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Ligand glyceraldehyde 3-phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

KEGG

Biosynthesis of alkaloids derived from histidine and purine, Biosynthesis of alkaloids derived from ornithine, lysine and nicotinic acid, Biosynthesis of alkaloids derived from shikimate pathway, Biosynthesis of alkaloids derived from terpenoid and polyketide, Biosynthesis of amino acids, Biosynthesis of cofactors, Biosynthesis of phenylpropanoids, Biosynthesis of plant hormones, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Biosynthesis of terpenoids and steroids, Carbon fixation in photosynthetic organisms, Carbon metabolism, Clavulanic acid biosynthesis, Diabetic cardiomyopathy, Fructose and mannose metabolism, Galactose metabolism, Glycolysis / Gluconeogenesis, Inositol phosphate metabolism, Methane metabolism, Microbial metabolism in diverse environments, Pentose phosphate pathway, Terpenoid backbone biosynthesis, Thiamine metabolism, Vitamin B6 metabolism more

MetaCyc

1,3-propanediol biosynthesis (engineered), 2-deoxy-alpha-D-ribose 1-phosphate degradation, 2-deoxy-D-ribose degradation I, 3,6-anhydro-alpha-L-galactopyranose degradation, 3-dehydroquinate biosynthesis II (archaea), 4-deoxy-L-threo-hex-4-enopyranuronate degradation, arsenate detoxification V, Bifidobacterium shunt, Calvin-Benson-Bassham cycle, clavulanate biosynthesis, D-apiose degradation I, D-fructuronate degradation, D-galactonate degradation, D-galactosamine and N-acetyl-D-galactosamine degradation, D-galacturonate degradation I, D-glucosaminate degradation, D-tagatose degradation, DIBOA-glucoside biosynthesis, Entner-Doudoroff pathway I, Entner-Doudoroff pathway III (semi-phosphorylative), Entner-Doudoroff shunt, formaldehyde assimilation II (assimilatory RuMP Cycle), formaldehyde assimilation III (dihydroxyacetone cycle), galactitol degradation, gluconeogenesis I, gluconeogenesis II (Methanobacterium thermoautotrophicum), gluconeogenesis III, glycerol degradation to butanol, glycolysis I (from glucose 6-phosphate), glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), glycolysis IV, glycolysis V (Pyrococcus), heterolactic fermentation, L-glucose degradation, L-tryptophan biosynthesis, lactate biosynthesis (archaea), lactose and galactose degradation I, lincomycin A biosynthesis, methanofuran biosynthesis, methylerythritol phosphate pathway I, methylerythritol phosphate pathway II, N-acetyl-D-galactosamine degradation, paspaline biosynthesis, pentose phosphate pathway (non-oxidative branch) I, pentose phosphate pathway (non-oxidative branch) II, pentose phosphate pathway (partial), pyridoxal 5'-phosphate biosynthesis I, pyridoxal 5'-phosphate biosynthesis II, rifamycin B biosynthesis, Rubisco shunt, sucrose biosynthesis I (from photosynthesis), sucrose degradation V (sucrose alpha-glucosidase), sulfoquinovose degradation III, sulfoquinovose degradation V, superpathway of glucose and xylose degradation, thiazole component of thiamine diphosphate biosynthesis I, thiazole component of thiamine diphosphate biosynthesis II more

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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

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

725013

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

725013

-

1.2.1.13

2 entries

1.2.1.9

DL-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-DL-glycerate + NADPH + H+

726000

-

2.2.1.1

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

735708

-

In Vivo Product in Enzyme-catalyzed Reactions (28 results)

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Show Natural Product (28 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = DL-glyceraldehyde 3-phosphate + phosphate + NADP+

0

-

2.2.1.3

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

0, 486046, 486049, 486051, 486050, 486052, 486048, 486047

-

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

7v6f, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

7v6f, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

7v6f, 3D-view

4.1.2.13

24 entries

4.1.2.8

indole-3-glycerol phosphate = indole + glyceraldehyde 3-phosphate

0

-

4.2.1.20

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O

0

2clk, 3D-view

Substrate in Enzyme-catalyzed Reactions (43 results)

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Show Substrate (43 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.149

DL-glyceraldehyde 3-phosphate + NADPH + H+ = glycerol 3-phosphate + NADP+

285999

-

1.1.1.95

DL-glyceraldehyde 3-phosphate + NAD+ = ?

