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Ligand L-homoserine

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

methionine metabolism, threonine metabolism

KEGG

Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Cysteine and methionine metabolism, Glycine, serine and threonine metabolism, Lysine biosynthesis, Microbial metabolism in diverse environments, Sulfur metabolism more

MetaCyc

canavanine biosynthesis, canavanine degradation, fusarin C biosynthesis, L-homocysteine biosynthesis, L-homoserine biosynthesis, L-methionine biosynthesis I, L-methionine biosynthesis II, L-threonine biosynthesis more

Show all BRENDA pathways known for L-homoserine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (31 results)

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Show Natural Substrate (31 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

688167

1ebu, 3D-view

1.1.1.3

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

688167

5xdf, 3D-view

1.1.1.3

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

688167

6a0s, 3D-view

1.1.1.3

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

688167

6a0t, 3D-view

1.1.1.3

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

688167

6a0u, 3D-view

1.1.1.3

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

739972

1ebu, 3D-view

1.1.1.3

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

739972

5xdf, 3D-view

1.1.1.3

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

739972

6a0s, 3D-view

1.1.1.3

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

739972

6a0t, 3D-view

1.1.1.3

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

739972

6a0u, 3D-view

1.1.1.3

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

741408, 762359, 762453, 760354, 761712, 760402, 761404

1ebu, 3D-view

1.1.1.3

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

741408, 762359, 762453, 760354, 761712, 760402, 761404

5xdf, 3D-view

1.1.1.3

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

741408, 762359, 762453, 760354, 761712, 760402, 761404

6a0s, 3D-view

1.1.1.3

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

741408, 762359, 762453, 760354, 761712, 760402, 761404

6a0t, 3D-view

1.1.1.3

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

741408, 762359, 762453, 760354, 761712, 760402, 761404

6a0u, 3D-view

1.1.1.3

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

657018

1ebu, 3D-view

1.1.1.3

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

657018

5xdf, 3D-view

1.1.1.3

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

657018

6a0s, 3D-view

1.1.1.3

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

657018

6a0t, 3D-view

1.1.1.3

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

657018

6a0u, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404

1ebu, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404

5xdf, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404

6a0s, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404

6a0t, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404

6a0u, 3D-view

2.3.1.31

acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine

735393, 736358, 758449, 755982, 486786, 486788, 486781, 486789, 486787, 658488, 671984, 687796

6ioh, 3D-view

2.3.1.31

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

687796

6ioh, 3D-view

1.1.1.3

25 entries

2.3.1.31

2 entries

2.3.1.46

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

487045, 671625, 701784, 735854, 737132, 755666, 757283, 487043, 487046, 671413, 672232

2vdj, 3D-view

2.7.1.39

ATP + L-homoserine = ADP + O-phospho-L-homoserine

737948, 758579, 759641, 641475, 641471, 641473, 641468, 641467, 641469, 641472, 641461, 641462, 641476, 641464, 662779, 661325, 663091

1h72, 3D-view

4.4.1.1

L-homoserine + H2O = 2-oxobutanoate + NH3 + H2O

708517

-

4.4.1.1

L-homoserine = 2-oxobutyrate + NH3

721432

-

4.4.1.1

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (16 results)

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Show Natural Product (16 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)+

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

3.13.2.2

S-adenosyl-L-methionine + H2O = L-homoserine + S-methyl-5'-thioadenosine

0

-

3.13.2.2

S-adenosyl-L-methionine + H2O = methylthioadenosine + L-homoserine

246556, 246557, 246558, 246559, 246560, 246561, 246562

-

3.5.1.97

N-3-oxododecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + 3-oxododecanoic acid

0

-

3.5.1.97

N-dodecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + dodecanoic acid

0

-

3.5.1.97

N-tetradecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + tetradecanoic acid

0

-

3.5.1.97

N-undecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + undecanoic acid

0

-

1.1.1.3

10 entries

3.13.2.2

2 entries

3.5.1.97

4 entries

Substrate in Enzyme-catalyzed Reactions (81 results)

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Show Substrate (81 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

246393, 246387, 246390, 246401, 246388, 246382, 246395, 246391, 246403, 246394, 246392, 688167, 246402

1ebu, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246401, 246388, 246382, 246395, 246391, 246403, 246394, 246392, 688167, 246402

5xdf, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246401, 246388, 246382, 246395, 246391, 246403, 246394, 246392, 688167, 246402

6a0s, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246401, 246388, 246382, 246395, 246391, 246403, 246394, 246392, 688167, 246402

6a0t, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246401, 246388, 246382, 246395, 246391, 246403, 246394, 246392, 688167, 246402

