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Ligand D-erythrose 4-phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

chorismate metabolism, pentose phosphate pathway, photosynthesis, vitamin B12 metabolism, vitamin B6 metabolism

KEGG

Biosynthesis of alkaloids derived from shikimate pathway, 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 various antibiotics, Biosynthesis of various other secondary metabolites, Carbon fixation in photosynthetic organisms, Carbon metabolism, Microbial metabolism in diverse environments, Pentose phosphate pathway, Phenylalanine, tyrosine and tryptophan biosynthesis, Vitamin B6 metabolism more

MetaCyc

3-dehydroquinate biosynthesis I, 5,6-dimethylbenzimidazole biosynthesis I (aerobic), Bifidobacterium shunt, Calvin-Benson-Bassham cycle, D-apionate degradation I (xylose isomerase family decarboxylase), D-apionate degradation II (RLP decarboxylase), D-threitol degradation, erythritol biosynthesis I, erythritol biosynthesis II, erythritol degradation I, erythritol degradation II, formaldehyde assimilation II (assimilatory RuMP Cycle), formaldehyde assimilation III (dihydroxyacetone cycle), L-threitol degradation, lincomycin A biosynthesis, pentose phosphate pathway (non-oxidative branch) I, pentose phosphate pathway (non-oxidative branch) II, pentose phosphate pathway (partial), pyridoxal 5'-phosphate biosynthesis I, Rubisco shunt, sedoheptulose bisphosphate bypass, superpathway of glucose and xylose degradation more

Show all BRENDA pathways known for D-erythrose 4-phosphate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Natural Substrate (11 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.72

D-erythrose 4-phosphate + NAD+ = 4-phosphoerythronate + NADH

661984

-

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

1ngs, 3D-view

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

5xps, 3D-view

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

5xu9, 3D-view

2.2.1.1

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

756489

1ngs, 3D-view

2.2.1.1

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

756489

5xps, 3D-view

2.2.1.1

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

756489

5xu9, 3D-view

2.2.1.1

6 entries

2.2.1.2

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

756739, 736749, 671553, 755719, 756034, 758246

3s1u, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate

639772, 639795, 639745, 639798, 639796, 639773, 639786, 639755, 639744, 639746, 639767, 639771, 639774, 639783, 639769, 639758, 639765, 639742, 639778, 639791

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate

738530, 738155, 738708, 737813, 739438, 739599, 738228

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate

710184, 701494

1rzm, 3D-view

2.5.1.54

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (13 results)

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Show Natural Product (13 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.79

FMNH2 + NADH + H+ + O2 + alloxan = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + dialuric acid

0

-

1.13.11.79

FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ?

0

-

1.13.11.79

FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + dialiric acid + pyrimidinetrione + alloxan

0

-

1.13.11.79

FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + urea + ?

0

-

2.2.1.1

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

0

1ngs, 3D-view

2.2.1.1

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

0

5xps, 3D-view

2.2.1.1

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

0

5xu9, 3D-view

2.2.1.1

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

0

1ngs, 3D-view

2.2.1.1

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

0

5xps, 3D-view

2.2.1.1

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

0

5xu9, 3D-view

1.13.11.79

4 entries

2.2.1.1

6 entries

2.2.1.2

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

0

3s1u, 3D-view

4.1.2.22

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

0

-

5.3.1.34

D-erythrulose 4-phosphate = D-erythrose 4-phosphate

0

-

Substrate in Enzyme-catalyzed Reactions (39 results)

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Show Substrate (39 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.405

D-erythrose 4-phosphate + NADPH + H+ = ? + NADP+

645254

-

1.2.1.72

D-erythrose 4-phosphate + 3-acetylpyridine adenine dinucleotide = 4-phosphoerythronate + ?

661984

-

1.2.1.72

D-erythrose 4-phosphate + NAD+ = 4-phosphoerythronate + NADH

661984, 662097, 692925

-

2.2.1.1

D-erythrose 4-phosphate + ? = ?

486023, 486026, 486018

1ngs, 3D-view

2.2.1.1

D-erythrose 4-phosphate + ? = ?

486023, 486026, 486018

5xps, 3D-view

2.2.1.1

D-erythrose 4-phosphate + ? = ?

486023, 486026, 486018

5xu9, 3D-view

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

1ngs, 3D-view

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

5xps, 3D-view

2.2.1.1

D-erythrose 4-phosphate + D-xylulose 5-phosphate = ?

