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Ligand L-aspartic 4-semialdehyde

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

chorismate metabolism, grixazone biosynthesis, lysine metabolism, polyamine pathway, threonine metabolism

KEGG

2-Oxocarboxylic acid metabolism, Arginine and proline metabolism, Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Biosynthesis of various antibiotics, Biosynthesis of various other secondary metabolites, Cysteine and methionine metabolism, Glycine, serine and threonine metabolism, Lysine biosynthesis, Microbial metabolism in diverse environments, Monobactam biosynthesis, Phenylalanine, tyrosine and tryptophan biosynthesis more

MetaCyc

3-dehydroquinate biosynthesis II (archaea), baumannoferrin biosynthesis, cremeomycin biosynthesis, dipicolinate biosynthesis, ectoine biosynthesis, ectoine degradation, grixazone biosynthesis, L-homoserine biosynthesis, L-lysine biosynthesis I, L-lysine biosynthesis II, L-lysine biosynthesis III, L-lysine biosynthesis VI, L-methionine biosynthesis IV, norspermidine biosynthesis, platensimycin biosynthesis, pyoverdine I biosynthesis, rhizobactin 1021 biosynthesis, spermidine biosynthesis II more

Show all BRENDA pathways known for L-aspartic 4-semialdehyde

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (20 results)

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Show Natural Substrate (20 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

L-aspartate 4-semialdehyde + NAD(P)H = L-homoserine + NAD(P)+

246388, 246387, 246401, 246382, 654955

-

1.1.1.3

L-aspartate 4-semialdehyde + NADPH = L-homoserine + NADP+

654640

-

1.2.1.11

aspartate-4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+

684192

-

1.2.1.11

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+

673074, 670165, 687340, 741702, 674667, 742070, 742704, 762956, 675505, 725944, 675355, 763308, 742287, 710717, 726268, 741540, 741535, 762575, 762696, 688468, 684192, 684158

-

1.2.1.11

L-aspartate-4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH

654110, 654103

-

1.1.1.3

2 entries

1.2.1.11

3 entries

1.4.1.B4

L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O

719993

-

1.5.1.43

L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ = carboxynorspermidine + H2O + NADP+

741488, 742792

-

1.5.1.43

L-aspartate 4-semialdehyde + putrescine + NADPH + H+ = carboxyspermidine + H2O + NADP+

741488, 742792

-

2.2.1.10

L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate

718845

-

2.2.1.10

L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate

692386

-

2.2.1.10

L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = ?

718838

-

1.5.1.43

2 entries

2.2.1.10

3 entries

2.6.1.46

L-2-amino-4-oxobutanoate + L-glutamate = L-2,4-diaminobutanoate + 2-oxoglutarate

640091, 640090

-

2.8.1.16

hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster

752754

-

4.1.2.56

glycerone phosphate + L-aspartate 4-semialdehyde = 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate

722650

-

4.3.3.7

(S)-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + H2O

692356, 693141, 690252, 695011, 692255, 652939, 649771, 678046

-

4.3.3.7

(S)-aspartate-4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O

729062, 728904, 728889, 729237, 730908, 720852, 730915, 728891, 728886, 729694, 729385

-

4.3.3.7

L-aspartate 4-semialdehyde + pyruvate = (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O

712704, 713953, 713969, 714351, 715195

-

4.3.3.7

L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + H2O

664072, 691786

-

4.3.3.7

L-aspartate-4-semialdehyde + pyruvate = ?

33903, 33911, 33902, 33912, 33914

-

4.3.3.7

pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O

747107, 748035, 730623, 730624, 746655, 746659, 749225, 749039

-

4.3.3.7

6 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

1.1.1.3

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H

0

-

1.1.1.3

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+

0

-

1.1.1.3

L-homoserine + NAD+ = L-aspartate 4-semialdehyde + NADH + H+

0

-

1.1.1.3

L-homoserine + NADP+ = L-aspartate 4-semialdehyde + NADPH

0

-

1.1.1.3

L-homoserine + NADP+ = L-aspartate 4-semialdehyde + NADPH + H+

0

-

1.2.1.11

L-4-aspartyl phosphate + NADPH + H+ = L-aspartate 4-semialdehyde + phosphate + NADP+

0

-

1.2.1.11

L-4-aspartyl phosphate + NADPH = L-aspartate 4-semialdehyde + phosphate + NADP+

390202, 390200, 390188, 390199, 390203, 137551, 390182, 390187, 390189, 390183

-

1.2.1.11

L-4-aspartyl phosphate + NADPH = L-aspartate-4-semialdehyde + phosphate + NADP+

0

-

1.1.1.3

5 entries

1.2.1.11

3 entries

2.6.1.46

L-2,4-diaminobutanoate + pyruvate = L-2-amino-4-oxobutanoate + L-alanine

640089

-

2.6.1.76

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate

0

-

Substrate in Enzyme-catalyzed Reactions (37 results)