6a0u, 3D-view

1.1.1.3

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

739972

1ebu, 3D-view

1.1.1.3

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

739972

5xdf, 3D-view

1.1.1.3

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

739972

6a0s, 3D-view

1.1.1.3

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

739972

6a0t, 3D-view

1.1.1.3

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

739972

6a0u, 3D-view

1.1.1.3

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

712490

1ebu, 3D-view

1.1.1.3

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

712490

5xdf, 3D-view

1.1.1.3

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

712490

6a0s, 3D-view

1.1.1.3

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

712490

6a0t, 3D-view

1.1.1.3

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

712490

6a0u, 3D-view

1.1.1.3

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

741408, 762359, 739972, 762453, 760354, 761712, 760402, 761404

1ebu, 3D-view

1.1.1.3

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

741408, 762359, 739972, 762453, 760354, 761712, 760402, 761404

5xdf, 3D-view

1.1.1.3

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

741408, 762359, 739972, 762453, 760354, 761712, 760402, 761404

6a0s, 3D-view

1.1.1.3

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

741408, 762359, 739972, 762453, 760354, 761712, 760402, 761404

6a0t, 3D-view

1.1.1.3

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

741408, 762359, 739972, 762453, 760354, 761712, 760402, 761404

6a0u, 3D-view

1.1.1.3

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

657018, 642341, 642340, 712490

1ebu, 3D-view

1.1.1.3

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

657018, 642341, 642340, 712490

5xdf, 3D-view

1.1.1.3

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

657018, 642341, 642340, 712490

6a0s, 3D-view

1.1.1.3

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

657018, 642341, 642340, 712490

6a0t, 3D-view

1.1.1.3

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

657018, 642341, 642340, 712490

6a0u, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404, 741408

1ebu, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404, 741408

5xdf, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404, 741408

6a0s, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404, 741408

6a0t, 3D-view

1.1.1.3

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

740860, 762359, 738802, 739791, 739804, 740548, 762453, 761687, 760736, 761404, 741408

6a0u, 3D-view

1.1.1.3

30 entries

1.4.1.1

L-homoserine + H2O + NAD+ = 4-hydroxy-2-oxobutanoate + NH3 + NADH

743722

-

1.4.1.4

L-homoserine + H2O + NAD+ = 4-hydroxy-2-oxobutanoate + NH3 + NADH

742178

-

1.4.3.2

L-homoserine + H2O + O2 = 2-oxo-4-hydroxybutyric acid + NH3 + H2O2

711874

-

2.1.1.280

S-adenosyl-L-methionine + L-homoserine = ?

692948

-

2.3.1.31

acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine

735393, 719673, 486779, 486783, 687796, 486782, 684480, 658488, 486787, 672001, 684874, 736358, 758449, 755982, 486786, 486784, 486781, 486780, 486788, 486789, 671984, 673497

6ioh, 3D-view

2.3.1.31

beta-hydroxybutyryl-CoA + L-homoserine = CoA + beta-hydroxybutyryl-L-homoserine

673497

6ioh, 3D-view

2.3.1.31

butyryl-CoA + L-homoserine = CoA + O-butyryl-L-homoserine

486788, 671984

6ioh, 3D-view

2.3.1.31

crotonyl-CoA + L-homoserine = CoA + O-crotonyl-L-homoserine

486788

6ioh, 3D-view

2.3.1.31

glutaryl-CoA + L-homoserine = CoA + O-glutaryl-L-homoserine

673497, 486788

6ioh, 3D-view

2.3.1.31

isobutyryl-CoA + L-homoserine = CoA + O-isobutyryl-L-homoserine

673497

6ioh, 3D-view

2.3.1.31

malonyl-CoA + L-homoserine = CoA + O-malonyl-L-homoserine

673497

6ioh, 3D-view

2.3.1.31

propionyl-CoA + L-homoserine = CoA + O-propionyl-L-homoserine

486788, 671984, 673497

6ioh, 3D-view

2.3.1.31

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

673497, 486788, 687796

6ioh, 3D-view

2.3.1.46

glutaryl-CoA + L-homoserine = CoA + O-glutaryl-L-homoserine

487046

2vdj, 3D-view

2.3.1.46

succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine

487045, 487043, 487044, 671413, 671625, 672232, 701784, 487046, 735854, 737132, 755666, 757283

2vdj, 3D-view

2.3.1.31

9 entries

2.3.1.46

2 entries

2.3.1.58

oxalyl-CoA + L-homoserine = ?

487271

-

2.5.1.47

L-homoserine + sulfide = ?

637383

-

2.5.1.49

L-homoserine + H2S = homocysteine + ?

637834, 637839

-

2.5.1.49

L-homoserine + H2S = L-homocysteine + H2O

661358

-

2.5.1.49

L-homoserine + KCN = ?

662480

-

2.6.1.14

2-oxosuccinamic acid + L-homoserine = L-asparagine + 4-hydroxy-2-oxobutanoate

637253

-

2.6.1.14

phenylpyruvate + L-homoserine = phenylalanine + 4-hydroxy-2-oxobutanoate

637254

-

2.6.1.15

2-oxoglutaramate + L-homoserine = L-glutamine + 4-hydroxy-2-oxobutanoate

639898

-

2.6.1.15

glyoxylate + L-homoserine = glycine + 4-hydroxy-2-oxobutanoate

639901, 639898

-

2.5.1.49

3 entries

2.6.1.14

2 entries

2.6.1.15

2 entries

2.6.1.42

L-homoserine + 2-oxobutyrate = ? + 2-aminobutyrate

758697

-

2.6.1.52

L-homoserine + 2-oxoglutarate = 4-hydroxy-2-oxobutyrate + L-glutamate

758955

-

2.6.1.73

L-homoserine + glyoxylate = 4-hydroxy-2-oxobutanoate + glycine

636989

-

2.6.1.76

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

640091

-

2.7.1.39

ATP + L-homoserine = ADP + O-phospho-L-homoserine

641463, 641465, 641470, 641471, 641473, 641468, 641469, 722151, 722152, 641467, 641460, 641461, 641476, 661325, 722043, 641466, 641462, 662779, 641464, 641474, 704525, 673979, 641472, 663091, 737948, 641475, 758579, 759641

