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Ligand D-serine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for D-serine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)

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Show Natural Substrate (12 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.3

D-Ser + H2O + O2 = 2-oxo-3-hydroxypropionate + NH3 + H2O2

741867, 742077, 743062, 743191, 743827, 711718

-

1.4.3.3

D-serine + H2O + O2 = 2-oxo-3-hydroxypropionate + NH3 + H2O2

711720, 696139, 696158, 699758, 711529, 712324, 698099, 696568, 700312, 700611, 713477, 723920

-

1.4.3.3

D-serine + H2O + O2 = 2-oxo-3-hydroxypropionic acid + NH3 + H2O2

723921, 391854, 391853, 391834, 391833, 391844, 391852, 391841, 391847, 391848, 674360

-

1.4.3.3

D-serine + H2O + O2 = ? + NH3 + H2O2

696568

-

2.1.2.1

(6S)-tetrahydrofolate + D-serine = 5,10-methylenetetrahydrofolate + glycine + H2O

736084

6tgh, 3D-view

2.1.2.1

(6S)-tetrahydrofolate + D-serine = 5,10-methylenetetrahydrofolate + glycine + H2O

736084

6yrw, 3D-view

2.3.1.36

acetyl-CoA + D-serine = CoA + N-acetyl-D-serine

486807

-

2.3.1.36

propionyl-CoA + D-serine = CoA + N-propionyl-D-serine

486807

-

1.4.3.3

4 entries

2.1.2.1

2 entries

2.3.1.36

2 entries

2.6.1.21

D-serine + 2-oxoglutarate = 3-hydroxy-2-oxopropanoate + D-glutamate

759235

-

4.3.1.18

D-serine = ?

210801, 210817

3awo, 3D-view

4.3.1.18

D-serine = pyruvate + NH3

677529, 680567, 651969, 653275, 666133, 677539, 678079, 664227, 666610, 747858

3awo, 3D-view

4.3.1.18

2 entries

6.3.2.35

D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate

726688

-

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

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Show Natural Product (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.2.1

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + D-serine

-

6tgh, 3D-view

2.1.2.1

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + D-serine

-

6yrw, 3D-view

3.1.3.3

3-phospho-D-serine + H2O = D-serine + phosphate

-

-

3.1.3.3

O-phospho-D-serine + H2O = D-serine + phosphate

-

-

2.1.2.1

2 entries

3.1.3.3

2 entries

5.1.1.10

L-serine = D-serine

-

-

5.1.1.18

L-serine = D-serine

-

-

Substrate in Enzyme-catalyzed Reactions (100 results)

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Show Substrate (100 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.276

D-serine + NADP+ = 2-aminomalonate semialdehyde + NADPH

639084, 639082

-

1.1.1.381

D-serine + NADP+ = ?

639084

-

1.4.1.1

D-Ser + H2O + NAD+ = 3-hydroxypyruvate + NH3 + NADH

349581, 349539

-

1.4.1.7

D-serine + H2O + NAD+ = 3-hydroxypyruvate + NH3 + NADH + H+

725474

-

1.4.3.3

D-Ser + H2O + O2 = 2-oxo-3-hydroxypropionate + NH3 + H2O2

673646, 677016, 741867, 742077, 743062, 672703, 674365, 743191, 743827, 711718, 655441, 655274, 743058, 684417, 654786, 741688

-

1.4.3.3

D-Ser + H2O + O2 = 2-oxo-3-hydroxypropionic acid + NH3 + H2O2

724401

-

1.4.3.3

D-serine + H2O + O2 = 2-oxo-3-hydroxypropionate + NH3 + H2O2

700611, 711720, 686069, 696139, 696158, 696568, 699758, 700312, 688278, 699464, 711529, 712324, 698099, 685602, 686020, 713477, 684409, 699164, 723920

-

1.4.3.3

D-serine + H2O + O2 = 2-oxo-3-hydroxypropionic acid + NH3 + H2O2

677529, 674360, 686567, 723921, 679652, 687746, 689217, 690048, 725676, 679665, 686570, 724965, 391854, 391853, 391834, 391833, 391844, 391852, 687891, 391841, 391847, 391848, 686020, 684835, 688608, 685750, 724793

-

1.4.3.3

D-serine + H2O + O2 = 3-hydroxypyruvate + NH3 + H2O2

677529, 391854, 391848

-

1.4.3.3

D-serine + H2O + O2 = ?

699464

-

1.4.3.3

D-serine + H2O + O2 = ? + NH3 + H2O2

696568

-

1.4.5.1

D-Ser + oxidized coenzyme Q1 + H2O = 3-hydroxy-2-oxopropanoate + NH3 + reduced coenzyme Q1

695533

-

1.4.5.1

D-serine + oxidized 2,6-dichloroindophenol + H2O = 3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol

394971

-

1.4.5.1

D-serine + oxidized 2,6-dichlorophenolindophenol + H2O = 3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol

394968

-

1.4.5.1

D-serine + oxidized acceptor + H2O = 3-hydroxy-2-oxopropanoate + NH3 + reduced acceptor

700217

-

1.4.99.6

D-Ser + H2O + oxidized 2,6-dichlorophenolindophenol = 3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol

695533

-

1.4.99.6

D-serine + H2O + 2,6-dichlorophenolindophenol = 3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichlorophenolindophenol

705545, 394974

-

1.4.99.6

D-serine + H2O + FAD = 3-hydroxy-2-oxopropanoate + NH3 + FADH2

748083

-

1.4.99.6

D-serine + H2O + methylene blue = 3-hydroxy-2-oxopropanoate + NH3 + reduced methylene blue

394974

-

1.4.3.3

7 entries

1.4.5.1

4 entries

1.4.99.6

4 entries

1.5.99.13

D-serine + oxidized 2,6-dichloroindophenol + H2O = 3-hydroxy-2-oxopropanoate + NH3 + reduced 2,6-dichloroindophenol

394966

-

2.1.2.1

(6S)-tetrahydrofolate + D-serine = 5,10-methylenetetrahydrofolate + glycine + H2O