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Show Substrate (37 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

L-aspartate 4-semialdehyde + NAD(P)H = L-homoserine + NAD(P)+

246393, 246387, 246390, 246398, 654955, 246401, 246388, 246382, 246395, 246391, 246403, 246392, 246396, 246402

-

1.1.1.3

L-aspartate 4-semialdehyde + NADH + H+ = L-homoserine + NAD+

246382

-

1.1.1.3

L-aspartate 4-semialdehyde + NADH = L-homoserine + NAD+

712490

-

1.1.1.3

L-aspartate 4-semialdehyde + NADPH + H+ = L-homoserine + NADP+

670165, 246385

-

1.1.1.3

L-aspartate 4-semialdehyde + NADPH = L-homoserine + NADP+

654640, 662432, 712490

-

1.2.1.11

aspartate-4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+

684192

-

1.2.1.11

L-aspartate 4-semialdehyde + arsenate + NADP+ = ?

390200

-

1.2.1.11

L-aspartate 4-semialdehyde + HasO42- + NADP+ = ?

390180

-

1.2.1.11

L-aspartate 4-semialdehyde + phosphate + NAD+ = L-4-aspartyl phosphate + NADH + H+

675355, 742287

-

1.2.1.11

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH

390202, 137551, 390180, 390181, 390183, 390184, 390185, 390191, 390200, 390182, 390189, 390197, 390198, 390187, 390188, 390186, 390194, 390193, 390196, 390192, 390190, 390201, 390199, 390203

-

1.2.1.11

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+

673074, 670165, 687340, 741702, 725219, 674667, 742070, 684192, 742704, 762956, 675505, 725944, 675355, 684158, 763308, 742287, 710717, 726268, 741540, 741535, 762575, 762696, 688468

-

1.2.1.11

L-aspartate 4-semialdehyde + vanadate + NADP+ = ?

390200

-

1.2.1.11

L-aspartate-4-semialdehyde + cacodylate + NADP+ = L-4-aspartyl cacodylate + NADPH

654110

-

1.2.1.11

L-aspartate-4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH

657153, 655821, 654891, 657298, 654110, 654103, 654112

-

1.1.1.3

5 entries

1.2.1.11

9 entries

1.4.1.B4

L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+ = carboxynorspermidine + NADP+ + H2O

719993

-

1.5.1.43

L-aspartate 4-semialdehyde + propane-1,3-diamine + NADH + H+ = carboxynorspermidine + H2O + NAD+

712623

-

1.5.1.43

L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ = carboxynorspermidine + H2O + NADP+

712623, 742792, 741488

-

1.5.1.43

L-aspartate 4-semialdehyde + putrescine + NADPH + H+ = carboxyspermidine + H2O + NADP+

719993, 741488, 742792, 712623

-

2.2.1.10

L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate

718845

-

2.2.1.10

L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate

692386

-

2.2.1.10

L-aspartate semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = ?

718838

-

1.5.1.43

3 entries

2.2.1.10

3 entries

2.6.1.46

L-2-amino-4-oxobutanoate + L-glutamate = L-2,4-diaminobutanoate + 2-oxoglutarate

640090, 640091

-

2.6.1.76

L-aspartate 4-semialdehyde + L-glutamate = L-2,4-diaminobutanoate + 2-oxoglutarate

640091

-

2.6.1.76

L-aspartate 4-semialdehyde + L-homoserine = L-2,4-diaminobutanoate + 4-hydroxy-2-oxobutanoic acid

640091

-

2.6.1.76

L-glutamic acid + L-aspartic beta-semialdehyde = L-2,4-diaminobutyric acid + 2-oxoglutaric acid

288732, 288731

-

2.6.1.76

3 entries

2.7.1.39

ATP + L-aspartate 4-semialdehyde = ?

641471, 641463

-

2.8.1.16

hydrogen sulfide + L-aspartate 4-semialdehyde + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = L-homocysteine + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster

752754

-

4.1.2.56

glycerone phosphate + L-aspartate 4-semialdehyde = 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate

722650

-

4.3.3.7

(S)-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + H2O

649771, 664244, 692356, 693141, 652939, 690252, 695011, 692255, 678046, 691294, 690914

-

4.3.3.7

(S)-aspartate-4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O

729062, 729385, 728904, 728889, 729237, 730908, 720852, 730915, 728891, 728886, 729694

-

4.3.3.7

L-aspartate 4-semialdehyde + pyruvate = (S)-2,3-dihydropyridine-2,6-dicarboxylate + 2 H2O

712704, 713953, 713969, 714351, 715195

-

4.3.3.7

L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O

702445, 701515, 705792, 701934, 702036, 702479, 701513, 704696, 702448, 702489, 702484

-

4.3.3.7

L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + H2O

664304, 664072, 691786, 706245, 690628, 691243

-

4.3.3.7

L-aspartate-4-semialdehyde + pyruvate = ?