1h72, 3D-view

2.7.1.39

L-homoserine + ATP = O-phospho-L-homoserine + ADP

704525

1h72, 3D-view

2.7.1.39

2 entries

4.3.1.19

L-homoserine = 2-oxobutanoate + NH3 + H2O

210821

-

4.4.1.1

D-Cys + L-homoserine = D-allocystathionine

34489, 34505, 34484

-

4.4.1.1

L-homoserine + 2-mercaptoethanol = S-hydroxyethyl-L-homocysteine

34489

-

4.4.1.1

L-homoserine + 2-mercaptopropionate = S-methylcarboxymethyl-L-homocysteine

34489, 34505, 34484

-

4.4.1.1

L-homoserine + 3-mercaptopropionate = S-carboxyethyl-L-homocysteine

34489, 34505, 34484

-

4.4.1.1

L-homoserine + 4-mercaptobutanoate = S-carboxy-n-propyl-L-homocysteine

34489

-

4.4.1.1

L-homoserine + D-homocysteine = meso-homolanthionine

34489, 34505

-

4.4.1.1

L-homoserine + H2O = 2-oxobutanoate + NH3 + H2O

707582, 709040, 708133, 708517

-

4.4.1.1

L-homoserine + H2O = H2O + NH3 + 2-oxobutanoate

709005

-

4.4.1.1

L-homoserine + H2O = NH3 + ?

651810

-

4.4.1.1

L-homoserine + L-Cys = L-cystathionine

34484, 34489, 34504

-

4.4.1.1

L-homoserine + L-homocysteine = L-homolanthionine

34489, 34505

-

4.4.1.1

L-homoserine + thioglycerol = S-(2,3-dihydroxypropyl)-L-homocysteine

34489

-

4.4.1.1

L-homoserine + thioglycolate = S-carboxymethyl-L-homocysteine

34489

-

4.4.1.1

L-homoserine = 2-oxobutyrate + NH3

721432

-

4.4.1.1

L-homoserine = ?

34506, 34504, 34487, 34499, 5584, 34484, 586904

-

4.4.1.11

L-homoserine + H2O = ?

701880

-

4.4.1.11

L-homoserine = NH3 + 2-oxobutanoate

649323

-

4.4.1.1

15 entries

4.4.1.11

2 entries

5.1.1.10

L-homoserine = D-homoserine

2045, 2047, 746725

-

6.3.2.13

ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-homoserine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-homoserine

744440

-

6.3.2.2

ATP + L-Glu + L-homoserine = ADP + phosphate + gamma-L-Glu-L-homoserine

649263, 1126

-

Product in Enzyme-catalyzed Reactions (44 results)

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Show Product (44 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246398, 0, 246401, 246382, 246395, 246388, 246391, 246403, 246392, 246396, 246402

1ebu, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246398, 0, 246401, 246382, 246395, 246388, 246391, 246403, 246392, 246396, 246402

5xdf, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246398, 0, 246401, 246382, 246395, 246388, 246391, 246403, 246392, 246396, 246402

6a0s, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246398, 0, 246401, 246382, 246395, 246388, 246391, 246403, 246392, 246396, 246402

6a0t, 3D-view

1.1.1.3

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

246393, 246387, 246390, 246398, 0, 246401, 246382, 246395, 246388, 246391, 246403, 246392, 246396, 246402

6a0u, 3D-view

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

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

0

1ebu, 3D-view

1.1.1.3

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

0

5xdf, 3D-view

1.1.1.3

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

0

6a0s, 3D-view

1.1.1.3

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

0

6a0t, 3D-view

1.1.1.3

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

0

6a0u, 3D-view

1.1.1.3

30 entries

3.1.1.81

L-homoserine lactone + H2O = L-homoserine

0

-

3.13.2.2

S-adenosyl-L-methionine + H2O = L-homoserine + S-methyl-5'-thioadenosine

0

-

3.13.2.2

S-adenosyl-L-methionine + H2O = methylthioadenosine + L-homoserine

246556, 246557, 246558, 246559, 246560, 246561, 246562

-

3.13.2.2

S-adenosyl-L-methionine chloride + H2O = ? + L-homoserine

246555

-

3.13.2.2

S-adenosyl-L-methionine iodide + H2O = ? + L-homoserine

246555

-

3.13.2.2

S-methylmethionine + H2O = L-homoserine + dimethylsulfide

649259

-

3.13.2.2

5 entries

3.4.11.2

L-hSer-7-amido-4-carbamoylmethylcoumarin + H2O = L-hSer + 7-amino-4-carbamoylmethylcoumarin

0

-

3.5.1.97

N-3-oxododecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + 3-oxododecanoic acid

0

-

3.5.1.97

N-dodecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + dodecanoic acid

0

-

3.5.1.97

N-heptanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + heptanoic acid

0

-

3.5.1.97

N-octanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + octanoic acid

0

-

3.5.1.97

N-tetradecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + tetradecanoic acid

0

-

3.5.1.97

N-undecanoyl-(S)-homoserine lactone + H2O = (S)-homoserine + undecanoic acid

0

-

3.5.1.97

6 entries

5.1.1.10

D-homoserine = L-homoserine

0

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.95

-

763108

-

1.1.1.95

10 mM, activates

763716

-

1.1.1.95

2 entries

Inhibitor in Enzyme-catalyzed Reactions (19 results)

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Show Inhibitors (19 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.95

