

760423

1.1.1.4

4 entries

1.2.1.22

18.3

-

100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+

670833

1.2.1.26

5.3

-

pH 7.5, 70°C

719837

1.2.1.3

1.2

-

-

348708

1.2.1.89

20

-

pH 6.9, 58°C

724992

1.2.1.89

37

-

pH 6.9, 58°C

724992

1.2.1.89

2 entries

2.2.1.1

0.45

-

pH 7.0, 65°C

778842

2.2.1.8

0.024

-

at pH 7.5 and 28°C

755884

4.1.2.52

175.5

-

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

702377

4.1.3.39

0.4

-

at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate

702377

4.1.3.39

0.4

-

pH 8.0, 25°C

702377

4.1.3.39

175.5

-

pH 8.0, 25°C

702377

4.1.3.39

3 entries

4.1.3.43

0.4

-

app. kcat-value with pyruvate as carbonyl donor, pH 8.0 and 25°C

702377

K_M Value (63 results)

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Show KM Value (63 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.1

16.11

-

pH 7.0, 30°C, with NADH

763285

1.1.1.1

88.32

-

pH 7.0, 30°C

739927

1.1.1.1

2 entries

1.1.1.2

9.9

-

AR2

286181

1.1.1.21

1.5

-

in 0.1 M potassium phosphate, pH 7.4

697266

1.1.1.21

1.8

-

-

286238

1.1.1.21

21

-

in 0.1 M potassium phosphate, pH 7.4, at 25°C

695881

1.1.1.21

3 entries

1.1.1.265

16.11

-

pH 7.0, 30°C

763285

1.1.1.4

9.38

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y

760423

1.1.1.4

15.52

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain Y

760423

1.1.1.4

17.91

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B

760423

1.1.1.4

29.42

-

recombinant enzyme, pH 7.0, 30°C, with NADH, from strain B

760423

1.1.1.4

4 entries

1.1.3.9

13.2

-

-

687852

1.2.1.10

20

-

-

390168

1.2.1.21

0.027

-

isozyme A

390213

1.2.1.21

0.25

-

-

390211

1.2.1.21

8.3

-

isozyme C

390213

1.2.1.21

14

-

isozyme A from vitamin B6 auxotroph mutant strain WG3

390213

1.2.1.21

27

-

isozyme B

390213

1.2.1.22

0.14

-

100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+

670833

1.2.1.22

0.38

-

-

288133

1.2.1.21

5 entries

1.2.1.22

2 entries

1.2.1.26

0.37

-

pH 6.0, 70°C, native enzyme form xylose-grown cells

715548

1.2.1.3

0.005

-

isoenzyme I

348705

1.2.1.3

0.021

-

isoenzyme II

348705

1.2.1.3

0.038

-

native enzyme

348695

1.2.1.3

0.045

-

-

348682

1.2.1.3

0.046

-

isoenzyme 2, pH 7.4

348693

1.2.1.3

0.077

-

mutant enzyme S74A

348695

1.2.1.3

0.11

-

isoenzyme III

348705

1.2.1.3

0.18

-

-

348683

1.2.1.3

0.2

-

enzyme from brain

348692

1.2.1.3

0.24

-

enzyme from liver

348692

1.2.1.3

0.69

-

-

348708

1.2.1.3

11 entries

1.2.1.4

2.2

-

-

437838

1.2.1.5

0.05

-

isoenzyme F2

348792, 348796

1.2.1.5

0.13

-

isoenzyme F1

348792, 348796

1.2.1.5

2 entries

1.2.1.69

0.15

-

-

636460

1.2.1.8

0.152

-

mitochondrial enzyme

390357

1.2.1.8

0.153

-

-

390362

1.2.1.8

0.24

-

-

390362

1.2.1.8

4.3

-

pH 7.7, coenzyme NAD+

656550

1.2.1.8

11.5

-

pH 7.7, coenzyme NADP+

656550

1.2.1.89

11.1

-

pH 6.9, 58°C

724992

1.2.1.89

12.3

-

pH 6.9, 58°C

724992

1.2.1.8

5 entries

1.2.1.89

2 entries

1.2.3.1

1

-

pH 7.0, 30°C

740776

2.2.1.1

0.1

1

and second value 2.2 mM, cosubstrate Fe(CN)6 , pH 7.6, temperature not specified in the publication