757197

5xu9, 3D-view

2.2.1.1

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

756489, 756467, 758271

1ngs, 3D-view

2.2.1.1

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

756489, 756467, 758271

5xps, 3D-view

2.2.1.1

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

756489, 756467, 758271

5xu9, 3D-view

2.2.1.1

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

485993, 486001, 486004

1ngs, 3D-view

2.2.1.1

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

485993, 486001, 486004

5xps, 3D-view

2.2.1.1

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

485993, 486001, 486004

5xu9, 3D-view

1.2.1.72

2 entries

2.2.1.1

12 entries

2.2.1.10

pyruvate + D-erythrose 4-phosphate = ?

692386

-

2.2.1.14

6-deoxy-6-sulfo-D-fructose + D-erythrose 4-phosphate = (2S)-3-sulfolactaldehyde + D-sedoheptulose 7-phosphate

761326

-

2.2.1.2

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

756739, 736749, 671553, 755719, 718671, 756034, 758246

3s1u, 3D-view

2.2.1.2

D-erythrose 4-phosphate + sedoheptulose 7-phosphate = ?

486027, 486031, 486041

3s1u, 3D-view

2.2.1.2

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

660839

3s1u, 3D-view

2.2.1.2

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

706567

3s1u, 3D-view

2.2.1.2

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

671553

3s1u, 3D-view

2.2.1.2

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

661356, 663096

3s1u, 3D-view

2.2.1.2

6 entries

2.2.1.3

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

486057

-

2.2.1.7

pyruvate + D-erythrose 4-phosphate = 1-deoxy-D-fructose 6-phosphate + CO2

660537, 658834, 659734

-

2.5.1.54

phosphoenol-3-fluoropyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate

658128

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 2-dehydro-3-deoxy-D-arabino-heptonate 7-phosphate + phosphate

639751, 639744, 639745, 674736, 637413, 639746, 639747, 639748, 639749, 639750, 639753, 639767, 639768, 639771, 639775, 639776, 639777, 639783, 639792, 672596, 680370, 684632, 637421, 639741, 639774, 639789, 672576, 639757, 639766, 639770, 639785, 676798, 688818, 639763, 639764, 639779, 639780, 639761, 639755, 639756, 639772, 639798, 639773, 639760, 639790, 639752, 639793, 639794, 684585, 639782, 639791, 639769, 639758, 639765, 639759, 639795, 676479, 639742, 639743, 639754, 639778, 639781, 639786, 639788, 639796, 639762

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phospate + phosphate

738530, 738155, 738708, 737813, 739438, 739599, 738228

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate

658128, 659071, 659072, 710184, 660428, 657871, 701494, 658097, 725725, 721793, 723700, 758795, 758943, 758627

1rzm, 3D-view

2.5.1.54

phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-erythro-hept-2-ulosonate 7-phosphate + phosphate

657873, 659228

1rzm, 3D-view

2.5.1.54

5 entries

3.1.3.23

D-erythrose 4-phosphate + H2O = D-erythrose + phosphate

730458

-

3.1.3.25

D-erythrose 4-phosphate + H2O = D-erythrose + phosphate

681812

-

3.1.3.58

D-erythrose-4-phosphate + H2O = D-erythrose + phosphate

646416

-

4.1.2.14

Pyruvate + D-erythrose 4-phosphate = 3-Deoxy-D-riboheptulosonic acid 7-phosphate

4979

-

4.1.2.21

pyruvate + D-erythrose 4-phosphate = 3-deoxy-D-arabino-heptulosonic acid 7-phosphate

680370

-

4.1.2.21

pyruvate + D-erythrose 4-phosphate = ?

665300

-

4.1.2.21

2 entries

4.1.2.4

D-Erythrose 4-phosphate + acetaldehyde = ?

5170

-

5.1.3.1

D-erythrose 4-phosphate = D-erythrulose 4-phosphate

738147

-

5.3.1.34

D-erythrose 4-phosphate = D-erythrulose 4-phosphate

738147

-

Product in Enzyme-catalyzed Reactions (28 results)

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Show Product (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.13.11.79

FMNH2 + NADH + H+ + O2 + alloxan = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + dialuric acid

0

-

1.13.11.79

FMNH2 + NADH + H+ + O2 + H2O = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ?

0

-

1.13.11.79

FMNH2 + NADH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NAD+ + ?

0

-

1.13.11.79

FMNH2 + NADPH + H+ + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + NADP+ + ?

0

-

1.13.11.79

FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + dialiric acid + pyrimidinetrione + alloxan

0

-

1.13.11.79

FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)

0

-

1.13.11.79

FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + urea + ?