-

287525

-

1.14.13.195

competitive inhibition

704269

-

1.4.1.13

-

391448

-

1.4.1.13

significant inhibitor

391438, 391447

-

1.4.1.13

2 entries

1.4.1.4

competitive inhibitor with respect to both ammonia and glutamine

391686

-

2.3.1.30

weak

34691, 486773

-

2.5.1.47

-

637330

-

2.5.1.47

non-competitive

637334

-

2.5.1.49

-

637830, 637832

-

2.5.1.49

competitive inhibition

637825

-

2.7.1.39

-

641468, 641471

1h72, 3D-view

2.7.1.39

above 0.75 mM

641463

1h72, 3D-view

2.7.1.39

substrate inhibition

641473

1h72, 3D-view

2.5.1.47

2 entries

2.5.1.49

2 entries

2.7.1.39

3 entries

2.7.1.81

40 mM, weak inhibition

642034

-

2.7.2.4

-

642329

-

2.7.2.4

inhibits the activity of aspartokinase encoded by metL

760402

-

2.7.2.4

2 entries

2.7.8.4

27-34% inhibition of the reaction

643775

-

4.1.99.2

-

678401

-

4.3.3.7

1 mM, 13% inhibition

33904

-

3D Structure of Enzyme-Ligand-Complex (PDB) (29 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (29 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.1.1.3

1ebu, 3D-view

1.1.1.3

5xdf, 3D-view

1.1.1.3

6a0s, 3D-view

1.1.1.3

6a0t, 3D-view

1.1.1.3

6a0u, 3D-view

1.1.1.3

1ebu, 3D-view

1.1.1.3

5xdf, 3D-view

1.1.1.3

6a0s, 3D-view

1.1.1.3

6a0t, 3D-view

1.1.1.3

6a0u, 3D-view

1.1.1.3

1ebu, 3D-view

1.1.1.3

5xdf, 3D-view

1.1.1.3

6a0s, 3D-view

1.1.1.3

6a0t, 3D-view

1.1.1.3

6a0u, 3D-view

1.1.1.3

15 entries

1.2.1.11

1pqp, 3D-view

1.8.4.2

3dks, 3D-view

2.3.1.31

6ioh, 3D-view

2.3.1.46

2vdj, 3D-view

2.7.1.39

1h72, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

9 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (41 results)

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Show Turnover Number (41 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.3

0.042

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

0.052

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

0.07

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

0.24

-

recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity

654640

1.1.1.3

0.51

-

recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity

654640

1.1.1.3

1.07

-

pH 9.0, 25°C, recombinant enzyme

761687

1.1.1.3

1.43

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

3.3

-

recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity

654640

1.1.1.3

7

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

10.15

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

24

-

recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity

654640

2.3.1.31

0.22

-

recombinant His-tagged mutant G52A enzyme, pH 8.0, 30°C

736358

2.3.1.31

0.63

-

recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C

736358

2.3.1.31

0.78

-

recombinant His-tagged mutant G52A/P55G enzyme, pH 8.0, 30°C

736358

2.3.1.31

1.47

-

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

736358

2.3.1.31

1.67

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

2.918

-

recombinant His-tagged enzyme, pH 8.0, 22°C

755982

2.3.1.31

8.4

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

9.6

-

21°C, pH 8.0, wild-type enzyme

671984

2.3.1.31

13.4

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

23

-

25°C, pH 7.5

673497

2.3.1.31

92

-

-

486788

2.3.1.31

122

-

-

684480

2.3.1.46

0.034

-

pH 7.2, 25°C, recombinant mutant K47A

672232

2.3.1.46

1.8

-

pH 7.2, 25°C, recombinant mutant K47R

672232

2.3.1.46

2

-

pH 7.2, 25°C, recombinant mutant K46R/K47R

672232

2.3.1.46

4.1

-

pH 7.2, 25°C, recombinant mutant K46A

672232

2.3.1.46

24

-

recombinant protein

487046

2.3.1.46

36.72

-

recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication

735854

2.3.1.46

37

-

pH 7.2, 25°C, recombinant mutant K46R

672232

2.3.1.46

38.59

-

recombinant His-tagged mutant I124L, pH and temperature not specified in the publication

735854

2.3.1.46

39.28

-

recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication

735854

2.3.1.46

130

-

pH 7.2, 25°C, recombinant mutant C90S

672232

2.3.1.46

130

-

pH 7.2, 25°C, recombinant wild-type enzyme

672232

2.7.1.39

0.2

-

mutant R234L

641471

2.7.1.39

0.75

-

method: isothermal titration calometry

704525

2.7.1.39

9.1

-

mutant H202L

641471

2.7.1.39

11.2

-

in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37°C

722043

2.7.1.39

18.3

-

wild-type enzyme

641471

2.7.1.39

40.2

-

pH 7.5, 30°C

661325

1.1.1.3

11 entries

2.3.1.31

12 entries

2.3.1.46

11 entries

2.7.1.39

6 entries

4.4.1.11

1.4

-

-

701880

K_M Value (112 results)

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Show KM Value (112 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.3