736084

6tgh, 3D-view

2.1.2.1

(6S)-tetrahydrofolate + D-serine = 5,10-methylenetetrahydrofolate + glycine + H2O

736084

6yrw, 3D-view

2.1.2.1

D-serine + (benzyloxy)acetaldehyde + H2O = (3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + (benzyloxy)acetaldehyde + H2O = (3R)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline + (3S)-4-(benzyloxy)-2',3-dihydroxy-L-isovaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + 2-fluorobenzaldehyde + H2O = (2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + 2-fluorobenzaldehyde + H2O = (2S,3S)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(2-fluorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + 3-phenylpropanal + H2O = (3S)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + 3-phenylpropanal + H2O = (3S)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline + (3R)-3-hydroxy-2-(hydroxymethyl)-5-phenyl-L-norvaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + 4-(benzyloxy)butanal + H2O = (3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + 4-(benzyloxy)butanal + H2O = (3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3S)-2',3-dihydroxy-4-(3-phenylpropoxy)-L-isovaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + 4-chlorobenzaldehyde + H2O = (2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + 4-chlorobenzaldehyde + H2O = (2S,3S)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-2-amino-3-(4-chlorophenyl)-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + 4-formylphenyl acetate + H2O = (2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + 4-formylphenyl acetate + H2O = (2S,3S)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid + (2S,3R)-3-[4-(acetyloxy)phenyl]-2-amino-3-hydroxy-2-(hydroxymethyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + 4-hydroxybenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + 4-hydroxybenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-hydroxyphenyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + 4-nitrobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + 4-nitrobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(4-nitrophenyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + benzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + benzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-phenylpropanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + benzyl (2-oxoethyl)carbamate + H2O = (3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + benzyl (2-oxoethyl)carbamate + H2O = (3S)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline + (3R)-4-[[(benzyloxy)carbonyl]amino]-2',3-dihydroxy-L-isovaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + benzyl (3-oxopropyl)carbamate + H2O = (3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine

755784

6tgh, 3D-view

2.1.2.1

D-serine + benzyl (3-oxopropyl)carbamate + H2O = (3S)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine + (3R)-N6-[(benzyloxy)carbonyl]-3-hydroxy-2-(hydroxymethyl)-L-lysine

755784

6yrw, 3D-view

2.1.2.1

D-serine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O = (3S,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + benzyl [(2R)-1-oxopropan-2-yl]carbamate + H2O = (3S,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4R)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O = (3S,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + benzyl [(2S)-1-oxopropan-2-yl]carbamate + H2O = (3S,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline + (3R,4S)-4-[[(benzyloxy)carbonyl]amino]-3-hydroxy-2-(hydroxymethyl)-L-norvaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + pentafluorobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid

755784

6tgh, 3D-view

2.1.2.1

D-serine + pentafluorobenzaldehyde + H2O = (2S,3S)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid + (2S,3R)-2-amino-3-hydroxy-2-(hydroxymethyl)-3-(pentafluorophenyl)propanoic acid

755784

6yrw, 3D-view

2.1.2.1

D-serine + phenoxyacetaldehyde + H2O = (3R)-2',3-dihydroxy-4-phenoxy-L-isovaline + (3S)-2',3-dihydroxy-4-phenoxy-L-isovaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + phenoxyacetaldehyde + H2O = (3R)-2',3-dihydroxy-4-phenoxy-L-isovaline + (3S)-2',3-dihydroxy-4-phenoxy-L-isovaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + phenylacetaldehyde + H2O = (3S)-2',3-dihydroxy-4-phenyl-L-isovaline + (3R)-2',3-dihydroxy-4-phenyl-L-isovaline

755784

6tgh, 3D-view

2.1.2.1

D-serine + phenylacetaldehyde + H2O = (3S)-2',3-dihydroxy-4-phenyl-L-isovaline + (3R)-2',3-dihydroxy-4-phenyl-L-isovaline

755784

6yrw, 3D-view

2.1.2.1

D-serine + tetrahydrofolate = glycine + 5,10-methylenetetrahydrofolate + H2O

703653, 705602

6tgh, 3D-view

2.1.2.1

D-serine + tetrahydrofolate = glycine + 5,10-methylenetetrahydrofolate + H2O

703653, 705602

6yrw, 3D-view

2.3.1.36

acetyl-CoA + D-serine = CoA + N-acetyl-D-serine

657695, 486807

-

2.3.1.36

propionyl-CoA + D-serine = CoA + N-propionyl-D-serine

486807

-

2.1.2.1

36 entries

2.3.1.36

2 entries

2.3.1.50

palmitoyl-CoA + [2,3,3-D] L-serine = ?

757380

-

2.6.1.21

D-serine + 2-oxoglutarate = 3-hydroxy-2-oxopropanoate + D-glutamate

759235, 636736, 636746

-

2.6.1.21

D-serine + pyruvate = 3-hydroxy-2-oxopropanoate + D-alanine

636746, 759259

-

2.6.1.21

2 entries

2.6.1.74

D-serine + 2-oxoadipate = 3-hydroxy-2-oxopropanoate + 2-aminoadipate

640195

-

3.1.4.4

docosahexanoylphosphatidylcholine + D-serine = docosahexanoylphosphatidylserine + choline

751157

-

3.1.4.4

phosphatidylcholine + D-serine = phosphatidylserine + choline

751157, 694606

-

3.5.99.7

D-Ser + H2O = ?

648260

-

3.5.99.7

D-serine + H2O = ?