0

-

2.2.1.1

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

0

1ngs, 3D-view

2.2.1.1

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

0

5xps, 3D-view

2.2.1.1

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

0

5xu9, 3D-view

2.2.1.1

D-fructose 6-phosphate + D-ribose 5-phosphate = D-erythrose 4-phosphate + sedoheptulose 7-phosphate

0

1ngs, 3D-view

2.2.1.1

D-fructose 6-phosphate + D-ribose 5-phosphate = D-erythrose 4-phosphate + sedoheptulose 7-phosphate

0

5xps, 3D-view

2.2.1.1

D-fructose 6-phosphate + D-ribose 5-phosphate = D-erythrose 4-phosphate + sedoheptulose 7-phosphate

0

5xu9, 3D-view

2.2.1.1

D-fructose 6-phosphate + Fe(CN)3- = glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+

0

1ngs, 3D-view

2.2.1.1

D-fructose 6-phosphate + Fe(CN)3- = glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+

0

5xps, 3D-view

2.2.1.1

D-fructose 6-phosphate + Fe(CN)3- = glycolic acid + D-erythrose 4-phosphate + Fe(CN)64- + H+

0

5xu9, 3D-view

2.2.1.1

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

0

1ngs, 3D-view

2.2.1.1

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

0

5xps, 3D-view

2.2.1.1

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

0

5xu9, 3D-view

2.2.1.1

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

0

1ngs, 3D-view

2.2.1.1

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

0

5xps, 3D-view

2.2.1.1

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

0

5xu9, 3D-view

1.13.11.79

7 entries

2.2.1.1

15 entries

2.2.1.2

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

0

3s1u, 3D-view

4.1.2.13

sedoheptulose 1,7-bis-phosphate = glycerone phosphate + D-erythrose 4-phosphate

0

-

4.1.2.13

sedoheptulose 1,7-bisphosphate = glycerone phosphate + D-erythrose 4-phosphate

0

-

4.1.2.13

2 entries

4.1.2.22

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

0, 5095, 653088, 651682

-

4.1.2.9

D-Fructose 6-phosphate + phosphate = Acetyl phosphate + D-erythrose 4-phosphate + H2O

0

-

5.3.1.34

D-erythrulose 4-phosphate = D-erythrose 4-phosphate

0

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.7.10

slight activation

642818

-

2.7.7.9

slight activation

642818

-

Inhibitor in Enzyme-catalyzed Reactions (12 results)

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Show Inhibitors (12 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.44

bio-isosteric analogue

654952

-

1.1.1.44

-

286885, 286896, 286904

-

1.1.1.44

2 entries

1.2.1.9

-

288338, 288340, 288343

-

2.2.1.10

competitive inhibition of aldolase activity

692386

-

2.2.1.2

-

486030

3s1u, 3D-view

2.5.1.54

-

639769

1rzm, 3D-view

2.5.1.54

isoenzyme DS-Mn: substrate inhibition above 0.5 mM

639782

1rzm, 3D-view

2.5.1.54

Phe-sensitive isozyme: in absence of phosphoenolpyruvate the enzyme is inhibited via formation of a covalent binding to Lys186 via a slow Schiff base reaction, mechanism

639796

1rzm, 3D-view

2.5.1.54

substrate-inhibition

639764

1rzm, 3D-view

2.5.1.54

4 entries

4.1.2.13

competitive

692386

-

4.3.3.6

-

724239

-

5.3.1.1

-

2561

-

3D Structure of Enzyme-Ligand-Complex (PDB) (33 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (33 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

1ngs, 3D-view

2.2.1.1

5xps, 3D-view

2.2.1.1

5xu9, 3D-view

2.2.1.1

18 entries

2.2.1.2

3s1u, 3D-view

2.5.1.54

1rzm, 3D-view

4.1.2.16

1fwt, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

1iri, 3D-view

5.3.1.9

1u0g, 3D-view

5.3.1.9

12 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (38 results)

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Show Turnover Number (38 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.405