684698

-

1.1.5.3

glyceraldehyde-3-phosphate + NAD(P)+ = ?

689802

-

1.17.3.2

glyceraldehyde-3-phosphate + H2O + O2 = ?

644655

-

1.2.1.107

DL-glyceraldehyde 3-phosphate + arsenate + NAD+ = 1-arsono-3-phospho-D-glycerate + NADH + H+

760549

-

1.2.1.12

arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?

657393

1nqa, 3D-view

1.2.1.12

arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?

657393

1nqo, 3D-view

1.2.1.12

arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?

657393

3cif, 3D-view

1.2.1.12

arsenate + GSH + NAD+ + glyceraldehyde 3-phosphate = arsenite + ?

657393

3lc2, 3D-view

1.2.1.12

glyceraldehyde 3-phosphate + NAD+ = ? + NADH

688953

1nqa, 3D-view

1.2.1.12

glyceraldehyde 3-phosphate + NAD+ = ? + NADH

688953

1nqo, 3D-view

1.2.1.12

glyceraldehyde 3-phosphate + NAD+ = ? + NADH

688953

3cif, 3D-view

1.2.1.12

glyceraldehyde 3-phosphate + NAD+ = ? + NADH

688953

3lc2, 3D-view

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+

725013

-

1.2.1.13

DL-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+

725013

-

1.2.1.3

DL-glyceraldehyde 3-phosphate + NAD+ + H2O = DL-glycerate 3-phosphate + NADH + H+

722210

-

1.2.1.3

glyceraldehyde 3-phosphate + NAD+ + H2O = ?

743680

4i3w, 3D-view

1.2.1.3

glyceraldehyde 3-phosphate + NAD+ + H2O = glycerate 3-phosphate + NADH

348708

4i3w, 3D-view

1.2.1.3

glyceraldehyde-3-phosphate + NAD+ + H2O = ?

729577

4i3w, 3D-view

1.2.1.12

8 entries

1.2.1.13

2 entries

1.2.1.3

4 entries

1.2.1.88

glyceralaldehyde-3-phosphate + NAD+ + H2O = glycerate-3-phosphate + NADH

392065

-

1.2.1.9

DL-glyceraldehyde 3-phosphate + NAD+ + H2O = 3-phospho-DL-glycerate + NADH + H+

679719

-

1.2.1.9

DL-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + H+

679719

-

1.2.1.9

DL-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-DL-glycerate + NADPH + H+

726000, 679719

-

1.2.1.9

3 entries

1.2.7.5

glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin = glycerate 3-phosphate + H+ + reduced ferredoxin

763266

-

1.2.7.6

glyceraldehyde 3-phosphate + H2O + oxidized ferredoxin = glycerate 3-phosphate + H+ + reduced ferredoxin

763266

-

1.2.99.8

glyceraldehyde-3-phosphate + 2,6-dichlorophenolindophenol + H2O = 3-phospho-D-glycerate + reduced 2,6-dichlorophenolindophenol

719397

-

1.20.4.1

arsenate + reduced glutathione + NAD+ + glyceraldehyde-3-phosphate = arsenite + glutathione + ?

677207

-

1.3.1.20

DL-glyceraldehyde-3-phosphate + NADPH = ?

349237

-

2.2.1.1

DL-glyceraldehyde 3-phosphate + ? = ?