33903, 33911, 33902, 33912, 33914

-

4.3.3.7

L-aspartate-4-semialdehyde + pyruvate = dihydrodipicolinate + H2O

33906, 33907, 33909, 33912, 33913, 33916, 33917, 33918, 33920, 33922, 33904, 33914, 4120, 33919, 33903, 33915, 33911, 33923, 33908, 33925, 33905, 33910, 33921, 33902

-

4.3.3.7

pyruvate + L-aspartate-4-semialdehyde = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O

747107, 748035, 730623, 718827, 746457, 730624, 746463, 746659, 746655, 749225, 749039

-

4.3.3.7

pyruvate + L-aspartate-4-semialdehyde = 2,3-dihydrodipicolinate + ?

746926

-

4.3.3.7

9 entries

Product in Enzyme-catalyzed Reactions (20 results)

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Show Product (20 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H

0, 246387, 246401, 246403, 246394, 246392, 246402

-

1.1.1.3

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+

0

-

1.1.1.3

L-homoserine + NAD+ = L-aspartate 4-semialdehyde + NADH

0

-

1.1.1.3

L-homoserine + NAD+ = L-aspartate 4-semialdehyde + NADH + H+

0

-

1.1.1.3

L-homoserine + NADP+ = L-aspartate 4-semialdehyde + NADPH

0

-

1.1.1.3

L-homoserine + NADP+ = L-aspartate 4-semialdehyde + NADPH + H+

0

-

1.2.1.11

L-4-aspartyl phosphate + NADPH + H+ = L-aspartate 4-semialdehyde + phosphate + NADP+

0

-

1.2.1.11

L-4-aspartyl phosphate + NADPH = L-aspartate 4-semialdehyde + phosphate + NADP+

390202, 390200, 390188, 0, 390199, 390203, 137551, 390182, 390187, 390189, 390183

-

1.2.1.11

L-4-aspartyl phosphate + NADPH = L-aspartate-4-semialdehyde + phosphate + NADP+

0

-

1.4.1.B4

carboxynorspermidine + NAD+ + H2O = L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADH + H+

0

-

1.4.1.B4

carboxynorspermidine + NADP+ + H2O = L-aspartic 4-semialdehyde + 1,3-diaminopropane + NADPH + H+

0

-

1.4.1.B4

carboxyspermidine + NADP+ + H2O = L-aspartic 4-semialdehyde + putrescine + NADPH + H+

0

-

1.5.1.43

carboxynorspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+

0

-

1.5.1.43

carboxyspermidine + H2O + NADP+ = L-aspartate 4-semialdehyde + putrescine + NADPH + H+

0

-

2.6.1.46

L-2,4-diaminobutanoate + pyruvate = L-2-amino-4-oxobutanoate + L-alanine

640089

-

2.6.1.46

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate

0

-

2.6.1.46

L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + L-alanine

0

-

2.6.1.76

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate

0

-

2.6.1.76

L-2,4-diaminobutyric acid + 2-oxoglutaric acid = L-glutamic acid + L-aspartic beta-semialdehyde

0

-

1.1.1.3

6 entries

1.2.1.11

3 entries

1.4.1.B4

3 entries

1.5.1.43

2 entries

2.6.1.46

3 entries

2.6.1.76

2 entries

4.1.1.86

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartic beta-semialdehyde + L-glutamic acid

0

-

Activator in Enzyme-catalyzed Reactions (1 result)

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Show Activating Compound (1 entry)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.1.8

crude extract

390613

-

Inhibitor in Enzyme-catalyzed Reactions (10 results)

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Show Inhibitors (10 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.39

mixed inhibition versus L-homoserine and ATP

641463

-

2.7.2.4

-

642314

-

4.3.1.1

-

6028

-

4.3.1.1

i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent

6009

-

4.3.3.7

-

693141

-

4.3.3.7

substrate inhibition

730915

-

4.3.3.7

competitive inhibition at high substrate concentrations

702484

-

4.3.3.7

DHDPS is subject to substrate inhibition by L-aspartate 4-semialdehyde

702448

-

4.3.3.7

is subject to substrate inhibition by high concentrations

702445

-

4.3.3.7

uncompetitive inhibition by high concentrations of, no overcome by increasing pyruvate concentrations from 5 to 15 mM

