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Ligand D-glyceraldehyde

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Carbon metabolism, Fructose and mannose metabolism, Galactose metabolism, Glycerolipid metabolism, Microbial metabolism in diverse environments, Pentose phosphate pathway more

MetaCyc

Entner-Doudoroff pathway II (non-phosphorylative), sucrose degradation V (sucrose alpha-glucosidase)

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.2

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

286177, 286178, 286182, 286187, 286196, 286172, 286175, 286149, 286168, 286176, 286186, 286199, 286165, 286174, 286192, 286204, 286167, 286171, 286179

-

1.1.1.372

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

673558

-

1.1.1.72

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

287287, 287283, 287286, 287288, 287285, 287284

-

1.2.1.89

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

762564, 724216, 724992

-

1.2.99.8

D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor

719397

-

2.2.1.7

pyruvate + D-glyceraldehyde = 1-deoxy-D-xylulose + CO2

659734

-

2.7.1.28

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

730035, 758623, 759025, 759363

-

2.7.1.28

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

641261, 641262

-

2.7.1.28

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (10 results)

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Show Natural Product (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.6

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

0

-

1.1.1.72

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

0

-

2.2.1.11

methylglyoxal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate

0

-

4.1.2.14

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

0

-

4.1.2.14

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

0

-

4.1.2.21

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

0

-

4.1.2.21

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

0

-

4.1.2.14

2 entries

4.1.2.21

2 entries

4.1.2.51

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

0

-

4.1.2.55

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

0

-

4.1.2.55

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

0

-

4.1.2.55

2 entries

Substrate in Enzyme-catalyzed Reactions (62 results)

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Show Substrate (62 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

D-glyceraldehyde + NAD+ = ?

745695

-

1.1.1.145

D-glyceraldehyde + NADPH = ?

389394

-

1.1.1.149

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

285998, 285999

-

1.1.1.19

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

286143, 286139

-

1.1.1.2

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

286177, 286178, 286182, 286187, 286196, 286172, 286175, 286181, 286149, 286168, 286176, 286184, 286186, 286199, 286165, 286174, 286192, 286204, 286167, 286171, 286179, 286194

-

1.1.1.21

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

760913

3v36, 3D-view

1.1.1.21

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

286249, 286241, 688043

3v36, 3D-view

1.1.1.21

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

738161

3v36, 3D-view

1.1.1.21

3 entries

1.1.1.372

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

673558

-

1.1.1.431

D-glyceraldehyde + NADH = ?

696083

-

1.1.1.6

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

747295

-

1.1.1.72

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

287287, 287283, 287286, 287288, 287285, 711534, 287284, 711743

-

1.1.3.41

D-glyceraldehyde + O2 = D-glycerate + H2O2

762881

-

1.2.1.13

D-glyceraldehyde + phosphate + NADP+ = D-glyceroylphosphate + NADPH

288005

-

1.2.1.3

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

348707, 722210

-

1.2.1.4

D-glyceraldehyde + NADP+ = D-glycerate + NADPH + H+

762562

-

1.2.1.5

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

722210

-

1.2.1.5

D-glyceraldehyde + NADP+ + H2O = D-glycerate + NADPH

722210

-

1.2.1.89

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

740187

-

1.2.1.89

D-glyceraldehyde + NAD+ = D-glycerate + NADH + H+

736023

-

1.2.1.89

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

736023, 762564, 724216, 724992, 726348

-

1.2.1.5

2 entries

1.2.1.89

3 entries

1.2.1.92

D-glyceraldehyde + NADP+ + H2O = ?

763358

-

1.2.99.8

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

741251

-

1.2.99.8

D-glyceraldehyde + H2O + acceptor = D-glycerate + reduced acceptor

719397

-

1.2.99.8

D-glyceraldehyde + H2O + methyl viologen = D-glycerate + reduced methyl viologen

741251

-

1.2.99.8

3 entries

1.3.1.20

D-glyceraldehyde + NADPH = ?

349237, 349242, 349254, 349243

-

2.2.1.1

D-glyceraldehyde + hydroxypyruvate = D-ribulose + ?

735416

-

2.2.1.1

D-glyceraldehyde + hydroxypyruvate = D-xylulose + CO2

735415

-

2.2.1.2

D-glyceraldehyde + sedoheptulose 7-phosphate = ?