0.013

-

-

246387

1.1.1.3

0.2

-

pH 10.0, 50°C, recombinant enzyme, with NADP+

761404

1.1.1.3

0.21

-

pH 8.0, 30°C, oxidized enzyme

739972

1.1.1.3

0.275

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

0.41

-

recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity

654640

1.1.1.3

0.54

-

pH 8.0, 30°C, reduced enzyme

739972

1.1.1.3

0.68

-

recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity

654640

1.1.1.3

0.69

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

1.08

-

cosubstrate NADP+, pH 8.0, 25°C

712490

1.1.1.3

1.08

-

pH 9.5, 50°C, recombinant enzyme, with NAD+

761404

1.1.1.3

1.2

-

recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity

654640

1.1.1.3

1.81

-

recombinant enzyme, pH 10.5, 55°C

760736

1.1.1.3

5.2

-

pH 8.0, 37°C, purified recombinant soluble enzyme

642340

1.1.1.3

6.1

-

pH 9.0, 50°C, recombinant enzyme

741408

1.1.1.3

9.57

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

13.4

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

17.2

-

recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity

654640

1.1.1.3

17.4

-

cosubstrate NAD+, pH 8.0, 25°C

712490

1.1.1.3

35.08

-

pH 9.0, 25°C, recombinant enzyme

761687

2.3.1.31

0.06

-

recombinant His-tagged enzyme, pH 8.0, 22°C

755982

2.3.1.31

0.13

-

-

486788

2.3.1.31

0.2

-

-

486782

2.3.1.31

0.2

-

E111G, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM succinyl-CoA, 25°C

687796

2.3.1.31

0.214

-

wild-type

687796

2.3.1.31

0.214

-

wild-type, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

0.24

-

25°C, pH 7.5

673497

2.3.1.31

0.287

-

E237Q, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

0.287

-

mutant E237Q

687796

2.3.1.31

0.405

-

E237D, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

0.405

-

mutant E237D

687796

2.3.1.31

0.85

-

E237A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

0.85

-

mutant E237A

687796

2.3.1.31

0.946

-

K47R, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

0.946

-

mutant K47R

687796

2.3.1.31

0.96

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

1

-

-

486784

2.3.1.31

1

-

recombinant His-tagged mutant P55G enzyme, pH 8.0, 30°C

736358

2.3.1.31

1.02

-

mutant S192A

687796

2.3.1.31

1.02

-

S192A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

1.09

-

21°C, pH 8.0, wild-type enzyme

671984

2.3.1.31

1.15

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

1.3

-

-

486779

2.3.1.31

1.38

-

K47M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

1.38

-

mutant K47M

687796

2.3.1.31

1.6

-

-

684874

2.3.1.31

2

-

recombinant His-tagged mutant G52A/P55G enzyme, pH 8.0, 30°C

736358

2.3.1.31

2.78

-

K163M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

2.78

-

mutant K163M

687796

2.3.1.31

2.8

-

-

486781

2.3.1.31

2.95

-

E250A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

2.95

-

mutant E250A

687796

2.3.1.31

6.43

-

21°C, pH 8.0, mutant enzyme

671984

2.3.1.31

10

-

exchange reaction

486782

2.3.1.31

13.8

-

mutant R249M

687796

2.3.1.31

13.8

-

R249M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C

687796

2.3.1.31

25

-

recombinant His-tagged mutant G52A enzyme, pH 8.0, 30°C

736358

2.3.1.31

98

-

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

736358

2.3.1.46

0.0032

-

pH 7.2, 25°C, recombinant mutant K47A

672232

2.3.1.46

0.027

-

pH 7.2, 25°C, recombinant mutant K46R/K47R

672232

2.3.1.46

0.044

-

pH 7.2, 25°C, recombinant mutant K46A

672232

2.3.1.46

0.044

-

pH 7.5, 25°C, recombinant mutant K45L

671625

2.3.1.46

0.049

-

pH 7.2, 25°C, recombinant mutant K47R

672232

2.3.1.46

0.31

-

pH 7.5, 25°C, recombinant mutant R193K

671625

2.3.1.46

0.36

-

pH 7.5, 25°C, recombinant mutant E237D

671625

2.3.1.46

0.38

-

pH 7.5, 25°C, recombinant wild-type enzyme

671625

2.3.1.46

0.58

-

pH 7.2, 25°C, recombinant mutant K46R

672232

2.3.1.46

0.72

-

pH 7.2, 25°C, recombinant wild-type enzyme

672232

2.3.1.46

0.83

-

recombinant His-tagged mutant I124L, pH and temperature not specified in the publication