776394

2.2.1.1

0.13

-

and second value 0.45 mM, cosubstrate xylulose 5-phosphate , pH 7.6, temperature not specified in the publication

776394

2.2.1.1

0.15

-

and second value 1.8 mM, one-substrate reaction, pH 7.6, temperature not specified in the publication

776394

2.2.1.1

0.47

-

and second value 1.7 mM, cosubstrate ribose 5-phosphate, pH 7.6, temperature not specified in the publication

776394

2.2.1.1

1.8

-

and second value 0.15 mM, one-substrate reaction, pH 7.6, temperature not specified in the publication

776394

2.2.1.1

3.6

-

pH 7.0, 65°C

778842

2.2.1.1

14

-

-

486023

2.2.1.1

35

-

wild-type, in the presence of 50 mM hydroxypyruvate

693289

2.2.1.1

200

-

mutant A29E, in the presence of 50 mM hydroxypyruvate

693289

2.2.1.1

9 entries

2.2.1.8

0.357

-

at pH 7.5 and 28°C

755884

2.5.1.54

8.6

-

cytosolic isozyme DS-Co, pH 8.6, 37°C

639780

4.1.2.25

10

-

apparent value

679768

4.1.2.43

4.3

-

apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30°C

690311

4.1.2.43

4.3

-

in 500 mM potassium phosphate buffer, at pH 7.5, at 30°C

694004

4.1.2.43

2 entries

4.1.2.52

33.3

-

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

702377

4.1.3.39

33.3

-

pH 8.0, 25°C

702377

4.1.3.39

124.6

-

at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate

702377

4.1.3.39

124.6

-

pH 8.0, 25°C

702377

4.1.3.39

3 entries

4.1.3.43

124.6

-

app. Km-value with pyruvate as carbonyl donor, pH 8.0 and 25°C

702377

K_i Value (4 results)

top print hide

Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.21

0.0021

-

isozyme A

390213

1.2.1.21

0.004

-

isozyme B

390213

1.2.1.21

8.3

-

isozyme C

390213

1.2.1.21

3 entries

5.1.3.4

0.37

-

37°C, pH 7.6, mutant enzyme H97N, with L-ribulose 5-phosphate as substrate

2396

References & Links

Literature References (156)

top print hide

Show Reference (156 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

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1998

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1962

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1972

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1982

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1969

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Biochemistry

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1975

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1966

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5103

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1980

Mathis, J.B.; Brown, G.M.

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5104

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1970

Mathis, J.B.; Brown, G.M.

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5105

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Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carnii

1995

Volpe, F.; Ballantine, S.P.; Delves, C.J.

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160

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5106

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Single amino acid substitutions dirupts tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carnii

1998

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Biochemistry

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5107

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1993

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5108

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The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase

1993

Volpe, F.; Ballantine, S.P.; Delves, C.J.

Eur. J. Biochem.

216

449-458

5109

9651328

Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase

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Hau¯mann, C.; Rohdich, F.; Schmidt, E.; Bacher, A.; Richter, G.

J. Biol. Chem.

273

17418-17424

5110

9586996

Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus

1998

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357-362

5123

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3 deoxy-D-Pentulosonic acid aldolase and its role in a new pathway of D-xylose degradation

1974

Dahms, A.S.

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5238

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2-keto-4-Hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in mammalian metabolism of L-homoserine

1971

Lane, R.S.; Shapley, A.; Dekker, E.E.

Biochemistry

10

1353-1364

5623

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Diol dehydrase

1982

Toraya, T.; Fukui, S.

B12 (Dolphin, D. ed. ) Wiley, New York

2

233-262

11936

7592385

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

1995

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

J. Bacteriol.

177

6195-6200

114290

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The enzymatic decarboxylation of hydroxypyruvate associated with purified pyruvate decarboxylase from wheat germ

1985

Davies, D.D.; Asker, H.

Phytochemistry

24

231-234

136646

164221

The attack mechanism of an exo-1,3-beta-glucosidase from Basidiomycete sp. QM 806

1975

Nelson, T.E.

Biochim. Biophys. Acta

377

139-145

207971

3896793

Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae

1985

Murata, K.; Fukuda, Y.; Simosaka, M.; Watanabe, K.; Saikusa, T.; Kimura, A.