690628

-

4.3.1.1

2 entries

4.3.3.7

6 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (56 results)

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Show Turnover Number (56 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.3

2.8

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.1.1.3

9.68

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.1.1.3

11.58

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.1.1.3

12.98

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.1.1.3

19.3

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.1.1.3

22.58

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.2.1.11

0.12

-

pH and temperature not specified in the publication

710717

1.2.1.11

0.24

-

recombinant mutant R103L

654103

1.2.1.11

0.4

-

recombinant mutant R270K

654103

1.2.1.11

1.2

-

recombinant mutant R103K

654103

1.2.1.11

2

-

-

674667

1.2.1.11

3.2

-

recombinant mutant H277N, pH 9.0, 30°C

654110

1.2.1.11

4

-

recombinant mutant E243D

654103

1.2.1.11

11

-

recombinant mutant K246L

654103

1.2.1.11

58

-

gene II

390202

1.2.1.11

120

-

gene I

390202

1.2.1.11

160

-

-

390202

1.2.1.11

330

-

-

390202

1.2.1.11

330

-

recombinant wild-type enzyme

654103

1.2.1.11

330

-

recombinant wild-type enzyme, pH 9.0, 30°C

654110

1.1.1.3

6 entries

1.2.1.11

14 entries

2.7.1.39

2.1

-

wild-type enzyme

641471

4.1.2.56

0.2

-

pH 7.2, 30°C

722650

4.3.3.7

0.038

-

mutant enzyme R138H

664072

4.3.3.7

0.12

-

mutant T44V, pH 8.0, 30°C

652939

4.3.3.7

0.149

-

mutant enzyme R138A

664072

4.3.3.7

0.7

-

mutant Y133F, pH 8.0, 30°C

652939

4.3.3.7

6.5

-

Y107W mutant

690914

4.3.3.7

6.5

-

mutant D193Y, at 30°C

701934

4.3.3.7

9.8

-

pH 8.0, 30°C, recombinant wild-type enzyme

713953

4.3.3.7

10.8

-

mutant Y107F, pH 8.0, 30°C

652939

4.3.3.7

10.8

-

Y107F mutant

690914

4.3.3.7

12.4

-

mutant D193A, at 30°C

701934

4.3.3.7

34

-

pH 8.0, 30°C, untagged enzyme

749225

4.3.3.7

35

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168

714351

4.3.3.7

39

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237

714351

4.3.3.7

46

-

pH 8.0, 30°C, His-tagged enzyme

749225

4.3.3.7

52

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171

714351

4.3.3.7

56

-

pH 8.0, 30°C

749039

4.3.3.7

63

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237

714351

4.3.3.7

68

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237

714351

4.3.3.7

88

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237

714351

4.3.3.7

97

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171

714351

4.3.3.7

108

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171

714351

4.3.3.7

111

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168

714351

4.3.3.7

119

-

pH 8.0, 30°C, recombinant mutant A204R

713969

4.3.3.7

124

-

30°C

664244

4.3.3.7

124

-

wild-type

690914

4.3.3.7

124

-

wild-type enzyme, pH 8.0, 30°C

652939

4.3.3.7

134

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237

714351

4.3.3.7

136

-

pH not specified in the publication, 30°C, recombinant wild-type enzyme

714351

4.3.3.7

138

-

pH 8.0, 30°C, recombinant wild-type enzyme

713969

4.3.3.7

141

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237

714351

4.3.3.7

213

-

-

690628

4.3.3.7

223

-

-

33909

4.3.3.7

233

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171

714351

4.3.3.7

465

-

pH not specified in the publication, 45°C, recombinant wild-type enzyme

714351

4.3.3.7

34 entries

K_M Value (106 results)

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Show KM Value (106 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.3