735854

2.3.1.46

1.07

-

pH 7.2, 25°C, recombinant mutant C90S

672232

2.3.1.46

1.1

-

pH 7.5, 25°C, recombinant mutant E237A

671625

2.3.1.46

1.1

-

pH 7.5, 25°C, recombinant mutant R193A

671625

2.3.1.46

1.15

-

pH 7.5, 25°C, recombinant mutant R249A

671625

2.3.1.46

1.25

-

recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication

735854

2.3.1.46

1.42

-

recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication

735854

2.3.1.46

1.51

-

pH 7.5, 25°C, recombinant mutant R249K

671625

2.3.1.46

1.6

-

recombinant protein

487046

2.3.1.46

2

-

pH 7.5, 25°C, recombinant mutant Y238F

671625

2.3.1.46

2.26

-

pH 7.5, 25°C, recombinant mutant K46L

671625

2.3.1.46

9.1

-

pH 7.5, 25°C, recombinant mutant E246D

671625

2.3.1.46

59.1

-

pH 7.5, 25°C, recombinant mutant E246A

671625

2.3.1.46

93.8

-

pH 7.5, 25°C, recombinant mutant R193A/E246A

671625

2.3.1.46

95.5

-

pH 7.5, 25°C, recombinant mutant Y238F/E246A

671625

1.1.1.3

19 entries

2.3.1.31

38 entries

2.3.1.46

25 entries

2.5.1.49

10.4

-

-

637834

2.6.1.14

1.4

-

cosubstrate phenylpyruvate

637254

2.6.1.52

14.15

-

pH 8.2, 30°C, recombinant mutant R42W/R77W

758955

2.6.1.52

158.5

-

pH 8.2, 30°C, recombinant wild-type enzyme

758955

2.7.1.39

0.087

-

method: isothermal titration calometry

704525

2.7.1.39

0.11

-

mutant enzyme H202L

641471

2.7.1.39

0.13

-

mutant enzyme R234H

641471

2.7.1.39

0.14

-

wild-type enzyme

641471

2.7.1.39

0.15

-

pH 7.8

641463

2.7.1.39

0.24

-

-

641467

2.7.1.39

0.24

-

pH 7.8, 37°C

641470

2.7.1.39

0.25

-

pH 7.5, 30°C

641468

2.7.1.39

0.3

-

pH 7.8, 27°C

641465

2.7.1.39

0.4

-

-

641460, 641472

2.7.1.39

0.463

-

in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37°C

722043

2.7.1.39

0.52

-

pH 7.5, 30°C

661325

2.7.1.39

0.77

-

pH 7.5, 30°C

641466

2.7.1.39

2.5

-

mutant enzyme H139L

641471

2.7.1.39

3

-

pH 8, 28°C

641464

2.7.1.39

3.7

-

mutant enzyme H205Q

641471

2.7.1.39

6.2

-

mutant enzyme R234H

641471

2.7.1.39

6.7

-

pH 8.5

641461

2.7.1.39

6.9

-

wild-type enzyme

641471

2.7.1.39

8.5

-

mutant enzyme R234C

641471

2.7.1.39

40.1

-

mutant enzyme R234L

641471

2.7.1.39

58.2

-

mutant enzyme H202L

641471

2.6.1.52

2 entries

2.7.1.39

22 entries

4.4.1.1

12.5

-

-

586904

4.4.1.11

30

-

-

701880

4.4.1.11

30

-

37°C, pH 8.0

649323

4.4.1.11

2 entries

5.1.1.10

171

-

pH 8.5, 37°C, recombinant enzyme

746725

K_i Value (12 results)

top print hide

Show KI Value (12 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.13.195

3.1

-

pH 8.0, 25°C, recombinant detagged enzyme

704269

2.5.1.47

1.32

-

pH 6.8, 37 C

637334

2.5.1.49

16

-

-

637825

2.7.1.39

0.1

-

in 20% DMSO

641473

2.7.1.39

2

-

pH 7.5, 30°C

641468

2.7.1.39

2

-

pH 7.6

641463

2.7.1.39

3

-

aqueous sulution, pH 8

641473

2.7.1.39

4 entries

2.7.2.4

7.7

-

pH 8.0, 25°C, aspartokinase III

642329

4.1.99.2

1.33

-

wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using L-Tyr as a substrate

678401

4.1.99.2

1.33

-

wild type enzyme, in 50 mM potassium phosphate pH 8.0, at 25°C, using S-(o-nitrophenyl)-L-Cys as a substrate

678401

4.1.99.2

69

-

mutant enzyme D214N, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

82

-

mutant enzyme D214A, in 50 mM potassium phosphate pH 8.0, at 25°C

678401

4.1.99.2

4 entries

References & Links

Literature References (169)

top print hide

Show Reference (169 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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gamma-Cystathionase (Neurospora)

1971

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Insight into the active site of Streptomyces cystathionine gamma-lyase based on the results of studies on its substrate specificity

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34691

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Sulphur metabolism in Paracoccus denitrificans. Purification, properties and regulation of serine transacetylase, O-acetylserine sulphydrylase and beta-cystathionase

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Burnell, J.N.; Whatley, F.R.

Biochim. Biophys. Acta

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1986

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J. Basic Microbiol.

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246382

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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

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

1993

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246388

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Comparison of homoserine dehydrogenase from different plant sources

1980

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Phytochemistry

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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

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246391

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Threonine-sensitive aspartate kinase and homoserine dehydrogenase from Pisum sativum

1974

Aarnes, H.; Rognes, S.E.

Phytochemistry

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246392

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Properties of homoserine dehydrogenase in a thermophilic bacterium

1973

Cavari, B.Z.; Grossowicz, N.

Biochim. Biophys. Acta

302

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246393

4781056

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

1973

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J. Biochem.

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

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Appl. Microbiol. Biotechnol.

45

612-620

246395

7549965

Purification and characterization of homoserine dehydrogenase from spinach leaves

1995

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Biochem. Mol. Biol. Int.

36

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246396

10700284

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

2000

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Nat. Struct. Biol.

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246398

1907968

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

1991

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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

246555

5849106

Decomposition of methyl methionine sulfonium salts by a bacterial enzyme

1965

Mazelis, M.; Levin, B.; Mallinson, N.

Biochim. Biophys. Acta

105

106-114

246556

110588

Colivirus-T3-coded S-adenosylmethionine hydrolase

1979

Spoerel, N.; Herrlich, P.

Eur. J. Biochem.

95

227-233

246557

763348

A novel bacteriophage defence mechanism: the anti-restriction protein

1979

Spoerel, N.; Herrlich, P.; Bickle, T.A.

Nature

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246558

3301808

Expression of the cloned coliphage T3 S-adenosylmethionine hydrolase gene inhibits DNA methylation and polyamine biosynthesis in Escherichia coli

1987

Hughes, J.A.; Brown, L.R.; Ferro, A.J.

J. Bacteriol.

169

3625-3632

246559

3547328

Nucleotide sequence and analysis of the coliphage T3 S-adenosylmethionine hydrolase gene and its surrounding ribonuclease III processing sites

1987

Hughes, J.A.; Brown, L.R.; Ferro, A.J.

Nucleic Acids Res.

15

717-729

246560

7926842

A novel Tn10 tetracycline regulon system controlling expression of the bacteriophage T3 gene encoding S-adenosyl-L-methionine hydrolase

1994

Collier, G.B.; Mattson, T.L.; Connaughton, J.F.; Chirikjian, J.G.