Eur. J. Biochem.

151

631-636

207974

3276516

Metabolism of 2-oxoaldehyde in mold. Purification and characterization of two methylglyoxal reductases from Aspergillus niger

1988

Inoue, Y.; Rhee, H.; Watanabe, K.; Murata, K.; Kimura, A.

Eur. J. Biochem.

171

213-218

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

286042

4146296

NADP specific dihydroxyacetone reductase from Dunaliella parva

1973

Amotz-Ben, A.; Avron, M.

FEBS Lett.

29

153-155

286181

6753936

Purification and properties of human liver aldehyde reductases

1982

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

Biochim. Biophys. Acta

707

105-114

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

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

287283

7144572

Glycerol dehydrogenase from rabbit muscle

1982

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

Methods Enzymol.

89

237-242

287285

-

Purification and properties of NADP+ -linked glycerol dehydrogenase from Neurospora crassa

1978

Viswanath-Reddy, M.; Pyle, J.E.; Branch Howe, E.

J. Gen. Microbiol.

107

289-296

288131

6345530

Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli

1983

Caballero, E.; Baldoma, L.; Ros, J.; Boronat, A.; Aguilar, J.

J. Biol. Chem.

258

7788-7792

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

288397

-

Partial purification and characterization of glyoxylate oxidase from the brown-rot basidiomycete Tyromyces palustris

1994

Akamatsu, Y.; Shimada, M.

Phytochemistry

37

649-653

348682

10852

Localization and characteristics of rat liver mitochondrial aldehyde dehydrogenases

1976

Siew, C.; Deitrich, R.A.

Arch. Biochem. Biophys.

176

638-649

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

348692

8645224

Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution

1996

Kikonyogo, A.; Pietruszko, R.

Biochem. J.

316

317-324

348693

9787766

Methylglyoxal as substrate and inhibitor of human aldehyde dehydrogenase: comparison of kinetic properties among the three isoenzymes

1998

Izaguirre, G.; Kikonyogo, A.; Pietruszko, R.

Comp. Biochem. Physiol. B

119

747-754

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

348705

3592683

Purification and characterization of aldehyde dehydrogenase from human brain

1987

Ryzlak, M.T.; Pietruszko, R.

Arch. Biochem. Biophys.

255

409-418

348708

6651766

Bovine lens aldehyde dehydrogenase. Kinetics and mechanism

1983

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

Biochem. J.

215

361-368

348792

7144584

Isozymes of aldehyde dehydrogenase from horse liver

1982

Eckfeldt, J.H.; Yonetani, T.

Methods Enzymol.

89

474-479

348793

6755180

Aldehyde dehydrogenase from bakers yeast

1982

Tamaki, N.; Hama, T.

Methods Enzymol.

89

469-473

348794

19457

Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae

1977

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

J. Biochem.

82

73-79

348795

30447

Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae

1978

Bostian, K.A.; Betts, G.F.

Biochem. J.

173

787-798

348796

1244351

Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes

1976

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

J. Biol. Chem.

251

236-240

389862

3813549

Purification and characterization of intracellular galactose oxidase from Dactylium dendroides

1987

Mendoca, M.H.; Zancan, G.T.

Arch. Biochem. Biophys.

252

507-514

390168

13061511

The oxidation of acetaldehyde to acetyl coenzyme A

1953

Burton, R.M.; Stadtman, E.R.

J. Biol. Chem.

202

873-890

390210

6336729

Experimental evolution of a metabolic pathway for ethylene glycol utilization by Escherichia coli

1983

Boronat, A.; Caballero, E.; Aguilar, J.

J. Bacteriol.

153

134-139

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

390212

-

Bacterial distribution of glycolaldehyde dehydrogenase in relation to vitamin B6 biosynthesis

1979

Morita, H.; Nishimura, T.; Tani, Y.; Ogata, K.; Yamada, H.

Agric. Biol. Chem.

43

185-186

390213

-

Further characterization of glycolaldehyde dehydrogenase isozymes from Escherichia coli B involvement in vitamin B6 biosynthesis

1978

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

Agric. Biol. Chem.