0.5

-

wild-type, pH 7.2, 25°C

645254

1.2.1.72

0.21

-

25°C, mutant enzyme H176N

662097

1.2.1.72

0.6

-

25°C, mutant enzyme C311Y

662097

1.2.1.72

3.5

-

25°C, mutant enzyme C311A

662097

1.2.1.72

4

-

25°C, mutant enzyme M179T

662097

1.2.1.72

7.4

-

25°C, mutant enzyme E32D

662097

1.2.1.72

20

-

25°C, wild-type enzyme

662097

1.2.1.72

200

-

-

661984

2.2.1.1

1.4

-

D477A

486018

2.2.1.1

69

-

wild-type

486018

2.2.1.1

1390

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.1

86500

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.1

104000

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.2

-999

-

pH 6.0, 20°C

671553

2.2.1.2

6.44

-

-

671553

2.2.1.2

22.9

-

pH 9.0, 80°C

718671

2.5.1.54

0.03

-

pH 7.5, 30°C

723700

2.5.1.54

0.3

-

isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

684585

2.5.1.54

1.14

-

isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

684585

2.5.1.54

1.183

-

pH 6.8

672576

2.5.1.54

5.5

-

pH 7.5, 60°C, wild-type enzyme

725725

2.5.1.54

6.08

-

pH 6.8

672576

2.5.1.54

11.7

-

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

738228

2.5.1.54

12.6

-

pH 6.8, 25°C, mutant R126S

739438

2.5.1.54

14.1

-

pH 7.3, temperature not specified in the publication, mutant H29S/S31H

738228

2.5.1.54

14.3

-

pH 7.3, temperature not specified in the publication, mutant S31G

738228

2.5.1.54

14.8

-

pH 6.8, 30°C, mutant R126S

739599

2.5.1.54

14.8

-

pH 6.8, 30°C, wild-type enzyme

739599

2.5.1.54

14.9

-

pH 7.5, 60°C, mutant enzyme I181D

725725

2.5.1.54

17.5

-

pH 7.3, temperature not specified in the publication, mutant H29A

738228

2.5.1.54

19.8

-

pH 7.5, 37°C, presence of Co2+

758943

2.5.1.54

21

-

Trp-sensitive isozyme, pH 7.0, 25°C

639767

2.5.1.54

27.1

-

pH 6.8, 25°C, wild-type enzyme

739438

2.5.1.54

32

-

Phe-sensitive isozyme, pH 6.8, 25°C

639789

2.5.1.54

71

-

Phe-sensitive isozyme, pH 6.8, 25°C

639796

2.5.1.54

122

-

pH 7.0, 37°C, MW 79000 assumed

639747

4.1.2.21

0.94

-

wild type enzyme, in MOPS buffer (50 mM, pH 7.5), 0.050 mM CoCl2, 0.010 mM NAD+, D-erythrose 4-phosphate, 2 mM pyruvate, 1 unit of 3-dehydroquinate synthase, 1 unit of 3-dehydroquinate dehydratase, at 25°C

680370

4.1.2.21

2.5

-

mutant enzyme F33I/D58N/Q72H/A75V/V85A/V154F, in MOPS buffer (50 mM, pH 7.5), 0.050 mM CoCl2, 0.010 mM NAD+, D-erythrose 4-phosphate, 2 mM pyruvate, 1 unit of 3-dehydroquinate synthase, 1 unit of 3-dehydroquinate dehydratase, at 25°C

680370

1.2.1.72

7 entries

2.2.1.1

5 entries

2.2.1.2

3 entries

2.5.1.54

20 entries

4.1.2.21

2 entries

K_M Value (92 results)

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Show KM Value (92 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.405