486023, 486026

-

2.2.1.1

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

735708

-

2.2.1.1

2 entries

2.2.1.2

dihydroxypropanone + glyceraldehyde 3-phosphate = D-fructose 6-phosphate

719298

-

2.2.1.7

pyruvate + DL-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2

286425, 395813

-

2.2.1.7

pyruvate + glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2

699265

-

2.2.1.7

2 entries

2.5.1.54

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

637421, 639780

-

3.1.3.11

glyceraldehyde 3-phosphate + H2O = ?

747723

-

3.1.3.18

glyceraldehyde-3-phosphate + H2O = glyceraldehyde + phosphate

750563

-

3.1.3.2

glyceraldehyde 3-phosphate + H2O = glyceraldehyde + phosphate

134706, 134800, 134768

-

4.1.2.14

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

650823

-

4.1.2.4

Glyceraldehyde phosphate + acetaldehyde = Hydroxyacetaldehyde + glyceraldehyde 3-phosphate

5170

-

4.3.3.6

D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate

726499, 726269, 724999

-

4.3.3.6

D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+ = pyridoxal 5'-phosphate + 4 H2O + phosphate

724239, 723192, 726499, 724999

-

4.3.3.6

ribulose 5-phosphate + glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate

721233

-

4.3.3.6

ribulose 5-phosphate + glyceraldehyde 3-phosphate + NH4+ = pyridoxal 5'-phosphate + 4 H2O + phosphate

724219

-

4.3.3.6

4 entries

Product in Enzyme-catalyzed Reactions (58 results)

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Show Product (58 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.13

3-phospho-D-glyceroyl phosphate + NADPH + H+ = DL-glyceraldehyde 3-phosphate + phosphate + NADP+

0

-

2.2.1.1

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

0

-

2.2.1.1

ribulose 5-phosphate + ribose 5-phosphate = a heptulose phosphate + glyceraldehyde 3-phosphate

0

-

2.2.1.2

D-fructose 6-phosphate + D-erythrose 4-phosphate = glyceraldehyde 3-phosphate + ?

0

-

2.2.1.2

D-fructose 6-phosphate + erythrose 4-phosphate = sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate

0

-

2.2.1.3

acetaldehyde + D-xylulose 5-phosphate = glyceraldehyde 3-phosphate + 1,3-dihydroxybutane-2-one

0

-

2.2.1.3

D-erythrose 4-phosphate + D-xylulose 5-phosphate = D-fructose 6-phosphate + glyceraldehyde 3-phosphate

0

-

2.2.1.3

D-xylulose 5-phosphate + butyraldehyde = glyceraldehyde 3-phosphate + 1,3-dihydroxyhexane-2-one

0

-

2.2.1.3

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

0

-

2.2.1.3

D-xylulose 5-phosphate + D-glucose = glyceraldehyde 3-phosphate + D-glycero-D-ido-oct-2-ulose

0

-

2.2.1.3

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

0

-

2.2.1.3

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

0

-

2.2.1.3

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

0, 486046, 486048, 486049, 486051, 486052, 486050, 486047

-

2.2.1.3

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

0

-

2.2.1.3

D-xylulose 5-phosphate + heptaldehyde = glyceraldehyde 3-phosphate + 1,3-dihydroxynonane-2-one

0

-

2.2.1.3

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

0

-

2.2.1.3

D-xylulose 5-phosphate + ribose 5-phosphate = glyceraldehyde 3-phosphate + sedoheptulose 7-phosphate

0

-

2.2.1.3

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

0

-

2.2.1.3

ribulose 5-phosphate + formaldehyde = glyceraldehyde 3-phosphate + 1,3-dihydroxyacetone

0

-

2.7.1.29

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

0

-

2.7.1.29

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

0

-

2.7.1.29

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

641267, 641268

1uod, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde 3-phosphate

0

7v6f, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose 1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

7v6f, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = dihydroxyacetone phosphate + glyceraldehyde-3-phosphate

0

7v6f, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

3qrh, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tk3, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tkc, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5tkl, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5uck, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5ucp, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

5ud0, 3D-view

4.1.2.13

D-fructose-1,6-bisphosphate = glyceraldehyde-3-phosphate + dihydroxyacetone phosphate