486027, 486031, 486041

-

2.2.1.2

dihydroxypropanone + D-glyceraldehyde = D-fructose

719298

-

2.2.1.1

2 entries

2.2.1.2

2 entries

2.2.1.3

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

486048, 486057

-

2.2.1.7

pyruvate + D-glyceraldehyde = 1-deoxy-D-xylulose + CO2

706051, 395816, 657953, 658834, 395812, 659734

-

2.5.1.54

phosphoenolpyruvate + D-glyceraldehyde = 2-dehydro-3-deoxy-D-threo-hexonate + phosphate

639780

-

2.7.1.28

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

641263, 730035, 758623, 759025, 759363

-

2.7.1.28

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

641261, 641263, 641262

-

2.7.1.28

GTP + D-glyceraldehyde = GDP + D-glyceraldehyde-3-phosphate

641261

-

2.7.1.28

ITP + D-glyceraldehyde = IDP + D-glyceraldehyde-3-phosphate

641261

-

2.7.1.28

4 entries

2.7.1.30

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

641287, 641294, 641295

-

4.1.2.13

2 D-glyceraldehyde = D-fructose

727267

-

4.1.2.13

Glycerone phosphate + D-glyceraldehyde = Fructose 1-phosphate

4964

-

4.1.2.14

2-oxobutyrate + D-glyceraldehyde = ?

586786

-

4.1.2.14

3-fluoropyruvate + D-glyceraldehyde = ?

586786

-

4.1.2.14

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

653924, 726975

-

4.1.2.14

Pyruvate + D-glyceraldehyde = ?

4979

-

4.1.2.17

dihydroxyacetone phosphate + D-glyceraldehyde = D-psicose 1-phosphate

727377

-

4.1.2.17

DL-glycerol 3-phosphate + D-glyceraldehyde = ?

714442

-

4.1.2.17

glycerone phosphate + D-glyceraldehyde = D-psicose 1-phosphate

749339, 5047, 5048, 5049

-

4.1.2.17

glycerone phosphate + D-glyceraldehyde = D-sorbose 1-phosphate

749339

-

4.1.2.17

L-glycerol 3-phosphate + D-glyceraldehyde = ?

714442

-

4.1.2.17

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

727788

-

4.1.2.19

2 glycerone phosphate + 2 D-glyceraldehyde = D-psicose 1-phosphate + D-sorbose 1-phosphate

747271

-

4.1.2.19

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

747271

-

4.1.2.19

glycerone phosphate + D-glyceraldehyde = D-psicose 1-phosphate

749339

-

4.1.2.19

glycerone phosphate + D-glyceraldehyde = D-sorbose 1-phosphate

5049, 5071, 749339, 5066

-

4.1.2.20

Pyruvate + D-glyceraldehyde = ?

4971

1w3t, 3D-view

4.1.2.20

Pyruvate + D-glyceraldehyde = ?

4971

4b5s, 3D-view

4.1.2.13

2 entries

4.1.2.14

4 entries

4.1.2.17

6 entries

4.1.2.19

4 entries

4.1.2.20

2 entries

4.1.2.23

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

33112, 33114

-

4.1.2.55

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

718713, 718771, 715259, 656156, 724729

-

4.1.2.55

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

657872, 718713, 718771, 678020, 715259, 656156, 724729

-

4.1.2.55

pyruvate + D-glyceraldehyde = 3-deoxy-D-erythro-hex-2-ulosonate

718528

-

4.1.2.55

pyruvate + D-glyceraldehyde = 3-deoxy-D-threo-hex-2-ulosonate

718528

-

4.1.2.55

4 entries

5.3.1.5

D-glyceraldehyde = dihydroxyacetone

726953

-

Product in Enzyme-catalyzed Reactions (19 results)

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Show Product (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.6

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

0

-

1.1.1.72

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

0

-

1.1.3.41

glycerol + O2 = D-glyceraldehyde + H2O2

0

-

1.1.5.12

D-glycerate + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = D-glyceraldehyde + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

0

-

2.2.1.11

methylglyoxal + D-fructose 1-phosphate = D-glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate

0

-

3.1.3.23

D-glyceraldehyde 3-phosphate + H2O = D-glyceraldehyde + phosphate

0

-

4.1.2.13

D-Fructose 1-phosphate = Glycerone phosphate + D-glyceraldehyde

0, 649476, 651985, 4902, 652386, 652150, 651313

-

4.1.2.14

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

0

-

4.1.2.14

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

0

-

4.1.2.14

D-2-dehydro-3-deoxygluconate = pyruvate + D-glyceraldehyde

650823

-

4.1.2.14

3 entries

4.1.2.19

L-Sorbose 1-phosphate = Glycerone phosphate + D-glyceraldehyde

0

-

4.1.2.21

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

0

-

4.1.2.21

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

0

-

4.1.2.21

2 entries

4.1.2.23

pyruvate + D-altrose = D-erythrose + D-glyceraldehyde

0, 33114

-

4.1.2.4

2-deoxy-D-ribose = D-glyceraldehyde + acetaldehyde

0

-

4.1.2.51

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

0

-

4.1.2.51

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

0

-

4.1.2.55

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

0

-

4.1.2.55

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

0

-

4.1.2.51

2 entries

4.1.2.55

2 entries

Inhibitor in Enzyme-catalyzed Reactions (7 results)

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Show Inhibitors (7 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.3

substrate inhibition

348707

-

1.2.1.4

substrate inhibition

762562

-

1.2.1.89

slight substrate inhibition, 25% inhibition at 2 mM

724992

-

2.2.1.7

competitive inhibition with respect to pyruvate

719975

-

4.1.2.4

the activity of wild-type enzyme sharply dropps by 43 % under 200 mM D-glyceraldehyde and acetaldehyde, which limits its large-scale synthetic applications

746897

-

4.1.2.54

inhibits reverse reaction with pyruvate and L-glyceraldehyde

722654

-

5.3.1.5

competitive inhibition of the isomerization of D-xylose

726953

-

3D Structure of Enzyme-Ligand-Complex (PDB) (13 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (13 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.21

3v36, 3D-view

3.5.2.6

5tg4, 3D-view

4.1.2.20

1w3t, 3D-view

4.1.2.20

4b5s, 3D-view

4.1.2.20

1w3t, 3D-view

4.1.2.20

4b5s, 3D-view

4.1.2.20

1w3t, 3D-view

4.1.2.20

4b5s, 3D-view

4.1.2.20

1w3t, 3D-view

4.1.2.20

4b5s, 3D-view

4.1.2.20

1w3t, 3D-view

4.1.2.20

4b5s, 3D-view

4.1.2.20

10 entries

5.3.1.6

3kwm, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (29 results)

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Show Turnover Number (29 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.2

14.4

-

-

286165

1.1.1.21

0.55

-

-

286241

1.2.1.5

0.92

-

pH 8, 80°C

722210

1.2.1.89

10

-

pH 6.9, 58°C

724992

1.2.1.89

26

-

pH 6.9, 58°C

724992

1.2.1.89

69.6

-

mutant N286H, pH 7.0, 37°C

740187

1.2.1.89

113.1

-

mutant N286H, pH 7.0, 37°C

740187

1.2.1.89

957

-

mutant N286H, pH 7.0, 37°C

740187

1.2.99.8

0.72

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

3.58

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.99.8

3.78

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.99.8

5.23

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

11.2

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

50.5

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.1.89

5 entries

1.2.99.8

6 entries

1.3.1.20

31.4

-

-

349237

2.2.1.2

0.53

-

mutant F178, pH 8.5, 30°C

719298

2.2.1.7

1.7

-

pH 7.4, 37°C

657953

2.7.1.28

0.16

-

mutant enzyme T112A, at pH 7.5 and 37°C

730035

2.7.1.28

0.74

-

mutant enzyme S446A, at pH 7.5 and 37°C

730035

2.7.1.28

2.09

-

mutant enzyme K204A, at pH 7.5 and 37°C

730035

2.7.1.28

2.27

-

mutant enzyme C404A, at pH 7.5 and 37°C

730035

2.7.1.28

4.83

-

wild type enzyme, at pH 7.5 and 37°C

730035

4.1.2.55

0.06

-

70°C, pH is not specified in the publication, mutant enzyme

715259

4.1.2.55

0.07

-

70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V

715259

4.1.2.55

4.4

-

pH 6.0, 50°C, wild-type enzyme

718713

4.1.2.55

5.5

-

70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V

715259

4.1.2.55

9.9

-

pH 6, 70°C

724729

4.1.2.55

15.7

-

pH 6.0, 50°C, mutant enzyme V193A

718713

2.7.1.28

5 entries

4.1.2.55

6 entries

5.3.1.5

0.0001

-

in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C

726953

K_M Value (61 results)