0.038

-

wild-type, pH 7.2, 25°C

645254

1.2.1.72

0.24

-

25°C, mutant enzyme H176N

662097

1.2.1.72

0.51

-

25°C, wild-type enzyme

662097

1.2.1.72

0.7

-

25°C, mutant enzyme C311Y

662097

1.2.1.72

0.7

-

25°C, mutant enzyme M179T

662097

1.2.1.72

0.8

-

25°C, mutant enzyme C311A

662097

1.2.1.72

0.96

-

-

661984

1.2.1.72

1.9

-

25°C, mutant enzyme E32D

662097

2.2.1.1

0.023

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.1

0.082

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.1

0.09

-

-

486023, 486026

2.2.1.1

0.099

-

with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

757197

2.2.1.1

0.36

-

-

486026

2.2.1.2

0.007

-

-

486035

2.2.1.2

0.013

-

pH 6.0, 20°C

671553

2.2.1.2

0.013

-

-

671553

2.2.1.2

0.0156

-

pH 7.5, 25°C

660839

2.2.1.2

0.018

-

-

486027

2.2.1.2

0.02

-

-

486032

2.2.1.2

0.0278

-

pH 7.5, 50°C

660839

2.2.1.2

0.078

-

T156A

486044

2.2.1.2

0.084

-

transaldolase B, at pH 7.2 and 37°C

756739

2.2.1.2

0.09

-

-

486041

2.2.1.2

0.1

-

-

486030

2.2.1.2

0.1

-

wild-type, N35A

486044

2.2.1.2

0.11

-

D17N

486044

2.2.1.2

0.111

-

S176A

486044

2.2.1.2

0.117

-

E96Q

486044

2.2.1.2

0.122

-

E96A

486044

2.2.1.2

0.14

-

transaldolase A, at pH 7.2 and 37°C

756739

2.2.1.2

0.265

-

R300A

486043

2.2.1.2

0.27

-

pH 9.0, 80°C

718671

2.2.1.2

0.295

-

wild-type

486043

2.2.1.2

0.35

-

R300E

486043

2.2.1.2

0.49

-

-

706567

2.2.1.2

0.555

-

D17A

486044

1.2.1.72

7 entries

2.2.1.1

5 entries

2.2.1.2

23 entries

2.2.1.7

0.12

-

pH 7.9, 37°C

658834

2.5.1.54

0.0026

-

pH 7.0, 37°C

639781

2.5.1.54

0.006

-

pH 7.5, 30°C

657871

2.5.1.54

0.009

-

pH 6.8, 60°C

658097

2.5.1.54

0.013

-

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

738228

2.5.1.54

0.013

-

pH 7.4, 37°C

639744

2.5.1.54

0.0134

-

pH 6.8, 25°C, mutant R126S

739438

2.5.1.54

0.015

-

pH 7.5, 25°C

758795

2.5.1.54

0.016

-

pH 7.5, 37°C, presence of Co2+

758943

2.5.1.54

0.018

-

wild-type, pH 7.9, 30°C

639794

2.5.1.54

0.021

-

pH 6.8

672576

2.5.1.54

0.028

-

60°C, pH 6.8

660428

2.5.1.54

0.028

-

pH 7.3, temperature not specified in the publication, mutant H29S/S31H

738228

2.5.1.54

0.03

-

pH 7.3, temperature not specified in the publication, mutant H29A

738228

2.5.1.54

0.033

-

pH 7.3, temperature not specified in the publication, mutant S31G

738228

2.5.1.54

0.037

-

pH 6.8, 25°C, wild-type enzyme

739438

2.5.1.54

0.04

-

pH 6.8, 30°C, mutant R126S

739599

2.5.1.54

0.043

-

pH 6.8, 30°C, wild-type enzyme

739599

2.5.1.54

0.055

-

pH 7.8, 25°C

639745

2.5.1.54

0.0573

-

pH 7.5, 50°C

659228

2.5.1.54

0.07

-

pH 7.0, 25°C

639758

2.5.1.54

0.071

-

pH 7.5, 60°C, mutant enzyme I181D

725725

2.5.1.54

0.0814

-

Tyr-sensitive isozyme, 25°C

639777

2.5.1.54

0.086

-

Phe-sensitive isozyme, pH 6.8, 25°C

639789

2.5.1.54

0.092

-

pH 7.5, 60°C, wild-type enzyme

725725

2.5.1.54

0.0965

-

pH 7.0, 37°C

639747

2.5.1.54

0.13

-

Phe-sensitive isozyme, pH 6.8, 30°C

639770

2.5.1.54

0.138

-

pH 7.5, 60°C

659228

2.5.1.54

0.141

-

recombinant enzyme, pH 7.5, 25°C

639774

2.5.1.54

0.16

-

30°C, pH 7.0

639742

2.5.1.54

0.195

-

Trp-sensitive isozyme, pH 7.0, 30°C

639779

2.5.1.54

0.25

-

Trp-sensitive isozyme, pH 7.2, 37°C

639769

2.5.1.54

0.25

-

wild-type, 25°C, pH 6.4

659072

2.5.1.54

0.278

-

mutant I10A, 25°C, pH 6.4

659072

2.5.1.54

0.28

-

pH 7.0, 60°C

721793

2.5.1.54

0.29

-

isozyme NCgl0950 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5, at 30°C

684585

2.5.1.54

0.3506

-

pH 7.5, 70°C

659228

2.5.1.54

0.392

-

mutant N5K, 25°C, pH 6.4

659072

2.5.1.54

0.43

-

pH 7.5, 30°C

723700

2.5.1.54

0.5

-

Tyr-sensitive isozyme, pH 6.8

639766

2.5.1.54

0.56

-

DAHP synthase-trp, pH 7.0, 37°C

639760

2.5.1.54

0.77

-

DAHP synthase-tyr, pH 7.0, 37°C

639759

2.5.1.54

0.87

-

DAHP synthase-phe, pH 7.0, 37°C

639759

2.5.1.54

0.9

-