0

7v6f, 3D-view

2.2.1.1

2 entries

2.2.1.2

2 entries

2.2.1.3

14 entries

2.7.1.29

3 entries

4.1.2.13

32 entries

4.1.2.20

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + glyceraldehyde-3-phosphate

0

-

4.1.2.4

Glyceraldehyde phosphate + acetaldehyde = Hydroxyacetaldehyde + glyceraldehyde 3-phosphate

0

6z9i, 3D-view

4.1.2.8

indole-3-glycerol phosphate = indole + glyceraldehyde 3-phosphate

0

-

4.2.1.20

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O

0

2clk, 3D-view

Activator in Enzyme-catalyzed Reactions (10 results)

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Show Activating Compound (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.19

activation

641030

-

2.7.1.40

activation

641516, 641556

-

2.7.1.40

not

641589

-

2.7.1.40

requirement with Mg2+

641556

-

2.7.1.40

with Mn2+

641556

-

2.7.1.40

4 entries

2.7.1.63

slight activation

761859

-

2.7.7.27

-

643144

-

2.7.7.27

less effective than fructose bisphosphate

643144

-

2.7.7.27

no activation

643120, 643135

-

2.7.7.27

slight activation

643134, 643123

-

2.7.7.27

4 entries

Inhibitor in Enzyme-catalyzed Reactions (41 results)

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Show Inhibitors (41 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.42

-

286796

-

1.1.1.49

-

286987

-

1.1.5.3

-

287806

-

1.1.5.3

about 80% inhibition at 2.5 mM, glyceraldehyde 3-phosphate is not a specific inhibitor of mGPDH but also alters succinate oxidation

741302

-

1.1.5.3

D-3-glyceraldehyde phosphate; L-3-glyceraldehyde phosphate

287802

-

1.1.5.3

competitive inhibitor

689802

-

1.1.5.3

4 entries

1.2.1.13

-

725013

-

1.2.1.23

strong inhibitor

288141

-

1.2.7.6

substrate inhibition above 0.5 mM

644692

-

2.1.1.45

-

485399

-

2.6.1.16

50% inhibition at 0.2 mM

639912

-

2.7.2.1

inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2; inhibits the activities of isozyme AckA1, but very poorly of isozyme AckA2

738528

-

2.7.4.3

-

642578

-

2.7.6.1

14% inhibition at 1 mM

642717

-

2.7.6.1

no inhibition

642735

-

2.7.9.2

-

645472

-

2.7.9.2

weak

645473

-

2.7.6.1

2 entries

2.7.9.2

2 entries

3.1.3.60

competitive

646421

-

4.1.2.13

-

4943

3qrh, 3D-view

4.1.2.13

-

4943

5tk3, 3D-view

4.1.2.13

-

4943

5tkc, 3D-view

4.1.2.13

-

4943

5tkl, 3D-view

4.1.2.13

-

4943

5uck, 3D-view

4.1.2.13

-

4943

5ucp, 3D-view

4.1.2.13

-

4943

5ud0, 3D-view

4.1.2.13

-

4943

7v6f, 3D-view

4.1.2.13

non-competitive inhibitor

652787

3qrh, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5tk3, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5tkc, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5tkl, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5uck, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5ucp, 3D-view

4.1.2.13

non-competitive inhibitor

652787

5ud0, 3D-view

4.1.2.13

non-competitive inhibitor

652787

7v6f, 3D-view

4.1.2.13

16 entries

4.1.2.9

-

37327

-

4.2.3.3

-

137612

-

5.3.1.6

competitive

2792

-

5.3.1.9

-

2867

-

6.2.1.1

weak

560

-

6.3.2.26

reacts with L-cysteinee

440078

-

6.3.4.21

at 1 mM 27% inhibition of activity (concentrations of substrates 1 mM)

721763

-

3D Structure of Enzyme-Ligand-Complex (PDB) (52 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (52 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.8