735145

-

4.1.2.42

D-serine + 3-nitrobenzaldehyde = beta-(3-nitrophenyl)-alpha-hydroxymethyl-serine

746900

-

4.1.2.42

D-serine + benzaldehyde = 2-amino-3-hydroxy-2-hydroxymethyl-3-phenylpropanoic acid

746900

-

4.1.2.5

D-serine + 3-nitrobenzaldehyde = beta-(3-nitrophenyl)-alpha-hydroxymethyl-serine

746900

-

4.1.2.5

D-serine + benzaldehyde = 2-amino-3-hydroxy-2-hydroxymethyl-3-phenylpropanoic acid

746900

-

4.1.99.1

D-serine + indole = L-tryptophan + H2O

704093, 715733

-

4.1.99.1

D-serine = pyruvate + NH3

715733

-

3.1.4.4

2 entries

3.5.99.7

2 entries

4.1.2.42

2 entries

4.1.2.5

2 entries

4.1.99.1

2 entries

4.1.99.2

D-serine + H2O = ?

651817

-

4.3.1.10

D-serine = ?

6035

-

4.3.1.15

D-serine + H2O = pyruvate + NH3

649621

4d9n, 3D-view

4.3.1.15

D-serine = pyruvate + NH3

6046, 729923

4d9n, 3D-view

4.3.1.17

D-serine = L-serine

662359, 661171, 661725

-

4.3.1.17

D-serine = pyruvate + NH3

680142, 661725, 662359, 661171

-

4.3.1.18

D-Ser = pyruvate + NH3

714985

3awo, 3D-view

4.3.1.18

D-serine = ?

210801, 210817

3awo, 3D-view

4.3.1.18

D-serine = pyruvate + NH3

210780, 677529, 680567, 210802, 210803, 210804, 210805, 210806, 210808, 210810, 210811, 210812, 210813, 210814, 210815, 210816, 210817, 651969, 653275, 666133, 680142, 677539, 678079, 210807, 210801, 664227, 666610, 729282, 729705, 729953, 730889, 748453, 729822, 745545, 747007, 747622, 747858, 715627

3awo, 3D-view

4.3.1.15

2 entries

4.3.1.17

2 entries

4.3.1.18

3 entries

4.3.1.27

D-serine = ?

712323

-

4.3.1.9

D-serine = pyruvate + NH3

644481

-

5.1.1.1

D-serine = L-serine

661002

-

5.1.1.10

D-Ser = L-Ser

2045, 2052

-

5.1.1.10

D-serine = L-serine

661171, 661725, 744003, 745414, 662359, 715591

-

5.1.1.10

D-serine = pyruvate + NH3

662359

-

5.1.1.18

D-serine = L-serine

727482, 663264, 660824, 661171, 661725, 662359, 714697, 680516

-

5.1.1.18

D-serine = pyruvate + H2O

662359

-

5.1.1.18

D-serine = pyruvate + NH3

661171, 661725

-

5.1.1.18

D-serine = S-serine

714348

-

5.1.1.10

3 entries

5.1.1.18

4 entries

6.1.1.11

ATP + D-Ser + tRNASer = ?

81, 87

-

6.2.1.54

ATP + D-Ser + diphosphate = ?

693175

-

6.3.2.3

ATP + gamma-L-Glu-L-Cys + D-Ser = ADP + phosphate + gamma-Glu-L-Cys-D-Ser

661012

-

6.3.2.35

D-alanine + D-serine + ATP = D-alanyl-D-serine + ADP + phosphate

706960, 726688, 710442

-

6.3.2.4

ATP + D-Ser = ADP + phosphate + D-Ser-D-Ser

672685

-

6.3.2.4

ATP + D-alanine + D-serine = ADP + D-alanyl-D-serine + D-alanyl-D-alanine + D-seryl-D-serine

662483

-

6.3.2.4

ATP + D-serine = ADP + phosphate + D-alanyl-D-serine

650819

-

6.3.2.4

D-serine + ATP = ADP + D-serinyl-D-serine

662483

-

6.3.2.4

D-serine + D-serine + ATP = D-seryl-D-serine + ADP + phosphate

672685

-

6.3.2.4

5 entries

Product in Enzyme-catalyzed Reactions (23 results)

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Show Product (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.1.2.1

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + D-serine

-

6tgh, 3D-view

2.1.2.1

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + D-serine

-

6yrw, 3D-view

2.1.2.1

2 entries

2.1.2.7

tetrahydrofolate + 2-hydroxymethylserine = 5,10-methylenetetrahydrofolate + D-serine + H2O

485777, 485776,

-

3.1.1.43

D-serine methyl ester + H2O = D-serine + methanol

80934

-

3.1.3.2

O-phospho-DL-serine + H2O = D-serine + phosphate

-

-

3.1.3.3

D-phosphoserine + H2O = D-Ser + phosphate

81048, 81050, 81054, 81041, 81046, 81055, 81056

-

3.1.3.3

3-phospho-D-serine + H2O = D-serine + phosphate

-

-

3.1.3.3

O-phospho-D-serine + H2O = D-serine + phosphate

-

-

3.1.3.3

3 entries

3.1.4.13

D-serine-phosphoethanolamine + H2O = D-serine + ethanolamine phosphate

81109

-

3.4.11.19

D-serine amide + H2O = D-serine + NH3

-

-

3.4.11.19

L-serine amide + H2O = D-serine + NH3

-

-

3.4.11.19

2 entries

3.4.13.17

Gly-D-Ser + H2O = Gly + D-Ser

81206

-

3.4.13.19

L-Leu-D-Ser + H2O = L-Leu + D-Ser

-

-

3.4.13.22

D-Ala-D-Ser + H2O = D-Ala + D-Ser

-

-

3.4.13.22

D-Ser-D-Ala + H2O = D-Ser + D-Ala

36315

-

3.4.13.22

2 entries

3.5.1.77

N-carbamoyl-D-Ser + H2O = D-Ser + NH3 + CO2

-

-

4.3.1.17

L-serine = D-serine

-

-

5.1.1.1

L-Ser = D-Ser

649578, 651680, 651822, 652947,

-

5.1.1.1

L-serine = D-serine

-

-

5.1.1.10

L-Ser = D-Ser

, 2041

-

5.1.1.10

L-serine = D-serine

-

-

5.1.1.1

2 entries

5.1.1.10

2 entries

5.1.1.12

L-serine = D-serine

-

-

5.1.1.18

L-serine = D-serine

-

-

Activator in Enzyme-catalyzed Reactions (3 results)