pH 7.0, 37°C

639749

2.5.1.54

1

-

DAHP synthase-tyr, pH 7.0, 37°C

639760

2.5.1.54

1.1

-

DS II isozyme, pH 7.5, 37°C

639778

2.5.1.54

1.2

-

pH 6.4, 37°C

639741

2.5.1.54

1.4

-

at 37°C

674736

2.5.1.54

1.76

-

pH 7.5, 37°C

657873

2.5.1.54

1.95

-

cytosolic isozyme DS-Co, pH 8.6, 37°C

639780

2.5.1.54

2.17

-

isozyme NCgl2098 DAHP synthase, in 50 mM Tris-HCl buffer, pH 7.5,at 30°C

684585

2.5.1.54

3.3

-

cytosolic isozyme, pH 8.6

639765

2.5.1.54

3.638

-

at 37°C

674736

2.5.1.54

52.36

-

N-terminal deletion mutant, 25°C, pH 6.4

659072

4.1.2.21

0.12

-

mutant enzyme F33I/D58N/Q72H/A75V/V85A/V154F, in MOPS buffer (50 mM, pH 7.5), 0.050 mM CoCl2, 0.010 mM NAD+, D-erythrose 4-phosphate, 2 mM pyruvate, 1 unit of 3-dehydroquinate synthase, 1 unit of 3-dehydroquinate dehydratase, at 25°C

680370

4.1.2.21

0.57

-

wild type enzyme, in MOPS buffer (50 mM, pH 7.5), 0.050 mM CoCl2, 0.010 mM NAD+, D-erythrose 4-phosphate, 2 mM pyruvate, 1 unit of 3-dehydroquinate synthase, 1 unit of 3-dehydroquinate dehydratase, at 25°C

680370

2.5.1.54

53 entries

4.1.2.21

2 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

1.1.1.44

0.175

-

pH 8.0, 20°C

654952

1.1.1.44

1.59

-

pH 8.0, 20°C

654952

1.1.1.44

2 entries

2.2.1.10

0.38

-

recombinant enzyme, pH 7.5, 50°C

692386

4.1.2.13

0.38

-

-

692386

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

4.3.3.6

3.7

-

Pdx1, pH 8.0, 37°C

724239

References & Links

Literature References (148)

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Show Reference (148 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2561

-

Triosephosphate isomerase from rabbit liver

1975

Krietsch, W.K.G.

Methods Enzymol.

41B

438-442

4979

-

Investigation of 2-oxo-3-deoxy-5-phosphogluconate aldolase from Zymomonas mobilis as a catalyst in organic synthesis

1995

Knappmann, B.R.; Steigel, A.; Kula, M.R.

Biotechnol. Appl. Biochem.

22

107-120

5095

13610828

Phosphorolytic cleavage of fructose-6-phosphate by fructose-6-phosphate phosphoketolase from Acetobacter xylinum

1958

Schramm, M.; Klybas, V.; Racker, E.

J. Biol. Chem.

233

1283-1288

5170

-

Deoxyribose 5-phosphate aldolase. I. Lactobacillus plantarum

1966

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

Methods Enzymol.

9

545-549

286885

-

Regulation of 6-phosphogluconate dehydrogenase in Brevibacterium flavum

1987

Sugimoto, S.I.; Shiho, I.

Agric. Biol. Chem.

51

1257-1263

286896

7773202

Purification and properties of 6-phosphogluconate dehydrogenase from beet leaves

1995

Signorini, M.; Bregoli, A.M.; Caselli, L.; Bergamini, C.M.

Biochem. Mol. Biol. Int.

35

669-675

286904

10848959

Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo

2000

Moritz, B.; Striegel, K.; de Graaf, A.A.; Sahm, H.

Eur. J. Biochem.

267

3442-3452

288338

-

Purification and properties of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the green algae Chlamydomonas reinhardtii

1987

Iglesias, A.A.; Serrano, A.; Guerrro, M.G.; Losada, M.

Biochim. Biophys. Acta

925

1-10

288340

16658509

Nonreversible D-glyceraldehyde 3-phosphate dehydrogenase of plant tissue

1973

Kelly, G.J.; Gibbs, M.

Plant Physiol.

52

111-118

288343

33184

Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans

1979

Crow, V.L.; Wittenberger, C.L.

J. Biol. Chem.

254

1134-1142

485993

13385248

The role of xylulose 5-phosphate in the transketolase reaction

1956

Horecker, B.L.; Smyrniotis, P.Z.; Hurwitz, J.

J. Biol. Chem.

223

1009-1019

486001

24271866

The properties from transketolase from photosynthetic tissue

1982

Murphy, D.J.; Walker, D.A.

Planta

155

316-320

486004

2495942

Transketolase from human leukocytes. Isolation, properties and induction of polyclonal antibodies

1989

Mocali, A.; Paoletti, F.

Eur. J. Biochem.

180

213-219

486018

9537513

Asp477 is a determinant of the enantioselectivity in yeast transketolase

1998

Nilsson, U.; Hecquet, L.; Gefflaut, T.; Guerard, C.; Schneider, G.

FEBS Lett.