1z82, 3D-view

1.2.1.12

1nqa, 3D-view

1.2.1.12

1nqo, 3D-view

1.2.1.12

3cif, 3D-view

1.2.1.12

3lc2, 3D-view

1.2.1.12

1nqa, 3D-view

1.2.1.12

1nqo, 3D-view

1.2.1.12

3cif, 3D-view

1.2.1.12

3lc2, 3D-view

1.2.1.12

8 entries

1.2.1.3

4i3w, 3D-view

1.2.1.9

1qi1, 3D-view

1.2.1.9

1uxu, 3D-view

1.2.1.9

2esd, 3D-view

1.2.1.9

2qe0, 3D-view

1.2.1.9

1qi1, 3D-view

1.2.1.9

1uxu, 3D-view

1.2.1.9

2esd, 3D-view

1.2.1.9

2qe0, 3D-view

1.2.1.9

8 entries

2.7.1.29

1uod, 3D-view

2.7.1.30

1glc, 3D-view

2.7.1.30

1gld, 3D-view

2.7.1.30

1gle, 3D-view

2.7.1.30

1glc, 3D-view

2.7.1.30

1gld, 3D-view

2.7.1.30

1gle, 3D-view

2.7.1.69

1glc, 3D-view

2.7.1.69

1gld, 3D-view

2.7.1.69

1gle, 3D-view

2.7.1.69

1glc, 3D-view

2.7.1.69

1gld, 3D-view

2.7.1.69

1gle, 3D-view

2.7.1.30

6 entries

2.7.1.69

6 entries

3.1.3.46

1c7z, 3D-view

4.1.2.13

3qrh, 3D-view

4.1.2.13

5tk3, 3D-view

4.1.2.13

5tkc, 3D-view

4.1.2.13

5tkl, 3D-view

4.1.2.13

5uck, 3D-view

4.1.2.13

5ucp, 3D-view

4.1.2.13

5ud0, 3D-view

4.1.2.13

7v6f, 3D-view

4.1.2.13

3qrh, 3D-view

4.1.2.13

5tk3, 3D-view

4.1.2.13

5tkc, 3D-view

4.1.2.13

5tkl, 3D-view

4.1.2.13

5uck, 3D-view

4.1.2.13

5ucp, 3D-view

4.1.2.13

5ud0, 3D-view

4.1.2.13

7v6f, 3D-view

4.1.2.13

16 entries

4.1.2.4

6z9i, 3D-view

4.1.2.40

5ff7, 3D-view

4.2.1.20

2clk, 3D-view

5.3.1.1

1m7p, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.2.1.3

0.098

-

wild type enzyme, at pH 7.5 and 30°C

743680

1.2.1.3

0.28

-

-

348708

1.2.1.3

0.83

-

in 50 mM Tris/HCl, at pH 8.0 and 80°C

722210

1.2.1.3

3 entries

1.3.1.20

8

-

-

349237

2.2.1.2

12

-

mutant F178, pH 8.5, 30°C

719298

2.2.1.2

13

-

wild-type, pH 8.5, 30°C

719298

2.2.1.2

2 entries

K_M Value (31 results)

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Show KM Value (31 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.149