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Show Activating Compound (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.13.9

activation of isoforms prolidase I and prolidase II

668271

-

5.1.1.18

up to 5fold increase in activity

662958

-

7.4.2.11

118% activity at 50 mM with D-methionine as substrate

749753

-

Inhibitor in Enzyme-catalyzed Reactions (22 results)

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Show Inhibitors (22 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.3

-

723920

-

2.3.2.2

-

487962

-

2.3.3.1

-

702966

-

2.6.1.21

inhibition of D- and L-transamination of D-alanine to 2-oxoglutarate

636737

-

2.6.1.45

competitive inhibition

636694

-

2.6.1.45

competitive inhibition with L-serine

702425

-

2.6.1.45

2 entries

2.7.1.40

-

641562

-

2.7.1.80

20 mM, weak inhibition

642033

-

3.1.3.2

-

663788

-

3.1.3.3

-

81047, 81048

-

3.5.99.7

-

648252, 648260

-

3.5.99.7

slow inactivation

648246

-

3.5.99.7

2 entries

3.7.1.3

competitive inhibition, 10 mM

289258

-

4.1.1.11

-

3947, 3948

7a8y, 3D-view

4.3.1.16

5 mM decrease the enzyme activity to 27%

692924

-

4.3.1.17

-

210775, 210781, 210792

-

4.3.1.17

competitive

210777, 210791

-

4.3.1.17

100 mM, 40% inhibition

651494

-

4.3.1.17

competitive

665546, 713970

-

4.3.1.17

4 entries

6.1.1.13

-

1056

-

6.3.2.16

-

1056

-

7.4.2.11

86% residual activity at 5 mM with L-methionine as substrate

749753

-

3D Structure of Enzyme-Ligand-Complex (PDB) (31 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (31 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.15.1.1

2wz0, 3D-view

2.1.2.1

6tgh, 3D-view

2.1.2.1

6yrw, 3D-view

2.1.2.1

6tgh, 3D-view

2.1.2.1

6yrw, 3D-view

2.1.2.1

6tgh, 3D-view

2.1.2.1

6yrw, 3D-view

2.1.2.1

6 entries

2.7.11.13

2uzp, 3D-view

2.7.7.6

4mq9, 3D-view

2.7.7.6

4oin, 3D-view

2.7.7.6

4oip, 3D-view

2.7.7.6

4oiq, 3D-view

2.7.7.6

4oir, 3D-view

2.7.7.6

4mq9, 3D-view

2.7.7.6

4oin, 3D-view

2.7.7.6

4oip, 3D-view

2.7.7.6

4oiq, 3D-view

2.7.7.6

4oir, 3D-view

2.7.7.6

4mq9, 3D-view

2.7.7.6

4oin, 3D-view

2.7.7.6

4oip, 3D-view

2.7.7.6

4oiq, 3D-view

2.7.7.6

4oir, 3D-view

2.7.7.6

15 entries

3.4.21.73

4jk5, 3D-view

3.5.1.98

6wi3, 3D-view

3.5.2.6

6qw7, 3D-view

4.1.1.11

7a8y, 3D-view

4.3.1.15

4d9n, 3D-view

4.3.1.18

3awo, 3D-view

4.4.1.15

4d97, 3D-view

5.2.1.8

1cyn, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (84 results)

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Show Turnover Number (84 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.381