0.04

-

isozyme II

246382

1.1.1.3

0.066

-

isozyme I

246382

1.1.1.3

0.08

-

threonine insensitive isozyme

246391

1.1.1.3

0.098

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.1.1.3

0.1

-

isozyme I

246382

1.1.1.3

0.13

0.15

threonine resistant isozyme

246388

1.1.1.3

0.15

-

threonine resistant isozyme

246385

1.1.1.3

0.15

-

threonine-resistant enzyme, pH and temperature not specified in the publication

246385

1.1.1.3

0.17

-

-

246387

1.1.1.3

0.24

0.25

threonine sensitive isozyme

246388

1.1.1.3

0.25

-

threonine sensitive isozyme

246385

1.1.1.3

0.25

-

threonine-sensitive enzyme, pH and temperature not specified in the publication

246385

1.1.1.3

0.36

0.4

isozyme II

246382

1.1.1.3

0.5

-

-

246395

1.1.1.3

0.5

-

threonine sensitive isozyme

246391

1.1.1.3

0.569

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.1.1.3

0.845

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.1.1.3

1.19

-

cosubstrate NADH, pH 8.0, 25°C

712490

1.1.1.3

1.25

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.1.1.3

2.19

-

cosubstrate NADPH, pH 8.0, 25°C

712490

1.2.1.11

0.03

-

recombinant mutant R103L

654103

1.2.1.11

0.1

-

recombinant mutant R103K and mutant K246L

654103

1.2.1.11

0.12

-

-

390202

1.2.1.11

0.16

-

gene II

390202

1.2.1.11

0.17

-

in 0.2 M bicine buffer, pH 8.6, at 25°C

725944

1.2.1.11

0.19

-

gene I

390202

1.2.1.11

0.2

-

-

390180, 390191

1.2.1.11

0.2

-

recombinant wild-type enzyme and mutant E243D

654103

1.2.1.11

0.2

-

recombinant wild-type enzyme, pH 9.0, 30°C

654110

1.2.1.11

0.24

-

-

390202

1.2.1.11

0.4

-

recombinant mutant R270K

654103

1.2.1.11

0.5

-

recombinant mutant H277N, pH 9.0, 30°C

654110

1.2.1.11

0.955

-

recombinant enzyme, pH 9.0, 30°C

655821

1.2.1.11

1.25

-

-

390201

1.2.1.11

2.6

-

-

390188

1.1.1.3

20 entries

1.2.1.11

15 entries

1.4.1.B4

4.68

-

pH 7.5, 37°C, Vmax: 35 micromol/min/mg carboxynorspermidine

712623

2.6.1.46

4.5

-

pH 8.5, 25ºC

640091

2.6.1.76

4.5

-

pH 8.5, 25°C

640091

2.7.1.39

0.28

-

wild-type enzyme

641471

2.7.1.39

0.58

-

pH 7.8

641463

2.7.1.39

2 entries

4.1.2.56

0.0056

-

pH 7.2, 30°C

722650

4.3.3.7

0.05

-

mutant L170E/G191E, at 30°C

704696

4.3.3.7

0.052

-

at 30°C, in 100 mM HEPES buffer, pH 8.0

702445

4.3.3.7

0.07

-

pH 8.0, 30°C

749039

4.3.3.7

0.08

-

pH 8.0, 30°C, untagged enzyme

749225

4.3.3.7

0.09

-

mutant T44V, pH 8.0, 30°C

652939

4.3.3.7

0.09

-

pH 8.0, 30°C, His-tagged enzyme

749225

4.3.3.7

0.11

-

30°C

664244

4.3.3.7

0.11

-

pH 8.0, 30°C, with pyruvate

649771

4.3.3.7

0.11

-

wild-type

690914

4.3.3.7

0.11

-

wild-type enzyme, pH 8.0, 30°C

652939

4.3.3.7

0.11

-

at 30°C, in 100 mM HEPES buffer, pH 8.0

702445

4.3.3.7

0.12

-

mutant K161R, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR

702489

4.3.3.7

0.12

-

wild-type, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR

702489

4.3.3.7

0.13

-

mutant T44S

702479

4.3.3.7

0.13

-

wild-type, at 30°C

701934

4.3.3.7

0.137

-

recombinant mutant H56K, pH 8.0, temperature not specified in the publication

729062

4.3.3.7

0.14

-

pH 8.0

664304

4.3.3.7

0.14

-

30°C, pH not specified in the publication

746463

4.3.3.7

0.15

-

mutants Q196D, D193A and D193Y, at 30°C

701934

4.3.3.7

0.15

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp237

714351

4.3.3.7

0.16

0.32

pH and temperature not specified in the publication

730915

4.3.3.7

0.17

-

mutant D193A, at 30°C

701934

4.3.3.7

0.17

-

pH 8.0, 37°C, recombinant His-tagged enzyme

715195

4.3.3.7

0.18

-

-

702448

4.3.3.7

0.18

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp237

714351

4.3.3.7

0.22

-

similar to those of DHDPS enzyme of Escherichia coli

693141

4.3.3.7

0.23

-

C-terminal truncated DHDPS (H225*), at 30°C, in 150 mM HEPES, pH 8.0, 0.16 mM NADPH, 50 microg/ml DHDPR