0.852

1.3

-

285999

1.1.1.149

1.3

-

-

285999

1.1.1.149

2 entries

1.17.3.2

2

-

-

644655

1.2.1.13

0.21

-

wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C

725013

1.2.1.13

0.77

-

wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C

725013

1.2.1.3

0.097

-

wild type enzyme, at pH 7.5 and 30°C

743680

1.2.1.3

0.372

-

-

348708

1.2.1.3

6.12

-

in 50 mM Tris/HCl, at pH 8.0 and 80°C

722210

1.2.1.9

0.501

-

in the presence of D-glucose 1-phosphate

679719

1.2.1.9

0.51

-

70°C, pH 7

679719

1.2.1.9

0.51

-

in the absence of D-glucose 1-phosphate

679719

1.2.1.13

2 entries

1.2.1.3

3 entries

1.2.1.9

3 entries

1.3.1.20

50

-

-

349237

2.2.1.1

2.1

-

-

486023, 486026

2.2.1.1

4.9

-

-

486026

2.2.1.2

0.038

-

-

486041

2.2.1.2

0.072

-

-

486030

2.2.1.2

0.22

-

-

486027

2.2.1.2

1.9

-

wild-type, pH 8.5, 30°C

719298

2.2.1.2

2.4

-

mutant F178, pH 8.5, 30°C

719298

2.2.1.1

2 entries

2.2.1.2

5 entries

2.2.1.3

0.42

-

-

486047

2.5.1.54

3

-

cytosolic isozyme DS-Co, pH 8.6, 37°C

639780

3.1.3.2

0.21

-

-

134800

4.3.3.6

0.155

-

pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C

726269

4.3.3.6

0.186

-

pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C

726269

4.3.3.6

0.195

-

pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.22

-

pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.229

-

pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.249

-

pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.262

-

pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.267

-

pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

0.307

-

pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C

726269

4.3.3.6

9 entries

K_i Value (4 results)

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Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.13

2.8

-

wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C

725013

1.2.1.13

13.1

-

wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C

725013

1.2.1.13

2 entries

2.1.1.45

12

-

-

485399

2.7.2.1

4

-

pH 7.5, 30°C, recombinant His-tagged isozyme AckA1

738528

References & Links

Literature References (89)

top print hide

Show Reference (89 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

560

12800

Characterization of the acetyl-CoA synthetase of Acetobacter aceti

1976

O'Sullivan, J.; Ettlinger, L.

Biochim. Biophys. Acta

450

410-417

2792

16668459

Purification and characterization of pea chloroplastic phosphoriboseisomerase

1991

Skrukrud, C.L.; Gordon, I.M.; Dorwin, S.; Yuan, X.H.; Johansson, G.; Anderson, L.E.

Plant Physiol.

97

730-735

2867

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Competitive inhibition of spinach leaf phosphoglucose isomerase isoenzymes by erythrose 4-phosphate

1997

Backhausen, J.E.; Jöstingmeyer, P.; Scheibe, R.

Plant Sci.

130

121-131

4943

7872790

Properties of fructose-1,6-bisphosphate aldolase from Escherichia coli: an NMR analysis

1995

Szwergold, B.S.; Ugurbil, K.; Brown, T.R.

Arch. Biochem. Biophys.

317

244-252

5170

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Deoxyribose 5-phosphate aldolase. I. Lactobacillus plantarum

1966

Hoffee, P.; Rosen, O.M.; Horecker, B.L.

Methods Enzymol.

9

545-549

37327

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Phosphoketolase

1966

Goldberg, M.; Fessenden, J.M.; Racker, E.

Methods Enzymol.

9

515-520

134706

16665451

Purification and properties of acid phosphatase-1 from a nematode resistant tomato cultivar

1987

Paul, E.M.; Williamson, V.M.

Plant Physiol.

84

399-403

134768

4975746

Staphylococcal acid phosphatase: preliminary physical and chemical characterization of the loosely bound enzyme

1969

Malveaux, F.J.; San Clemente, C.L.

J. Bacteriol.

97

1215-1219

134800

1897950

Purification, characterization, and subcellular localization of an acid phosphatase from black mustard cell-suspension cultures: comparison with phosphoenolpyruvate phosphatase

1991

Duff, S.M.G.; Lefebvre, D.D.; Plaxton, W.C.

Arch. Biochem. Biophys.

286

226-232

137612

3899111

Characterization of methylglyoxal synthase in Saccharomyces cerevisiae

1985

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

Biochem. Biophys. Res. Commun.

131

190-198

285999

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

1995

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

Adv. Exp. Med. Biol.

372

249-258

286425

11034300

Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa

2000

Altincicek, B.; Hintz, M.; Sanderbrand, S.; Wiesner, J.; Beck, E.; Jomaa, H.

FEMS Microbiol. Lett.