3.5

-

pH 9.0, 30°C

639084

1.1.1.381

7.84

-

pH 9.0, 30°C

639084

1.4.3.3

1.51

-

pH 8.3, 37°C, recombinant DAO

711718

1.4.3.3

1.8

-

mutant T317A

391854

1.4.3.3

2.2

-

mutant enzyme E220D/Y224G

674365

1.4.3.3

2.5

-

pH 8.5, 25°C, recombinant EGFP-DAAO

713477

1.4.3.3

2.7

-

wild-type

391854

1.4.3.3

2.83

-

pH 8.3, 25°C

677016

1.4.3.3

3

-

pH 8.5, 25°C

673646

1.4.3.3

3

-

wild-type enzyme

674365

1.4.3.3

3

-

at pH 7.0 and 25°C

723920

1.4.3.3

3

-

pH 8.5, 25°C, recombinant wild-type DAAO

713477

1.4.3.3

4

-

in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C

684835

1.4.3.3

6.4

-

in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C

724965

1.4.3.3

20.5

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

34.5

-

pH 8.0, 37°C

655274

1.1.1.381

2 entries

1.4.3.3

14 entries

1.4.5.1

5.33

-

-

394971

1.4.99.6

0.8

-

pH 8.7, 37°C

748083

2.1.2.1

0.246

-

apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C

705602

2.1.2.1

0.26

-

in 50 mM HEPES buffer (pH 7.0), at 25°C

703653

4.3.1.15

5.17

-

pH 7.4, 30°C, sDAPL

729923

4.3.1.15

10.5

-

pH 7.4, 30°C, mutant T385S sDAPL

729923

4.3.1.15

34.17

-

pH 7.4, 30°C, mutant T385D sDAPL

729923

4.3.1.17

0.0033

-

wild-type, pH 7.4, 37°C

662359

4.3.1.17

0.012

-

mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

662359

4.3.1.17

0.042

-

wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

662359

4.3.1.17

3.2

-

pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

661171

4.3.1.17

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

4.3.1.18

0.08

-

pH not specified in the publication, 30°C, mutant H398A

729705

4.3.1.18

0.083

-

pH 8, 30°C, mutant Y203E

729953

4.3.1.18

0.097

-

pH 8, 30°C, mutant Y203D

729953

4.3.1.18

0.098

-

pH not specified in the publication, 30°C, mutant K57A

729705

4.3.1.18

0.5

-

pH 8, 30°C, mutant Y203R

729953

4.3.1.18

0.811

-

-

680567

4.3.1.18

1.67

-

EDTA-treated

678079

4.3.1.18

2.3

-

pH 8, 30°C, mutant Y203A

729953

4.3.1.18

2.3

-

pH 8, 30°C, mutant Y203S

729953

4.3.1.18

2.6

-

pH 8.5, 30°C

747858

4.3.1.18

4.3

-

pH 8, 30°C, mutant Y203F

729953

4.3.1.18

6.08

-

-

680567

4.3.1.18

9.4

-

pH 5.7, 25°C

210802

4.3.1.18

12.5

-

EDTA-treated + 2.5 microM ZnCl2

678079

4.3.1.18

13.1

-

pH and temperature not specified in the publication

730889

4.3.1.18

13.1

-

untreated

678079

4.3.1.18

15.7

-

-

666133

4.3.1.18

17

-

pH 8, 30°C, wild-type

729953

4.3.1.18

17

-

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

729705

4.3.1.18

30

-

pH 7.8, 5°C

210802

4.3.1.18

48

-

pH 8.9, 25°C

210802

4.3.1.18

118

-

pH 7.8, 25°C

210802

2.1.2.1

2 entries

4.3.1.15

3 entries

4.3.1.17

5 entries

4.3.1.18

22 entries

4.3.1.27

8.68

-

at pH 8.5 and 50°C

712323

5.1.1.1

5.5

-

pH 8.2, 37°C

661002

5.1.1.10

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

5.1.1.18

0.00211

-

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

746724

5.1.1.18

0.00366

-

pH 8.0, 30°C, recombinant mutant P151S/F152S

746724

5.1.1.18

0.00392

-

pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S

746724

5.1.1.18

0.004

-

wild-type, pH 7.4, 37°C

662359

5.1.1.18

0.00423

-

pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S

746724

5.1.1.18

0.00772

-

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

746724

5.1.1.18

0.015

-

mutant Q155D, racemization, pH 7.4, 37°C

662359

5.1.1.18

0.028

-

wild-type, racemization, presence of ATP, pH 7.4, 37°C

662359

5.1.1.18

0.0551

-

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

746724

5.1.1.18

0.057

-

pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S

746724

5.1.1.18

0.11

-

mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C

662359

5.1.1.18

0.12

-

mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

0.14

-

mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

0.2

-

wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

0.285

-

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

746724

5.1.1.18

0.31

-

wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

0.376

-

pH 8.0, 30°C, recombinant mutant H150S/P151S

746724

5.1.1.18

0.516

-

pH 8.0, 30°C, recombinant mutant H150S

746724

5.1.1.18

0.523

-

pH 8.0, 30°C, recombinant mutant P151S/N152S

746724

5.1.1.18

0.611

-

pH 8.0, 30°C, recombinant mutant H150S/N152S

746724

5.1.1.18

0.816

-

pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S

746724

5.1.1.18

1.41

-

pH 8.0

694974

5.1.1.18

1.88

-

pH 8.0

694974

5.1.1.18

2.16

-

pH 8.0, 30°C, recombinant mutant N152S

746724

5.1.1.18

2.22

-

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

748612

5.1.1.18

3.2

-

pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

661171

5.1.1.18

5.22

-

pH 8.2, 95°C

680516

5.1.1.18

5.68

-

pH 8.0, 30°C, recombinant mutant P151S

746724

5.1.1.18

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

5.1.1.18

29 entries

6.3.2.35

8.17

-

pH 7.5

710442

6.3.2.4

2.6

-

-

650819

K_M Value (118 results)

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Show KM Value (118 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.276

44

-

pH 9.0, 30 °C

639082

1.1.1.381

69

-

pH 9.0, 30°C

639084

1.1.1.381

71

-

pH 9.0, 30°C

639084

1.4.3.3

0.909

-

pH 8.0, 37°C

655274

1.4.3.3

1.7

-

pH 8.5, 25°C, mutant enzyme Y238F

655441

1.4.3.3

2.9

-

pH 8.5, 25°C, mutant enzyme Y238S

655441

1.4.3.3

3.3

-

wild-type enzyme

674365

1.4.3.3

3.6

-

pH 8.3, 25°C

677016

1.4.3.3

3.62

-

apparent value, immobilized enzyme

684417

1.4.3.3

3.9

-

in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C

684835

1.4.3.3

4

-

pH 8.5, 25°C, recombinant EGFP-DAAO

713477

1.4.3.3

4.7

-

pH 8.3, 37°C, mutant enzyme F42C

672703

1.4.3.3

4.8

-

wild-type

391854

1.4.3.3

7

-

pH 8.5, 25°C, recombinant wild-type DAAO

713477

1.4.3.3

7.5

-

pH 8.5, 25°C

673646

1.4.3.3

7.5

-

at pH 7.0 and 25°C

723920

1.4.3.3

12.7

-

pH 8.3, 37°C, wild-type enzyme

672703

1.4.3.3

13.7

-

pH 8.5, 25°C, wild-type enzyme

655441

1.4.3.3

13.75

-

apparent value, free enzyme

684417

1.4.3.3

13.75

-

-

391833

1.4.3.3

17.3

-

-

391848

1.4.3.3

20

-

pH 8.3, 37°C, recombinant DAO

711718

1.4.3.3

20.8

-

mutant T317A

391854

1.4.3.3

25

-

-

391847

1.4.3.3

33.7

-

-

391853

1.4.3.3

36.6

-

wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

310

-

in 75 mM sodium diphosphate buffer (pH 8.3) at 25°C

724965

1.1.1.381

2 entries

1.4.3.3

24 entries

1.4.5.1

19

-

with 2,6-dichlorophenolindophenol

394971

1.4.99.6

1.65

-

pH 8.7, 37°C

748083

2.1.2.1

0.071

-

apparent value, in 50 mM HEPES, pH 8.0 containing 0.5 mM EDTA, 1 mM dithiothreitol, at 25°C