42

2077-2081

390214

-

Control of glycolaldehyde dehydrogenase in vitamin B6 biosynthesis in Escherichia coli B

1978

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

Agric. Biol. Chem.

42

69-73

390215

-

Separation and characterization of glycolaldehyde dehydrogenase isozymes in Escherichia coli B

1978

Tani, Y.; Morita, H.; Nishise, H.; Ogata, K.

Agric. Biol. Chem.

42

63-68

390357

11306043

Betaine aldehyde dehydrogenase from rat liver mitochondrial matrix

2001

Pietruszko, R.; Chern, M.K.

Chem. Biol. Interact.

130-132

193-199

390362

10505788

Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, characterization, and comparison with human cytoplasmic E3 isozyme

1999

Chern, M.K.; Pietruszko, R.

Biochem. Cell Biol.

77

179-187

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

437838

13061400

Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast

1953

Seegmiller, J.E.

J. Biol. Chem.

201

629-637

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

486048

2280716

Dihydroxyacetone synthase from Candida boidinii KD1

1990

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

Methods Enzymol.

188

435-445

486051

-

Dihydroxyacetone synthase: a special transketolase for formaldehyde fixation from the methylotrophic yeast Candida boidinii CBS 5777

1983

Waites, M.J.; Quayle, J.R.

J. Gen. Microbiol.

129

935-944

486057

9324250

Dihydroxyacetone synthase from a methanol-utilizing carboxydobacterium, Acinetobacter sp. strain JC1 DSM 3803

1997

Ro, Y.T.; Eom, C.Y.; Song, T.; Cho, J.W.; Kim, Y.M.

J. Bacteriol.

179

6041-6047

488128

14085361

n-Propylmalate synthetase

1963

Imai, K.; Reeves, H.C.; Ajl, S.J.

J. Biol. Chem.

238

3193-3198

586786

11814840

Cloning, Isolation and Characterization of the Thermotoga Maritima KDPG aldolase

2002

Griffiths, J.S.; Wymer, N.J.; Njolito, E.; Niranjanakumari, S.; Fierke, C.A.; Toone, E.J.

Bioorg. Med. Chem.

10

545-550

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

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

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

639780

-

The cytosolic isoenzyme of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in Spinacia oleracea and other higher plants: extreme substrate ambiguity and other properties

1992

Doong, R.L.; Gander, J.E.; Ganson, R.J.; Jensen, R.A.

Physiol. Plant.

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639912

4650135

Inhibition of L-glutamine:D-fructose-6-phosphate aminotransferase by methylglyoxal

1972

Kikuchi, H.; Ikeda, Y.; Tsuiki, S.

Biochim. Biophys. Acta

289

303-310

650823

11094340

Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars

2000

Fong, S.; Machajewski, T.D.; Mak, C.C.; Wong, C.

Chem. Biol.

7

873-883

652042

10896664

A vibrational structure of 7,8-dihydrobiopterin bound to dihydroneopterin aldolase

2000

Deng, H.; Callender, R.; Dale, G.E.

J. Biol. Chem.

275

30139-30143

652283

12039964

Biosynthesis of tetrahydrofolate. Stereochemistry of dihydroneopterin aldolase

2002

Illarionova, V.; Eisenreich, W.; Fischer, M.; Haussmann, C.; Romisch, W.; Richter, G.; Bacher, A.

J. Biol. Chem.

277

28841-28847

653544

15107504

Folate biosynthesis in higher plants. cDNA cloning, heterologous expression, and characterization of Dihydroneopterin aldolases

2004

Goyer, A.; Illarionova, V.; Roje, S.; Fischer, M.; Bacher, A.; Hanson, A.D.

Plant Physiol.

135

103-111

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

658678

15752351

Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae

2005

Golbik, R.; Meshalkina, L.E.; Sandalova, T.; Tittmann, K.; Fiedler, E.; Neef, H.; Konig, S.; Kluger, R.; Kochetov, G.A.; Schneider, G.; Hubner, G.

Febs J.

272

1326-1342

659734

-

Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars

2002

Schürmann, M.; Schürmann, M.; Sprenger, G.A.

J. Mol. Catal. B

19-20

247-252

670833

16731973

Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases

2006

Rodriguez-Zavala, J.S.; Allali-Hassani, A.; Weiner, H.

Protein Sci.

15

1387-1396

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

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