Gene

148

75-80

246561

7999994

Reduced ethylene synthesis by transgenic tomatoes expressing S-adenosylmethionine hydrolase

1994

Good, X.; Kellogg, J.A.; Wagoner, W.; Langhoff, D.; Matsumura, W.; Bestwick, R.K.

Plant Mol. Biol.

26

781-790

246562

-

Reduced ethylene synthesis and ripening control in tomatoes expressing S-adenosylmethionine hydrolase

1997

Kramer, M.G.; Kellogg, J.; Wagoner, W.; Matsumura, W.; Good, X.; Peters, S.; Clough, G.; Bestwick, R.K.

Biology and Biotechnology of the Plant Hormone Ethylene (A. K. Kanellis et al. (eds. ))

34

307-319

287525

4384871

The mechanism of end product inhibition of serine biosynthesis. I. purification and kinetics of phosphoglycerate dehydrogenase

1968

Sugimoto, E.; Pizer, L.I.

J. Biol. Chem.

243

2081-2089

391438

4565085

Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein

1972

Miller, R.E.; Stadtman, E.R.

J. Biol. Chem.

247

7407-7419

391447

-

Properties of glutamate synthase from Brevibachterium flavum

1984

Sung, H.C.; Tachiki, T.; Kumagai, H.; Tochikura, T.

J. Ferment. Technol.

62

569-575

391448

-

Purification and some properties of glutamate synthase from Gluconobacter subodydans on glutamate as a nitrogen source

1983

Tachiki, T.; Sung, H.C.; Wakisaka, S.; Tochikura, T.

J. Ferment. Technol.

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391686

241744

Glutamate dehydrogenase from Escherichia coli: purification and properties

1975

Sakamoto, N.; Kotre, A.M.; Savageau, M.A.

J. Bacteriol.

124

775-783

486773

11106665

Characterization of transsulfuration and cysteine biosynthetic pathways in the protozoan hemoflagellate, Trypanosoma cruzi. Isolation and molecular characterization of cystathionine b-synthase and serine acetyltransferase from Trypanosoma

2001

Nozaki, T.; Shigeta, Y.; Saito-Nakano, Y.; Imada, M.; Kruger, W.D.

J. Biol. Chem.

276

6516-6523

486779

-

Acetyl-CoA: L-homoserine O-acetyltransferase of the yeast Saccharomyces: substrate kinetics

1988

Yamagata, S.

Kyoyobu Kenkyu Hokoku

24

27-28

486780

-

Homoserine transacetylase (Neurospora)

1971

Nagai, S.; Kerr, D.

Methods Enzymol.

17B

442-445

486781

4721772

Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. VII. Properities of homoserine O-transacetylase

1973

Miyajima, R.; Shiio, I.

J. Biochem.

73

1061-1068

486782

1126938

Purification and properties of homoserine transacetylase from Bacillus polymyxa

1975

Wyman, A.; Paulus, H.

J. Biol. Chem.

250

3897-3903

486783

3552887

The MET2 gene of Saccharomyces cerevisiae: molecular cloning and nucleotide sequence

1986

Langin, T.; Faugeron, G.; Goyon, C.; Nicolas, A.; Rossignol, J.L.

Gene

49

283-293

486784

3301801

Partial purification and some properties of homoserine O-acetyltransferase of a methionine auxotroph of Saccharomyces cerevisiae

1987

Yamagata, S.

J. Bacteriol.

169

3458-3463

486786

6037552

Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine

1967

Nagai, S.; Flavin, M.

J. Biol. Chem.

242

3884-3895

486787

9209059

Homoserine O-acetyltransferase, involved in the Leptospira meyeri methionine biosynthetic pathway, is not feedback inhibited

1997

Bourhy, P.; Martel, A.; Margarita, D.; Saint Girons, I.; Belfaiza, J.

J. Bacteriol.

179

4396-4398

486788

10913262

Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Haemophilus influenzae met2-encoded homoserine transacetylase

2000

Born, T.L.; Franklin, M.; Blanchard, J.S.

Biochemistry

39

8556-8564

486789

9666465

Isolation and analysis of metA, a methionine biosynthetic gene encoding homoserine acetyltransferase in Corynebacterium glutamicum

1998

Park, S.D.; Lee, J.Y.; Kim, Y.; Kim, J.H.; Lee, H.S.

Mol. Cell

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286-294

487043

14217349

O-Succinyl-homoserine as an intermediate in the synthesis of cystathionine by Escherichia coli

1964

Rowbury, R.J.; Woods, D.D.

J. Gen. Microbiol.

36

341-358

487044

3304182

Biological properties and mode of action of clavams

1987

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147

315-320

487045

1729233

Regulation of the Salmonella typhimurium metA gene by the metR protein and homocysteine

1992

Mares, R.; Urbanowski, M.L.; Stauffer, G.V.

J. Bacteriol.

174

390-397

487046

10572016

Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase

1999

Born, T.L.; Blanchard, J.S.

Biochemistry

38

14416-14423

487271

-

Biosynthesis of beta-N-oxalyl-L-alpha,beta-diaminopropionic acid, the Lathyrus sativus neurotoxin

1970

Malathi, K.; Padmanaban, G.; Sarma, P.S.

Phytochemistry

9

1603-1610

586904

6432781

Cystathionine gamma-lyase of Streptomyces phaeochromogenes. The occurrence of cystathionine gamma-lyase in filamentous bacteria and its purification and characterization

1984

Nagasawa, T.; Kanzaki, H.; Yamada, H.

J. Biol. Chem.

259

10393-10403

636989

-

Allylglucosinolate biosynthesis in Brassica carinata

1988

Glover, J.R.; Chapple, C.C.S.; Rothwell, S.; Tober, I.; Ellis, B.E.