702036

4.3.3.7

0.23

-

mutant K161A, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR

702489

4.3.3.7

0.23

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171/Arg237

714351

4.3.3.7

0.23

-

pH not specified in the publication, 30°C, recombinant wild-type enzyme

714351

4.3.3.7

0.248

-

recombinant mutant E84T, pH 8.0, temperature not specified in the publication

729062

4.3.3.7

0.25

-

wild-type, at 30°C

704696

4.3.3.7

0.25

-

-

33907

4.3.3.7

0.29

-

polyhistidine-tagged wild-type DHDPSR

702036

4.3.3.7

0.3

-

recombinant wild-type enzyme, pH 8.0, temperature not specified in the publication

729062

4.3.3.7

0.32

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171/Arg237

714351

4.3.3.7

0.33

-

-

692356

4.3.3.7

0.36

-

pH not specified in the publication, 45°C, recombinant wild-type enzyme

714351

4.3.3.7

0.38

-

by adding 20 mM pyruvate, at 60°C

692255

4.3.3.7

0.39

-

Y107W mutant

690914

4.3.3.7

0.4

-

-

33915

4.3.3.7

0.42

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp171

714351

4.3.3.7

0.43

-

pH 8.0, 30°C, recombinant wild-type enzyme

713969

4.3.3.7

0.46

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp171

714351

4.3.3.7

0.46

-

-

33908

4.3.3.7

0.58

-

mutant Y107F, pH 8.0, 30°C

652939

4.3.3.7

0.58

-

Y107F mutant

690914

4.3.3.7

0.6

-

-

33911

4.3.3.7

0.63

-

reaction mixture includes 100 mM Tris-HCl, 2.5 mM pyruvate, 0.05-0.1 microg dihydrodipicolinate synthase and 0.2 mM NADPH, from 5.6 to 22.4 mM plots deviate from typical Michaelis-Menten kinetics, increased concentration fits an uncompetitive substrate inhibition model

690628

4.3.3.7

0.765

-

-

33910

4.3.3.7

0.8

-

-

33902

4.3.3.7

0.92

-

modeled with substrate inhibition, at 60°C

692255

4.3.3.7

1

-

-

33904, 33903

4.3.3.7

1.1

-

pH 8.0, 30°C, recombinant mutant A204R

713969

4.3.3.7

1.1

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp171

714351

4.3.3.7

1.2

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp237

714351

4.3.3.7

1.3

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168/Asp171

714351

4.3.3.7

1.5

-

pH not specified in the publication, 30°C, recombinant mutant DELTAAsp168

714351

4.3.3.7

1.7

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168/Asp237

714351

4.3.3.7

2.2

-

pH not specified in the publication, 45°C, recombinant mutant DELTAAsp168

714351

4.3.3.7

2.7

-

mutant Y133F, pH 8.0, 30°C

652939

4.3.3.7

3.13

-

-

33906

4.3.3.7

5

-

-

33905

4.3.3.7

5.1

-

mutant enzyme R138A

664072

4.3.3.7

37

-

mutant enzyme R138H

664072

4.3.3.7

65 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.3.3.7

0.07

-

substrate inhibition

693141

4.3.3.7

0.15

-

pH and temperature not specified in the publication

730915

4.3.3.7

5.4

-

-

702448

4.3.3.7

3 entries

References & Links

Literature References (173)

top print hide

Show Reference (173 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4120

-

Lysine biosynthesis in Methanobacterium thermoautotrophicum is by the diaminopimelic acid pathway

1984

Bakhiet, N.; Forney, F.W.; Stahly, D.P.; Daniels, L.

Curr. Microbiol.

10

195-198

6009

3003513

Aspartate ammonia-lyase

1985

Tokushige, M.

Methods Enzymol.

113

618-627

6028

9169023

Mapping the mechanism-based modification sites in L-aspartase from Escherichia coli

1997

Giorgianni, F.; Beranova, S.; Wesdemiotis, C.; Viola, R.E.

Arch. Biochem. Biophys.

341

329-336

33902

16665646

Purification and characterization of dihydrodipicolinate synthase from wheat suspension cultures

1987

Kumpaisal, R.; Hashimoto, T.; Yamada, Y.

Plant Physiol.

85

145-151

33903

-

Spinach leaf dihydrodipicolinate synthase: partial purification and characterization

1981

Wallsgrove, R.M.; Mazelis, M.

Phytochemistry

20

2651-2655

33904

598503

The enzymology of lysine biosynthesis in higher plants. The occurrence, characterization and some regulatory properties of dihydrodipicolinate synthase

1977

Mazelis, M.; Watley, F.R.; Whatley, J.

FEBS Lett.

84

236-240

33905

1009127

Dihydrodipicolinic acid synthase of Bacillus licheniformis. Quaternary structure, kinetics, and stability in the presence of sodium chloride and substrates

1976

Halling, S.M.; Stahly, D.P.