190

329-333

286796

3337829

Purification and characterization of NADP+-linked isocitrate dehydrogenase from an alkalophilic Bacillus

1988

Shikata, S.; Ozaki, K.; Kawai, S.; Ito, S.; Okamoto, K.

Biochim. Biophys. Acta

952

282-289

286987

31936

Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii

1979

Kato, N.; Sahm, H.; Schutte, H.; Wagner, F.

Biochim. Biophys. Acta

566

1-11

287802

-

L-3-Glycerophosphate dehydrogenase from pig brain mitochondria

1978

Dawson, A.P.; Thorne, C.J.R.

Methods Enzymol.

41B

254-259

287806

6796038

Purification and properties of L-3-glycerophosphate dehydrogenase from pig brain mitochondria

1980

Cottingham, I.R.; Ragan, C.I.

Biochem. J.

192

9-18

288141

7107626

On the interaction of nucleotides and glycolytic intermediates with NAD-linked alpha-ketoaldehyde dehydrogenase

1982

Ray, M.; Ray, S.

J. Biol. Chem.

257

10571-10574

348708

6651766

Bovine lens aldehyde dehydrogenase. Kinetics and mechanism

1983

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

Biochem. J.

215

361-368

349237

2697716

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

1989

Nakagawa, M.; Matsuura, K.; Hara, A.; Sawada, H.; Bunai, H.; Ohya, I.

J. Biochem.

106

1104-1109

392065

9418013

Enzymes of DELTA1-pyrroline-5-carboxylate metabolism in the camel tick Hyalomma dromedarii during embryogenesis. Purification and characterization of DELTA1-pyrroline-5-carboxylate dehydrogenases

1997

Fahmy, A.S.; Mohamed, S.A.; Girgis, R.B.; Abdel-Ghaffar, F.A.

Comp. Biochem. Physiol. B

118

229-237

395813

9482846

Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis

1998

Lois, L.M.; Campos, N.; Putra, S.R.; Danielsen, K.; Rohmer, M.; Boronat, A.

Proc. Natl. Acad. Sci. USA

95

2105-2110

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

485399

1907578

Inhibition of thymidylate synthase by glyceraldehyde 3-phosphate

1991

Bures, A.K.; Daron, H.H.; Aull, J.L.

Int. J. Biochem.

23

733-736

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

486026

9924800

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

1998

Schenk, G.; Duggleby, R.G.; Nixon, P.F.

Int. J. Biochem. Cell Biol.

30

1297-1318

486027

-

Transaldolase

1972

Tsolas, O.; Horecker, B.L.

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

7

259-280

486030

-

Partial purification and kinetic characterization of transaldolase from Dictyostelium discoideum

1991

Albe, K.R.

Exp. Mycol.

15

255-262

486041

7592346

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

1995

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

J. Bacteriol.

177

5930-5936

486046

6276498

The interrelation between transketolase and dihydroxyacetone synthase activities in the methylotrophic yeast Candida boidinii

1981

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

J. Gen. Microbiol.

124

309-316

486047

7074134

Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilizing yeast, candida boidinii (Kloeckera sp.) No. 2201

1982

Kato, N.; Higuchi, T.; Sakazawa, C.; Nishizawa, T.; Tani, Y.; Yamada, H.

Biochim. Biophys. Acta

715

143-150

486048

2280716

Dihydroxyacetone synthase from Candida boidinii KD1

1990

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

Methods Enzymol.

188

435-445

486049

-

Pentose phosphate-dependent fixation of formaldehyde by methanol-grown Hansenula polymorpha and Candida boidinii

1980

O'Connor, M.L.; Quayle, J.R.

J. Gen. Microbiol.

120

219-225

486050

-

Purification and properties of dihydroxyacetone synthase from methylotrophic yeast Candida boidinii

1981

Bystrykh, L.V.; Sokolov, A.P.; Trotsenko, Y.A.

FEBS Lett.

132

324-328

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

486052

3997860

Dihydroxyacetone synthase is an abundant constituent of the methanol-induced peroxisome of Candida boidinii

1985

Goodman, J.M.