424

49-52

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

486031

11946741

The forward and reverse reactions of transaldolase

1972

Wood, T.

FEBS Lett.

25

153-155

486032

-

Transaldolase

1975

Tsolas, O.; Joris, L.

Methods Enzymol.

42 C

290-297

486035

5025625

Purification and properties of transaldolase from bovine mammary gland

1972

Kuhn, E.; Brand, K.

Biochemistry

11

1767-1772

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

486043

9883893

Disruption of Escherichia coli transaldolase into catalytically active monomers: evidence against half-of-the-sites mechanism

1998

Schorken, U.; Jia, J.; Sahm, H.; Sprenger, G.A.; Schneider, G.

FEBS Lett.

441

247-250

486044

11298760

Identification of catalytically important residues in the active site of Escherichia coli transaldolase

2001

Schorken, U.; Thorell, S.; Schurmann, M.; Jia, J.; Sprenger, G.A.; Schneider, G.

Eur. J. Biochem.

268

2408-2415

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

637413

10734095

Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase

2000

Radaev, S.; Dastidar, P.; Patel, M.; Woodard, R.W.; Gatti, D.L.

J. Biol. Chem.

275

9476-9484

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

639741

13654249

2-Keto-3-deoxy-D-arabo-heptonic acid 7-phosphate synthetase

1954

Srinivasan, P.R.; Sprinson, D.B.

J. Biol. Chem.

234

716-722

639742

5003718

2-Deoxy-D-arabino-heptulosonate-7-phosphate synthase of Streptomyces aureofaciens Tü 24

1971

Görisch, H.; Lingens, F.

Biochim. Biophys. Acta

242

617-629

639743

5003719

3-Deoxy-D-arabino-heptulosonate-7-phosphate synthase of Streptomyces aureofaciens Tü 24

1971

Görisch, H.; Lingens, F.

Biochim. Biophys. Acta

242

630-636

639744

4572729

Purification and kinetics of tyrosine-sensitive 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase from Salmonella

1973

DeLeo, A.B.; Dayan, J.; Sprinson, D.B.

J. Biol. Chem.

248

2344-2353

639745

239657

Aromatic amino acid biosynthesis in Alcaligenes eutrophus H16. I. Properties and regulation of 3-deoxy-D-arabino heptulosonate 7-phosphate synthase

1975

Friedrich, C.G.; Schlegel, H.G.

Arch. Microbiol.

103

133-140

639746

821531

Purification and properties of tyrosine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase of Escherichia coli K12

1976

Dusha, I.; Dénes, G.

Biochim. Biophys. Acta

438

563-573

639747

9387

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification, properties, and kinetics of the tyrosine-sensitive isoenzyme from Escherichia coli

1976

Schoner, R.; Herrmann, K.M.

J. Biol. Chem.

251

5440-5447

639748

12951

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli. Purification and subunit structure

1976

Simpson, R.J.; Davidson, B.E.

Eur. J. Biochem.

70

493-500

639749

12952

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12. 2. Kinetic properties

1976

Simpson, R.J.; Davidson, B.E.

Eur. J. Biochem.

70

501-507

639750

12953

Studies on 3-deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12. 3. Structural studies

1976

Simpson, R.J.; Davidson, B.E.

Eur. J. Biochem.

70

509-516

639751

12135

Properties of tyrosine-inhibitable 3-deoxy-D-arabinoheptulosonic acid-7-phosphate synthase from Salmonella

1977

Hu, Ch.Y.; Sprinson, D.B.

J. Bacteriol.

129

177-183

639752

21700

Purification of the tyrosine inhibitable 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Schizosaccharomyces pombe

1977

Bracher, M.; Schweingruber, M.E.

Biochim. Biophys. Acta

485

446-451

639753

26682

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase. Purification and molecular characterization of the phenylalanine-sensitive isoenzyme from Escherichia coli

1978

McCandliss, R.J.; Poling, M.D.; Herrmann, K.M.

J. Biol. Chem.

253

4259-4265

639754

3341755

The essential role of cobalt in the inhibition of the cytosolic isoenzyme of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Nicotiana silvestris by glyphosate

1988

Ganson, R.J.; Jensen, R.A.

Arch. Biochem. Biophys.

260

85-93

639755

16666241

Glyphosate induces 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in potato (Solanum tuberosum L.) Cells grown in suspension culture

1988

Pinto, J.E.B.P.; Dyer, W.E.; Weller, S.C.; Herrmann, K.M.

Plant Physiol.

87

891-893

639756

16665132

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase from potato tuber (Solanum tuberosum L.)

1986

Pinto, J.E.B.P.; Suzich, J.A.; Herrmann, K.M.

Plant Physiol.