Biochim. Biophys. Acta

452

580-596

33906

4215809

Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis

1974

Yamakura, F.; Ikeda, Y.; Kimura, K.; Sasakawa, T.

J. Biochem.

76

611-621

33907

-

Pyruvate-aspartic semialdehyde condensing enzyme (Escherichia coli)

1971

Shedlarski, J.G.

Methods Enzymol.

17B

129-134

33908

4983642

Partial purification and characterization of dihydrodipicolinic acid synthetase from sporulating Bacillus megaterium

1970

Webster, F.H.; Lechowich, R.V.

J. Bacteriol.

101

118-126

33909

4910051

The pyruvate-aspartic semialdehyde condensing enzyme of Escherichia coli

1970

Shedlarski, J.G.; Gilvarg, C.

J. Biol. Chem.

245

1362-1373

33910

4901235

Dihydrodipicolinic acid synthase of Bacillus licheniformis

1969

Stahly, D.P.

Biochim. Biophys. Acta

191

439-451

33911

16668206

Isolation and characterization of dihydrodipicolinate synthase from maize

1991

Frisch, D.A.; Gengenbach, B.G.; Tommy, A.M.; Sellner, J.M.; Somers, D.A.; Myers, D.E.

Plant Physiol.

96

444-452

33912

-

Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization

1992

Laber, B.; Gomis-Rueth, F.X.; Romao, M.J.; Huber, R.

Biochem. J.

268

691-695

33913

7853400

The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution

1995

Mirwaldt, C.; Korndoerfer, I.; Huber, R.

J. Mol. Biol.

246

227-239

33914

8206742

Regulation of dihydrodipicolinate synthase and diaminopimelate decarboxylase activity in Bacillus stearothermophilus

1994

Selli, A.; Crociani, F.; DiGioia, D.; Fava, F.; Crisetig, G.; Matteuzzi, D.

Ital. J. Biochem.

43

29-35

33915

16668753

Purification and characterization of dihydrodipicolinate synthase from pea

1991

Dereppe, C.; Bold, G.; Ghisalba, O.; Ebert, E.; Schaer, H.P.

Plant Physiol.

98

813-821

33916

1643284

Regulation of lysine synthesis in transgenic potato plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts

1992

Perl, A.; Shaul, O.; Galili, G.

Plant Mol. Biol.

19

815-823

33917

8251629

Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase

1993

Shaul, O.; Galili, G.

Plant Mol. Biol.

23

759-768

33918

-

Pyridine and piperidine derivatives as inhibitors of dihydrdipicolinic acid synthase, a key enzyme in the diaminopimelate pathway to L-lysine

1994

Couper, L.; McKendrick, J.E.; Robins, D.J.

Bioorg. Med. Chem. Lett.

4

2267-2272

33919

8980513

Engineering of the aspartate family biosynthetic pathway in barley (Hordeum vulgare L.) by transformation with heterologous genes encoding feed-back-insensitive aspartate kinase and dihydrodipicolinate synthase

1996

Brinch-Pedersen, H.; Galili, G.; Knudsen, S.; Holm, P.B.

Plant Mol. Biol.

32

611-620

33920

9048556

Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine

1997

Karsten, W.E.

Biochemistry

36

1730-1739

33921

9417939

Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure

1997

Blickling, S.; Beisel, H.G.; Bozic, D.; Knaeblein, J.; Laber, B.; Huber, R.

J. Mol. Biol.

274

608-621

33922

9165072

Feedback inhibition of dihydrodipicolinate synthase enzymes by L-lysine

1997

Blickling, S.; Knaeblein, J.

Biol. Chem.

378

207-210

33923

10350084

The Arabidopsis thaliana dhdps gene encoding dihydrodipicolinate synthase, key enzyme of lysine biosynthesis, is expressed in a cell-specific manner

1990

Vauterin, M.; Frankhard, V.; Jacobs, M.

Plant Mol. Biol.

39

695-708

33925

2129555

Nucleotide sequence of the dapA gene from Corynebacterium glutamicum

1990

Bonnassie, S.; Oreglia, J.; Sicard, A.M.

Nucleic Acids Res.

18

6421

137551

6150934

Interaction of aspartate and aspartate-derived antimetabolites with the enzymes of the threonine biosynthetic pathway of Escherichia coli

1984

Shames, S.L.; Ash, D.E.; Wedler, F.C.; Villafranca, J.J.

J. Biol. Chem.

259

15331-15339

246382

24301152

Localisation and characterisation of homoserine dehydrogenase isolated from barley and pea leaves

1981

Sainis, J.K.; Mayne, R.G.; Wallsgrove, R.M.; Lea, P.J.; Miflin, B.J.