J. Biol. Chem.

260

7108-7113

637421

12718525

Mechanistic insight into 3-deoxy-D-manno-octulosonate-8-phosphate synthase and 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase utilizing phosphorylated monosaccharide analogues

2003

Howe, D.L.; Sundaram, A.K.; Wu, J.; Gatti, D.L.; Woodard, R.W.

Biochemistry

42

4843-4854

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.

84

351-360

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

641030

5079073

Properties of phosphoribulokinase from Thiobacillus neapolitanus

1972

MacElroy, R.D.; Mack, H.M.; Johnson, E.J.

J. Bacteriol.

112

532-538

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

641516

-

Purification and characteization of pyruvate kinase from the green alga Chlamydomonas reinhardtii

1992

Wu, H.B.; Turpin, D.H.

J. Phycol.

28

472-481

641556

-

Pyruvate kinase from Streptococcus lactis

1982

Crow, V.L.; Pritchard, G.G.

Methods Enzymol.

90

165-170

641589

7054143

Purification and properties of pyruvate kinase from Streptococcus mutans

1982

Abe, K.; Yamada, T.

J. Bacteriol.

149

299-305

642578

-

Some properties of adenylate kinase from chemolithotropically grown Thiobacillus novellus

1980

McKellar, I.R.C.; Charles, A.M.; Butler, B.J.

Arch. Microbiol.

124

275-284

642717

4335863

Human phosphoribosylpyrophosphate synthetase. Kinetic mechanism and end product inhibition

1972

Fox, I.H.; Kelley, W.N.

J. Biol. Chem.

247

2126-2131

642735

12223847

Purification and characterization of phosphoribosylpyrophosphate synthetase from rubber tree latex

1997

Gallois, R.; Prevot, J.C.; Clement, A.; Jacob, J.L.

Plant Physiol.

115

847-852

643120

16665182

Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm

1987

Plaxton, W.C.; Preiss, J.

Plant Physiol.

83

105-112

643123

16668507

Regulatiory and structural properties of the cyanobacterial ADPglucose pyrophophorylases

1991

Iglesias, A.A.; Kakefuda, G.; Preiss, J.

Plant Physiol.

97

1187-1195

643134

6156933

Biosynthesis of bacterial glycogen: purification and properties of Salmonella typhimurium LT-2 adenosine diphosphate glucose pyrophosphorylase

1980

Lehmann, M.; Preiss, J.

J. Bacteriol.

143

120-127

643135

6432

Kinetic properties of Serratia marcescens adenosine 5-diphosphate glucose pyrophosphorylase

1976

Preiss, J.; Crawford, K.; Downey, J.; Lammel, C.; Greenberg, E.

J. Bacteriol.

127

193-203

643144

345767

Regulation of adenosine diphosphate glucose pyrophosphorylase

1978

Preiss, J.

Adv. Enzymol. Relat. Areas Mol. Biol.

46

317-381

644655

6687810

Studies on the specificity toward aldehyde substrates and steady-state kinetics of xanthine oxidase

1983

Morpeth, F.F.

Biochim. Biophys. Acta

744

328-334

644692

7721730

Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus

1995

Mukund, S.; Adams, M.W.

J. Biol. Chem.

270

8389-8392

645472

-

Phosphoenolpyruvate synthetase and pyruvate, phosphate dikinase

1974

Cooper, R.A.; Kornberg, H.L.

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

10

631-649

645473

4572511

Phosphoenolpyruvate synthetase from Escherichia coli. Effects of adenylate energy charge and modifier concentrations

1973

Chulavatnatol, M.; Atkinson, D.E.

J. Biol. Chem.

248

2712-2715

646421

16666836

Purification and characterization of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells

1989

Duff, S.M.G.; Lefebvre, D.D.; Plaxton, W.C.

Plant Physiol.

90

734-741

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

652787

9878448

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Links to other databases for glyceraldehyde 3-phosphate

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