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Show KM Value (61 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.145

1.07

-

-

389394

1.1.1.149

0.3

0.464

-

285999

1.1.1.149

0.464

-

-

285999

1.1.1.149

0.67

-

-

285998

1.1.1.149

3 entries

1.1.1.19

4.8

-

-

286139

1.1.1.2

0.43

-

AR2

286184

1.1.1.2

4.5

-

-

286172

1.1.1.2

8.2

-

AR3

286184

1.1.1.2

3 entries

1.1.1.21

0.035

-

-

286241

1.1.1.372

0.9

-

at pH 7.0 and 30°C

673558

1.1.1.6

0.07

-

pH and temperature not specified in the publication

747295

1.1.1.72

0.04

-

-

287287

1.1.1.72

0.15

-

-

287286

1.1.1.72

2.69

-

reduction, pH 7.0, 30°C, Vmax: 77.9 micromol/min/mg

711743

1.1.1.72

11.5

-

-

287285

1.1.1.72

12.8

-

reverse reaction, pH 6.5, 25°C, crude extract

739934

1.1.1.72

20.2

-

reverse reaction, pH 6.5, 25°C, crude extract

739934

1.1.1.72

32.3

-

reverse reaction, pH 6.5, 25°C, crude extract

739934

1.1.1.72

7 entries

1.2.1.3

1.136

-

-

348707

1.2.1.5

8.51

-

pH 8, 80°C

722210

1.2.1.89

0.06

-

pH 6.9, 58°C

724992

1.2.1.89

0.2

-

pH 6.9, 58°C

724992

1.2.1.89

0.33

-

pH 8.0, 50°C

724216

1.2.1.89

1.14

-

mutant N286H, pH 7.0, 37°C

740187

1.2.1.89

1.97

-

mutant N286H, pH 7.0, 37°C

740187

1.2.1.89

2.2

-

mutant N286H, pH 7.0, 37°C

740187

1.2.99.8

0.011

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.99.8

0.018

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

0.03

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.99.8

0.091

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.99.8

0.138

-

cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

741251

1.2.99.8

0.63

-

cosubstrate methyl viologen, pH 7.0, 70°C

741251

1.2.1.89

6 entries

1.2.99.8

6 entries

1.3.1.20

45

-

-

349237

2.2.1.1

6

-

at pH 7.2 and 50°C

735416

2.2.1.2

59

-

mutant F178, pH 8.5, 30°C

719298

2.2.1.7

5.6

-

pH 7.9, 37°C

658834

2.2.1.7

10

-

recombinant isoenzyme B

395816

2.2.1.7

14

-

recombinant isoenzyme A

395816

2.2.1.7

33

-

pH 7.4, 37°C

657953

2.2.1.7

35

-

recombinant protein

395812

2.2.1.7

38

-

-

395812

2.2.1.7

6 entries

2.5.1.54

3.5

-

cytosolic isozyme DS-Co, pH 8.6, 37°C

639780

2.7.1.28

0.0071

-

mutant enzyme S446A, at pH 7.5 and 37°C

730035

2.7.1.28

0.008

-

pH 7.5, 23-24°C, cosubstrate 1.0 mM MgATP2-

641263

2.7.1.28

0.012

-

pH 7.5, 23-24°C, cosubstrate 0.5 mM MgATP2-

641263

2.7.1.28

0.0137

-

mutant enzyme T112A, at pH 7.5 and 37°C

730035

2.7.1.28

0.015

-

mutant enzyme K204A, at pH 7.5 and 37°C

730035

2.7.1.28

0.0162

-

mutant enzyme C404A, at pH 7.5 and 37°C

730035

2.7.1.28

0.0181

-

wild type enzyme, at pH 7.5 and 37°C

730035

2.7.1.28

0.019

-

pH 7.5, 23-24°C, cosubstrate 2.0 mM MgATP2-

641263

2.7.1.28

8 entries

4.1.2.17

0.743

-

assay with DL-glyceraldehyde, pH and temperature not specified in the publication