Phytochemistry

27

1345-1348

637253

14957

Asparagine transaminase from rat liver

1977

Cooper, A.J.L.

J. Biol. Chem.

252

2032-2038

637254

3099645

Kinetic properties and characteristics of mouse liver mitochondrial asparagine aminotransferase

1986

Maul, D.M.; Schuster, S.M.

Arch. Biochem. Biophys.

251

585-593

637330

-

Some properties of cysteine synthase from radish roots

1976

Tamura, G.; Iwasawa, T.; Masada, M.; Fukushima, K.

Agric. Biol. Chem.

40

637-638

637334

-

Purification and properties of O-acetyl-L-serine sulphhydrolase from wheat leaves

1977

Ascano, A.; Nicholas, D.J.D.

Phytochemistry

16

889-893

637383

12005048

Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8

2002

Mizuno, Y.; Miyashita, Y.; Yamagata, S.; Iwama, T.; Akamatsu, T.

Biosci. Biotechnol. Biochem.

66

549-557

637825

4947307

Homocysteine in yeast. Partial purification and properties of O-acetylhomoserine sulfhydrylase

1971

Yamagata, S.

J. Biochem.

70

1035-1045

637830

15989

O-Alkylhomoserine synthesis catalyzed by O-acetylhomoserine sulfhydrylase in microorganisms

1977

Murooka,Y.; Kakihara, K.; Miwa, T.; Seto, K.; Harada, T.

J. Bacteriol.

130

62-73

637832

7096282

Methionine biosynthesis in Brevibacterium flavum: Properties and essential role of O-acetylhomoserine sulfhydrylase

1982

Ozaki, H.; Shiio, I.

J. Biochem.

91

1163-1171

637834

6526818

O-Acetylhomoserine sulfhydrylase of the fission yeast Schizosaccharomyces pombe: Partial purification, characterization, and its probable role in homocysteine biosynthesis

1984

Yamagata, S.

J. Biochem.

96

1511-1523

637839

11566369

Cloning and overexpression of the oah1 gene encoding O-acetyl-L-homoserine sulfhydrylase of Thermus thermophilus HB8 and characterization of the gene product

2001

Shimizu, H.; Yamagata, S.; Masui, R.; Inoue,Y.; Shibata, T.; Yokoyama, S.; Kuramitsu, S.; Iwama, T.

Biochim. Biophys. Acta

1549

61-72

639898

5059882

Isolation and properties of highly purified glutamine transaminase

1972

Cooper, A.J.L.; Meister, A.

Biochemistry

11

661-671

639901

4822504

Isolation and properties of a new glutamine transaminase form rat kidney

1974

Cooper, A.J.L.; Meister, A.

J. Biol. Chem.

249

2554-2561

640091

9864317

Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata

1999

Ono, H.; Sawada, K.; Khunajakr, N.; Tao, T.; Yamamoto, M.; Hiramoto, M.; Shinmyo, A.; Takano, M.; Murooka, Y.

J. Bacteriol.

181

91-99

641460

-

Homoserine kinase from barley seedlings

1976

Aarnes, H.

Plant Sci. Lett.

7

187-194

641461

-

Biosynthesis of threonine from homoserine in pea seedlings: I. Homoserine kinase

1978

Thoen, A.; Rognes, S.E.; Aarnes, H.

Plant Sci. Lett.

13

103-112

641462

-

Feedback inhibition of homoserine kinase from radish leaves

1983

Baum, H.J.; Madison, J.T.; Thompson, J.F.

Phytochemistry

22

2409-2412

641463

6097184

Homoserine kinase of Escherichia coli: kinetic mechanism and inhibition by L-aspartate semialdehyde

1984

Shames, S.L.; Wedler, F.C.

Arch. Biochem. Biophys.

235

359-370

641464

-

Homoserine kinase from phototrophic bacterium Rhodospirillum rubrum is not sensitive to feedback inhibition by L-Thr

1987

Finkelnburg, B.; Klemme, J.H.

FEMS Microbiol. Lett.

48(1-2)

93-96

641465

4364023

Homoserine kinase from Escherichia coli K-12: properties, inhibition by L-threonine, and regulation of biosynthesis

1974

Theze, J.; Kleidman, L.; Saint Girons, I.

J. Bacteriol.

118

577-581

641466

5016260

Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. V. Properties of homoserine kinase

1972

Miyajima, R.; Shiio, I.

J. Biochem.

71

219-226

641467

-

Purification to homogeneity and characterization of homoserine racemase from wheat germ

1993

Riesmeier, J.; Klonus, A.K.; Pohlenz, H.D.

Phytochemistry

32

581-584

641468

1847111

Inhibition by different amino acids of the aspartate kinase and the homoserine kinase of the yeast Saccharomyces cerevisiae

1991

Ramos, C.; Delgado, M.A.; Calderon, I.L.

FEBS Lett.

278

123-126

641469

2165904

Yeast homoserine kinase. Characteristics of the corresponding gene, THR1, and the purified enzyme, and evolutionary relationships with other enzymes of threonine metabolism

1990

Mannhaupt, G.; Pohlenz, H.D.; Seefluth, A.K.; Pilz, U.; Feldmann, H.

Eur. J. Biochem.

191

115-122

641470

177283

Homoserine kinase from Escherichia coli K12

1976

Burr, B.; Walker, J.; Truffa-Bachi, P.; Cohen, G.N.

Eur. J. Biochem.

62

519-526

641471

8973190

Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli

1996

Huo, X.; Viola, R.E.

Biochemistry

35

16180-16185

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