82

1040-1044

639757

2880280

Cloning of the ARO3 gene of Saccharomyces cerevisiae and its regulation

1986

Teshiba, S.; Furter, R.; Niederberger, P.; Braus, G.; Paravicini, G.; Hütter, R.

Mol. Gen. Genet.

205

353-357

639758

16664489

3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase from carrot root (Daucus carota) is a hysteretic enzyme

1985

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Pagor, R.; Sikdar, M.; Moon, E.; Kim, J.

J. Biol. Sci.

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33-39

739438

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The functional unit of Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase is dimeric

2016

Cross, P.J.; Heyes, L.C.; Zhang, S.; Nazmi, A.R.; Parker, E.J.

PLoS ONE

11

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739599

23754471

Neisseria meningitidis expresses a single 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase that is inhibited primarily by phenylalanine

2013

Cross, P.J.; Pietersma, A.L.; Allison, T.M.; Wilson-Coutts, S.M.; Cochrane, F.C.; Parker, E.J.

Protein Sci.

22

1087-1099

755719

27050126

Novel mode of inhibition by D-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants

2016

Stellmacher, L.; Sandalova, T.; Schneider, S.; Schneider, G.; Sprenger, G.A.; Samland, A.K.

Acta Crystallogr. Sect. D

72

467-476

756034

26131847

Converting transaldolase into aldolase through swapping of the multifunctional acid-base catalyst common and divergent catalytic principles in F6P aldolase and transaldolase

2015

Sautner, V.; Friedrich, M.M.; Lehwess-Litzmann, A.; Tittmann, K.

Biochemistry

54

4475-4486

756467

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Towards a mechanistic understanding of factors controlling the stereoselectivity of transketolase

2018

Baierl, A.; Theorell, A.; Mackfeld, U.; Marquardt, P.; Hoffmann, F.; Moers, S.; Noeh, K.; Buchholz, P.; Pleiss, J.; Pohl, M.

ChemCatChem

10

2601-2611

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The catalytic mechanism of human transketolase

2019

Prejano, M.; Medina, F.E.; Fernandes, P.A.; Russo, N.; Ramos, M.J.; Marino, T.

Chemphyschem

20

2881-2886

756739

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Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli

2016

Ogawa, T.; Murakami, K.; Yoshino, M.

FEMS Microbiol. Lett.

363

fnw183

757197

29848552

Salmonella enterica serovar Typhimurium has three transketolase enzymes contributing to the pentose phosphate pathway

2018

Shaw, J.A.; Henard, C.A.; Liu, L.; Dieckman, L.M.; Vazquez-Torres, A.; Bourret, T.J.

J. Biol. Chem.

293

11271-11282

758246

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Form III RubisCO-mediated transaldolase variant of the Calvin cycle in a chemolithoautotrophic bacterium

2019

Frolov, E.N.; Kublanov, I.V.; Toshchakov, S.V.; Lunev, E.A.; Pimenov, N.V.; Bonch-Osmolovskaya, E.A.; Lebedinsky, A.V.; Chernyh, N.A.

Proc. Natl. Acad. Sci. USA

116

18638-18646

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Structural and biochemical interrogation on transketolase from Pichia stipitis for new functionality

2016

Hsu, L.J.; Hsu, N.S.; Wang, Y.L.; Wu, C.J.; Li, T.L.

Protein Eng. Des. Sel.

29

513-522

758627

30715617

Isolation and biochemical characterization of a metagenome-derived 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase gene from subtropical marine mangrove wetland sediments

2019

Zhao, H.; Gao, H.; Ji, K.; Yan, B.; Li, Q.; Mo, S.; Zheng, M.; Ou, Q.; Wu, B.; Li, N.; Jiang, C.

AMB Express

9

19

758795

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Potent inhibition of 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) synthase by DAHP oxime, a phosphate group mimic

2016

Balachandran, N.; Heimhalt, M.; Liuni, P.; To, F.; Wilson, D.J.; Junop, M.S.; Berti, P.J.

Biochemistry

55

6617-6629

758943

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Structural and functional characterisation of the entry point to pyocyanin biosynthesis in Pseudomonas aeruginosa defines a new 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase subclass

2018

Sterritt, O.; Lang, E.; Kessans, S.; Ryan, T.; Demeler, B.; Jameson, G.; Parker, E.

Biosci. Rep.

38

BSR20181605

761326

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Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway

2020

Frommeyer, B.; Fiedler, A.; Oehler, S.; Hanson, B.; Loy, A.; Franchini, P.; Spiteller, D.; Schleheck, D.

iScience

23

101510

Links to other databases for D-erythrose 4-phosphate

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