727377

4.1.2.51

4.6

-

pH 6.2, 60°C

704334

4.1.2.55

2.1

-

pH 6.0, 50°C, wild-type enzyme

718713

4.1.2.55

3.9

-

pH 6, 70°C

724729

4.1.2.55

3.9

-

pH 6.0, 70°C

718771

4.1.2.55

5.3

-

70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V

715259

4.1.2.55

5.4

-

pH 6.0, 50°C, mutant enzyme V193A

718713

4.1.2.55

6.3

-

pH 6.0, 70°C

718771

4.1.2.55

8

-

70°C, pH is not specified in the publication, mutant enzyme

715259

4.1.2.55

9.1

-

70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V

715259

4.1.2.55

8 entries

5.3.1.5

3

-

in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C

726953

K_i Value (5 results)

top print hide

Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.3

14.32

-

-

348707

1.2.1.4

1.25

-

pH 7.3, temperature not specified in the publication, wild-type enzyme

762562

1.2.1.4

3.8

-

pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I

762562

1.2.1.4

31.2

-

pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I/W271Y/W275V

762562

1.2.1.4

3 entries

2.2.1.7

3.2

-

pH 8.0, 37°C

719975

References & Links

Literature References (127)

top print hide

Show Reference (127 entries)

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PUBMED ID

TITLE

YEAR

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1972

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1978

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1980

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1980

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1981

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1982

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1982

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1982

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6404249

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1983

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Isolation and characterization of multiforms of aldehyde reductase in chicken kidney

1983

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286186

3922304

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

1985

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3890957

Purification and properties of aldehyde reductases from human placenta

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286194

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

1990

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

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1982

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Pentose metabolism in Candida utilis

1966

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Glycerol dehydrogenase from rabbit muscle

1982

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1991

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1978

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1972

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1967

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1973

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6617882

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1983

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2322424

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1990

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349237

2697716

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

1989

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Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney

1987

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349243

3548826

Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis

1987

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

Biochim. Biophys. Acta

912

270-277

349254

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1994

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116

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Purification and characterization of 5alpha-dihydrotestosterone 3beta-hydroxysteroid dehydrogenase from mature pig testicular cytosol

1994

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17

1155-1160

395812

10648511

Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis

2000

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J. Bacteriol.

182

891-897

395816

11114895

1-Deoxy-D-xylulose 5-phosphate synthase, the gene product of open reading frame (ORF) 2816 and ORF 2895 in Rhodobacter capsulatus

2001

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J. Bacteriol.

183

1-11

486027

-

Transaldolase

1972

Tsolas, O.; Horecker, B.L.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

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259-280

486031

11946741

The forward and reverse reactions of transaldolase

1972

Wood, T.

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486041

7592346

Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains

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486048

2280716

Dihydroxyacetone synthase from Candida boidinii KD1

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

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586786

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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

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

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641261

13093749

Le metabolisme du fructose-1-phosphate dans le foie

1953

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641262

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641263

5139220

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641287

-

Glycerol and glycerate kinases

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The Enzymes,3rd ed. (Boyer,P. D. ,ed. )

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487-508

641294

-

Glycerol kinase

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Thorner, J.W.

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641295

5335908

Purification and properties of glycerol kinase from Escherichia coli

1967

Hayashi, S.; Lin, E.C.C.

J. Biol. Chem.

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1030-1035

649476

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The temperature dependence of activity and structure for the most prevalent mutant aldolase B associated with hereditary fructose intolerance

2002

Malay, A.D.; Procious, S.L.; Tolan, D.R.

Arch. Biochem. Biophys.

408

295-304

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

651313

12417303

Structural and functional analysis of aldolase B mutants related to hereditary fructose intolerance

2002

Esposito, G.; Vitagliano, L.; Santamaria, R.; Viola, A.; Zagari, A.; Salvatore, F.

FEBS Lett.

531

152-156

651985

10625657

Expression, purification, and characterization of natural mutants of human aldolase B. Role of quaternary structure in catalysis

2000

Rellos, P.; Sygusch, J.; Cox, T.M.

J. Biol. Chem.

275

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652150

11387336

Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolase

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J. Biol. Chem.

276

28710-28718

652386

12611890

Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolase

2003

Pezza, J.A.; Choi, K.H.; Berardini, T.Z.; Beernink, P.T.; Allen, K.N.; Tolan, D.R.