705602

2.1.2.1

47

-

apparent value, in 50 mM HEPES buffer (pH 7.0), at 25°C

703653

2.1.2.1

55

-

pH 7.0, 25°C, recombinant enzyme

736084

2.1.2.1

3 entries

2.3.1.36

0.034

-

30°C, recombinant enzyme

657695

2.3.1.50

4.09

-

at pH 8.1 and 37°C

757380

4.3.1.10

8.3

-

enzyme B

6035

4.3.1.15

0.285

-

pH 7.5, 37°C

649621

4.3.1.15

0.33

-

pH 7.4, 30°C, sDAPL

729923

4.3.1.15

0.375

-

pH 7.4, 30°C, mutant T385S sDAPL

729923

4.3.1.15

0.43

-

-

6046

4.3.1.15

0.6

-

pH 7.4, 30°C, mutant T385D sDAPL

729923

4.3.1.15

0.72

-

pH 7.5, 37°C

649621

4.3.1.17

3.2

-

pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

661171

4.3.1.17

8.5

-

wild-type, alpha,beta-elimination, pH 7.4, 37°C

662359

4.3.1.17

9

-

wild-type, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

662359

4.3.1.17

12

-

mutant Q155D, alpha,beta-elimination, presence of ATP, pH 7.4, 37°C

662359

4.3.1.17

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

4.3.1.17

49

-

pH 8.0, 37°C, racemization reaction

661725

4.3.1.17

75

-

pH 8.0, 37°C, elimination reaction

661725

4.3.1.18

0.086

-

pH 5.7, 25°C

210802

4.3.1.18

0.1

-

-

666133

4.3.1.18

0.131

-

-

680567

4.3.1.18

0.19

-

EDTA-treated

678079

4.3.1.18

0.19

-

pH 8.5, 30°C

747858

4.3.1.18

0.19

-

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

729705

4.3.1.18

0.2

-

pH 8, 30°C, wild-type

729953

4.3.1.18

0.24

-

pH 7.8, 5°C

210802

4.3.1.18

0.33

-

pH and temperature not specified in the publication

747622

4.3.1.18

0.35

-

pH 7.8, 25°C

210802

4.3.1.18

0.35

-

25°C, pH 7.8

651969

4.3.1.18

0.39

-

pH and temperature not specified in the publication

730889

4.3.1.18

0.39

-

untreated

678079

4.3.1.18

0.42

-

pH 7.5, 37°C, buffer K+-phosphate

714985

4.3.1.18

0.48

-

EDTA-treated + 2.5 microM ZnCl2

678079

4.3.1.18

0.7

-

-

210810

4.3.1.18

0.7

-

pH 8, 30°C, mutant Y203F

729953

4.3.1.18

0.87

-

pH 7.5, 37°C, buffer Na+-phosphate

714985

4.3.1.18

1.3

-

-

210811

4.3.1.18

1.68

-

pH 8.9, 25°C

210802

4.3.1.18

1.8

-

pH 8, 30°C, mutant Y203A

729953

4.3.1.18

2.8

-

-

210807

4.3.1.18

3.3

-

pH 8, 30°C, mutant Y203S

729953

4.3.1.18

5.1

-

pH 8, 30°C, mutant Y203R

729953

4.3.1.18

5.6

-

pH 8, 30°C, mutant Y203E

729953

4.3.1.18

8.5

-

pH 8, 30°C, mutant Y203D

729953

4.3.1.15

6 entries

4.3.1.17

7 entries

4.3.1.18

26 entries

4.3.1.27

0.15

-

at pH 8.5 and 50°C

712323

5.1.1.1

10

-

pH 8.2, 37°C

661002

5.1.1.10

1

-

-

2045

5.1.1.10

1

-

L-Arg

2052

5.1.1.10

1

-

L-Lys

2052

5.1.1.10

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

5.1.1.10

18

-

-

2049

5.1.1.10

49

-

pH 8.0, 37°C, racemization reaction

661725

5.1.1.18

2

3

wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

3.2

-

pH 8.0

694974

5.1.1.18

3.2

-

pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

661171

5.1.1.18

8

-

wild-type, racemization, pH 7.4, 37°C

662359

5.1.1.18

8.2

-

wild-type, racemization, presence of ATP, pH 7.4, 37°C

662359

5.1.1.18

8.48

-

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

746724

5.1.1.18

8.9

-

wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

9.2

-

mutant Q155D, racemization, pH 7.4, 37°C

662359

5.1.1.18

9.2

-

mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C

662359

5.1.1.18

10.8

-

pH 8.0

694974

5.1.1.18

12.7

-

pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S

746724

5.1.1.18

14.5

-

pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction

661171

5.1.1.18

20.9

-

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

746724

5.1.1.18

21.4

-

pH 8.0, 30°C, recombinant mutant P151S/F152S

746724

5.1.1.18

28.9

-

pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S

746724

5.1.1.18

28.9

-

pH 8.0, 30°C, recombinant mutant P151S

746724

5.1.1.18

29.3

-

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

746724

5.1.1.18

36.8

-

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

748612

5.1.1.18

37.4

-

pH 8.0, 30°C, recombinant mutant H150S

746724

5.1.1.18

40

-

mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

44.1

-

pH 8.0, 30°C, recombinant mutant H150S/P151S

746724

5.1.1.18

45.1

-

pH 8.0, 30°C, recombinant mutant N152S

746724

5.1.1.18

48

-

mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

714697

5.1.1.18

49

-

pH 8.0, 37°C, racemization reaction

661725

5.1.1.18

55.2

-

pH 8.0, 30°C, recombinant mutant H150S/N152S

746724

5.1.1.18

60

-

pH 8.0, 37°C

663264

5.1.1.18

69.7

-

pH 8.0, 30°C, recombinant mutant P151S/N152S

746724

5.1.1.18

75

-

pH 8.0, 37°C, elimination reaction

661725

5.1.1.18

95.4

-

pH 8.2, 95°C

680516

5.1.1.18

119

-

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

746724

5.1.1.18

172

-

pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S

746724

5.1.1.18

252

-

pH 8.0, 30°C, recombinant mutant H150S/P151S/F152S

746724

6.1.1.11

0.2

-

2'-dATP

87

6.1.1.11

0.2

-

serine-dependent ATP-diphosphate exchange

81

5.1.1.10

6 entries

5.1.1.18

32 entries

6.1.1.11

2 entries

6.3.2.35

1.8

-

pH 7.5

710442

6.3.2.4

56

-

-

650819

K_i Value (6 results)

top print hide

Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.2

0.61

-

in presence of borate

487962

2.6.1.45

1.4

-

-

702425

2.6.1.45

1.6

-

-

636694

2.6.1.45

2 entries

4.3.1.16

22.8

-

non-competitive inhibition

692924

4.3.1.17

1.41

-

pH 8.0, 37°C

665546

4.3.1.17

10

-

pH 7.0, temperature not specified in the publication

713970

4.3.1.17

2 entries

References & Links

Literature References (213)

top print hide

Show Reference (213 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

81

4906848

Purification and properties of seryl transfer ribonucleic acid synthetase from Escherichia coli

1970

Katze, J.R.; Konigsberg, W.