Planta

152

491-496

246385

762132

Isolation and characterization of two homoserine dehydrogenases from maize suspension cultures

1979

Walter, T.J.; Connelly, J.A.; Gengenbach, B.G.; Wold, F.

J. Biol. Chem.

254

1349-1355

246387

8444866

Kinetic and regulatory mechanisms for (Escherichia coli) homoserine dehydrogenase-I

1993

Wedler, F.C.; Ley, B.W.

J. Biol. Chem.

268

4880-4888

246388

-

Comparison of homoserine dehydrogenase from different plant sources

1980

Grego, S.; Tricoli, D.; Di Marco, G.

Phytochemistry

19

1619-1623

246390

974097

Reaction of Tris with aldehydes. Effect of Tris on reactions catalyzed by homoserine dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase

1976

Ogilvie, J.W.; Whitaker, S.C.

Biochim. Biophys. Acta

445

525-536

246391

-

Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum

1974

Aarnes, H.; Rognes, S.E.

Phytochemistry

13

2717-2724

246392

4144654

Properties of homoserine dehydrogenase in a thermophilic bacterium

1973

Cavari, B.Z.; Grossowicz, N.

Biochim. Biophys. Acta

302

183-190

246393

4781056

Studies on homoserine dehydrogenase from an extreme thermophile, Thermus flavus AT-62. Partial purification and properties

1973

Saiki, T.; Shinshi, H.; Arima, K.

J. Biochem.

74

1239-1248

246394

-

Engineering the homoserine dehydrogenase and threonine dehydratase control points to analyse flux towards L-isoleucine in Corynebacterium glutamicum

1996

Morbach, S.; Kelle, R.; Winkels, S.; Sahm, H.; Eggeling, L.

Appl. Microbiol. Biotechnol.

45

612-620

246395

7549965

Purification and characterization of homoserine dehydrogenase from spinach leaves

1995

Pavagi, S.; Kochhar, S.; Kochhar, V.K.; Sane, P.V.

Biochem. Mol. Biol. Int.

36

649-658

246396

10700284

Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases

2000

DeLaBarre, B.; Thompson, P.R.; Wright, G.D.; Berghuis, A.M.

Nat. Struct. Biol.

7

238-244

246398

1907968

Inhibition of homoserine dehydrogenase I by L-serine in Escherichia coli

1991

Hama, H.; Kayahara, T.; Tsuda, M.; Tsuchiya, T.

J. Biochem.

109

604-608

246401

11341915

Homoserine dehydrogenase from Saccharomyces cerevisiae: kinetic mechanism and stereochemistry of hydride transfer

2001

Jacques, S.L.; Ejim, L.J.; Wright, G.D.

Biochim. Biophys. Acta

1544

42-54

246402

11341914

Characterization of yeast homoserine dehydrogenase, an antifungal target: the invariant histidine 309 is important for enzyme integrity

2001

Jacques, S.L.; Nieman, C.; Bareich, D.; Broadhead, G.; Kinach, R.; Honek, J.F.; Wright, G.D.

Biochim. Biophys. Acta

1544

28-41

246403

8432719

Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by using site-directed mutagenesis

1993

Omori, K.; Komatsubara, S.

J. Bacteriol.

175

959-965

288731

9260954

Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii

1997

Ikai, H.; Yamamoto, S.

J. Bacteriol.

179

5118-5125

288732

9514614

Two genes involved in the 1,3-diaminopropane production pathway in Haemophilus influenzae

1998

Ikai, H.; Yamamoto, S.

Biol. Pharm. Bull.

21

170-173

390180

-

Aspartic semialdehyde dehydrogenase (Escherichia coli K12)

1970

Hegeman, G.D.; Cohen, G.N.; Morgan, R.

Methods Enzymol.

17A

708-713

390181

2868399

Aspartate-semialdehyde dehydrogenase from Escherichia coli

1985

Cohen, G.N.

Methods Enzymol.

113

600-602

390182

4145650

Purification and characterization of aspartic -semialdehyde dehydrogenase from yeast and purification of an isozyme of glyceraldehyde-3-phosphate dehydrogenase

1973

Holland, M.J.; Westhead, E.W.

Biochemistry

12

2264-2270

390183

6102909

Aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Purification and general properties

1980

Biellmann, J.F.; Eid, P.; Hirth, C.; Jörnvall, H.

Eur. J. Biochem.

104

53-58

390184

6102911

Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue

1980

Bielmann, J.F.; Eid, P.; Hirth, C.

Eur. J. Biochem.

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