J. Biol. Chem.

278

17307-17313

653924

11342129

Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli

2001

Wymer, N.; Buchanan, L.V.; Henderson, D.; Mehta, N.; Botting, C.H.; Pocivavsek, L.; Fierke, C.A.; Toone, E.J.; Naismith, J.H.

Structure

9

1-9

656156

12824170

Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase

2003

Lamble, H.J.; Heyer, N.I.; Bull, S.D.; Hough, D.W.; Danson, M.J.

J. Biol. Chem.

278

34066-34072

657872

15869466

The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation

2005

Ahmed, H.; Ettema, T.J.; Tjaden, B.; Geerling, A.C.; van der Oost, J.; Siebers, B.

Biochem. J.

390

529-540

657953

12549936

Rhodobacter capsulatus 1-deoxy-D-xylulose 5-phosphate synthase: steady-state kinetics and substrate binding

2003

Eubanks, L.M.; Poulter, C.D.

Biochemistry

42

1140-1149

658834

12499403

Identification, cloning, purification, and enzymatic characterization of Mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate synthase

2002

Bailey, A.M.; Mahapatra, S.; Brennan, P.J.; Crick, D.C.

Glycobiology

12

813-820

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

673558

16930134

Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina

2006

Liepins, J.; Kuorelahti, S.; Penttilae, M.; Richard, P.

FEBS J.

273

4229-4235

678020

10527934

An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates

1999

Buchanan, C.L.; Connaris, H.; Danson, M.J.; Reeve, C.D.; Hough, D.W.

Biochem. J.

343

563-570

688043

18569331

In vitro aldose reductase inhibitory activity of some flavonyl-2,4-thiazolidinediones

2008

Das-Evcimen, N.; Bozdag-Dundar, O.; Sarikaya, M.; Ertan, R.

J. Enzyme Inhib. Med. Chem.

23

297-301

696083

16336198

Probing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis

2006

Kratzer, R.; Leitgeb, S.; Wilson, D.K.; Nidetzky, B.

Biochem. J.

393

51-58

704334

20023024

The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-specific aldolase

2010

Reher, M.; Fuhrer, T.; Bott, M.; Schoenheit, P.

J. Bacteriol.

192

964-974

706051

19778006

Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase

2009

Brammer, L.A.; Meyers, C.F.

Org. Lett.

11

4748-4751

711534

20198657

Characterization of a whole-cell catalyst co-expressing glycerol dehydrogenase and glucose dehydrogenase and its application in the synthesis of L-glyceraldehyde

2010

Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Weckbecker, A.; Eggert, T.; Hummel, W.

Biotechnol. Bioeng.

106

541-552

711743

19579248

Characterisation of a recombinant NADP-dependent glycerol dehydrogenase from Gluconobacter oxydans and its application in the production of L-glyceraldehyde

2009

Richter, N.; Neumann, M.; Liese, A.; Wohlgemuth, R.; Eggert, T.; Hummel, W.

ChemBioChem

10

1888-1896

714442

21482110

Synthesis of rare sugars with l-fuculose-1-phosphate aldolase (FucA) from Thermus thermophilus HB8

2011

Li, Z.; Cai, L.; Qi, Q.; Styslinger, T.J.; Zhao, G.; Wang, P.G.

Bioorg. Med. Chem. Lett.

21

5084-5087

715259

20684556

Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts

2010

Royer, S.F.; Haslett, L.; Crennell, S.J.; Hough, D.W.; Danson, M.J.; Bull, S.D.

J. Am. Chem. Soc.

132

11753-11758

718528

-

A thermostable aldolase for the synthesis of 3-deoxy-2-ulosonic acids

2007

Lamble, H.J.; Royer, S.F.; Hough, D.W.; Danson, M.J.; Taylor, G.L.; Bull, S.D.

Adv. Synth. Catal.

349

817-821

718713

19478916

Improving low-temperature activity of Sulfolobus acidocaldarius 2-keto-3-deoxygluconate aldolase

2009

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Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates

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NADP+-dependent dehydrogenase SCO3486 and cycloisomerase SCO3480 key enzymes for 3,6-anhydro-L-galactose catabolism in Streptomyces coelicolor A3(2)

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Links to other databases for D-glyceraldehyde

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