J. Biol. Chem.

245

923-930

87

776617

Phenylalanyl-tRNA and seryl-tRNA synthetases from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reaction

1976

Freist, W.; von der Haar, F.; Sprinzl, M.; Cramer, F.

Eur. J. Biochem.

64

389-393

1056

4399593

D-Alanine:membrane acceptor ligase from Lactobacillus casei

1971

Reusch, V.M.; Neuhaus, F.C.

J. Biol. Chem.

246

6136-6143

2041

-

Amino acid racemase (Pseudomonas striata)

1971

Soda, K.; Osumi, T.

Methods Enzymol.

17

629-636

2045

-

Purification and characterization of amino acid racemase with very broad substrate specificity from Aeromonas caviae

1987

Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.

Agric. Biol. Chem.

51

173-180

2049

-

Amino acid racemase with broad substrate specificity, its properties and use in phenylalanine racemization

1988

Asano, Y.; Endo, K.

Appl. Microbiol. Biotechnol.

29

523-527

2052

6427786

Purification and properties of amino acid racemase from Aeromonas punctata subsp. caviae

1984

Inagaki, K.; Tanizawa, K.; Tanaka, H.; Soda, K.

Prog. Clin. Biol. Res.

144A

355-363

3947

3003510

L-Aspartate alpha-decarboxylase

1985

Williamson, J.M.

Methods Enzymol.

113

589-595

3948

381298

Purification and properties of L-aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli

1979

Williamson, J.M.; Brown, G.M.

J. Biol. Chem.

254

8074-8082

6035

1260040

Substrate specificity of the L-serine O-sulphate degrading activities of Pseudomonas FR

1976

Tudball, N.; O'Neill, J.G.

Biochim. Biophys. Acta

429

616-623

6046

3275662

Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide

1988

Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H.

J. Biol. Chem.

263

958-964

36315

7873524

Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147

1995

Wu, Z.; Wright, G.D.; Walsh, C.T.

Biochemistry

34

2455-2463

80934

-

Substrate specificity of alpha-amino acid hydrolase from Xanthomonas citri

1980

Kato, K.; Kawahara, K.; Takahashi, T.; Kakinuma, A.

Agric. Biol. Chem.

44

1075-1081

81041

-

Interactions of aminophosphonates with rat liver phosphoserine phosphatase

1985

Vidal, Y.; Cassaigne, A.; Neuzil, E.

Biochem. Soc. Trans.

13

788-789

81046

4307821

Phosphoserine phosphatase distribution in normal and neoplastic rat tissues

1969

Knox, W.E.; Herzfeld, A.; Hudson, J.

Arch. Biochem. Biophys.

132

397-403

81047

4290222

Mouse brain phosphoserine phosphohydrolase and phosphotransferase

1967

Bridgers, W.F.

J. Biol. Chem.

242

2080-2085

81048

-

Glucose 6-phosphatase and phosphoserine phosphatase

1961

Byrne, W.L.

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

5

73-78

81050

13610904

Metabolism of phosphoserine. II. Purification and properties of O-phosphoserine phosphatase

1959

Neuhaus, F.C.; Byrne, W.L.

J. Biol. Chem.

234

113-121

81054

-

Phosphoserine phosphatase of human brain: partial purification, characterization, regional distribution, and effect of certain modulators including psychoactive drugs

1991

Shetty, V.; Shetty, K.T.

Neurochem. Res.

16

1203-1210

81055

8858931

Formation of D-serine from L-phosphoserine in brain synaptosomes

1996

Wood, P.L.; Hawkinson, J.E.; Goodenough, D.B.

J. Neurochem.

67

1485-1490

81056

9430431

Novel phosphoserine phosphatase inhibitors

1997

Hawkinson, J.E.; Acosta-Burruel, M.; Ta, N.D.; Wood, P.L.

Eur. J. Pharmacol.

337

315-324

81109

14284710

The isolation and properties of chicken kidney serine ethanolamine phosphate phosphodiesterase

1965

Hagerman, D.D.; Rosenberg, H.; Ennor, A.H.; Schiff, P.; Inoue, S.

J. Biol. Chem.

240

1108-1112

81206

6444201

Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam. Purification and characterization

1984

D'Aniello, A.; Strazullo, L.

J. Biol. Chem.

259

4237-4243

210775

7011505

In vitro studies on L-serine deaminase activity of Escherichia coli K12

1980

Newman, E.B.; Kapoor, V.

Can. J. Biochem.

58

1292-1297

210777

322657

L-Serine dehydratase from Arthrobacter globiformis

1977

Gannon, F.; Bridgeland, E.S.; Jones, K.M.

Biochem. J.

161

345-355

210780

4800518

Serine dehydratase in animal tissues

1973

Grillo, M.A.

Acta Vitaminol. Enzymol.

27

51-61

210781

-

Purification and some properties of L-serine dehydratase of Corynebacterium sp.

1974

Morikawa, Y.; Nakamura, N.; Kimura, K.

Agric. Biol. Chem.

38

531-537

210791

9637015

Partial purification of an iron-dependent L-serine dehydratase from Clostridium sticklandii

1998

Zinecker, H.; Andreesen, J.R.; Pich, A.

J. Basic Microbiol.

38

147-155

210792

8344301

L-Serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups

1993

Hofmeister, A.E.M.; Grabowski, R.; Linder, D.; Buckel, W.

Eur. J. Biochem.

215

341-349

210801

-

Enzymes accompanying tyrosine phenol lyase and the problem of its substrate specificity

1983

Faleev, N.G.; Vikha, Yu.K.; Martinkova, N.S.; Belikov, V.M.

Curr. Microbiol.

9

235-240

210802

6406501

Characterization of the catalytic pathway for D-serine dehydratase

1983

Federiuk, C.S.; Bayer, R.; Shafer, J.A.

J. Biol. Chem.

258

5379-5385

210803

6853521

A reaction pathway for transimination of the pyridoxal 5'-phosphate in D-serine dehydratase by amino acids

1983

Federiuk, C.S.; Shafer, J.A.

J. Biol. Chem.

258

5372-5378

210804

9222324

Sequence of Escherichia coli D-serine dehydratase

1981

Schiltz, E.; Schmitt, W.

FEBS Lett.

134

57-62

210805

7019208

Inactivation of D-serine dehydratase by alkylamines via a transimination of enzyme-linked cofactor

1981

Federiuk, C.S.; Shafer, J.A.

J. Biol. Chem.

256

7416-7423

210806

383145

Mechanism of action of D-serine dehydratase. Identification of a transient intermediate

1979

Schnackerz, K.D.; Ehrlich, J.H.; Giesemann, W.; Reed, T.A.

Biochemistry

18

3557-3563

210807

32169

A D-serine dehydratase acting also on L-serine from Klebsiella pneumoniae

1978

Kikuchi, S.; Ishimoto, M.

J. Biochem.

84

1133-1138

210808

1090587

Escherichia coli K-12 mutant forming a temperature-sensitive D-serine deaminase

1975

McFall, E.

J. Bacteriol.

121

1074-1077

210810

-

D-Serine dehydratase (Escherichia coli)

1971

Robinson, W.G.; Labow, R.

Methods Enzymol.

17B

356-360

210811

5327100

Purification and properties of D-serine dehydrase from Escherichia coli

1966

Dupourque, D.; Newton, W.A.; Snell, E.E.

J. Biol. Chem.

241

1233-1238

210812

163811

Isolation and characterization of catabolite-resistant mutants in the D-serine deaminase system of Escherichia coli K-12

1975

Bloom, F.R.

J. Bacteriol.

121

1085-1091

210813

6998484

Pyridoxal-5'-deoxymethylenephosphonate reconstituted D-serine dehydratase: a phosphorus-31 nuclear magnetic resonance study

1980

Schackerz, K.D.; Feldmann, K.

Biochem. Biophys. Res. Commun.

95

1832-1838

210814

3053700

The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5'-phosphate produced by substitutions of aspartic acid for glycine

1988

Marceau, M.; Lewis, S.D.; Shafer, J.A.

J. Biol. Chem.

263

16934-16941

210815

-

Stability of hyperproduction of D-serine deaminase and tryptophanase in Escherichia coli

1987

Pavlasova, E.; Stejskalova, E.; Sikyta, B.

Biotechnol. Lett.

9

761-764

210816

2201774

Crystallization and preliminary X-ray studies of D-serine dehydratase from Escherichia coli

1990

Obmolova, G.; Tepliakov, A.; Harutyunyan, E.; Wahler, G.; Schnackerz, K.D.

J. Mol. Biol.

214

641-642

210817

7814336

D-Serine deaminase is a stringent selective marker in genetic crosses

1995

Maas, W.K.; Maas, R.; McFall, E.

J. Bacteriol.

177

459-461

289258

13129249

Kynureninase from Neurospora: Interaction of enzyme with substrates, coenzyme, and amines

1953

Jacoby, W.B.; Bonner, D.M.

J. Biol. Chem.

205

709-715

349539

-

Synthesis of L-alanine and L-valine by enzyme systems from Bacillus megaterium

1990

Honorat, A.; Monot, F.; Ballerini, D.

Enzyme Microb. Technol.

12

515-520

349581

11041346

Purification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia

2000

Laue, H.; Cook, A.M.

Arch. Microbiol.

174

162-167

391833

1348188

Specificity and kinetics of Rhodotorula gracilis D-amino acid oxidase

1992

Pollegioni, L.; Falbo, A.; Pilone, M.S.

Biochim. Biophys. Acta

1120

11-16

391834

-

Some properties of peroxisome-associated D-amino acid oxidase from Candida tropicalis

1986

Yoshizawa, M.; Ueda, M.; Mozaffar, S.; Tanaka, A.

Agric. Biol. Chem.

50

2637-2638

391841

15607

A D-amino acid oxidase from Chlorella vulgaris

1977

Pistorius, E.K.; Voss, H.

Biochim. Biophys. Acta

481

395-406

391844

-

D-Amino acid oxidase activity in the yeast Rhodotorula gracilis

1982

Simonetta, M.P.; Vanoni, M.A.; Curti, B.

FEMS Microbiol. Lett.

15

27-31

391847

2865242

D-amino acid oxidase from the yeast Trigonopsis variabilis

1985

Kubicek-Pranz, E.M.; Röhr, M.

J. Appl. Biochem.

7

104-113

391848

-

Properties and chemical modification of D-amino acid oxidase from Trigonopsis variabilis

1996

Schraeder, T.; Andreesen, J.R.

Arch. Microbiol.

165

41-47

391852

-

Purification and properties of D-amino-acid oxidase, an inducible flavoenzyme from Rhodotorula gracilis

1987

Simonetta, M.P.; Vanoni, M.A.; Casalin, P.

Biochim. Biophys. Acta

914

136-142

391853

11330678

Characterization and high-level production of D-amino acid oxidase in Candida boidinii

2001

Yurimoto, H.; Hasegawa, T.; Sakai, Y.; Kato, N.

Biosci. Biotechnol. Biochem.

65

627-633

391854

11754736

Effects of hydrogen bond in association with flavin and substrate in flavoenzyme D-amino acid oxidase. The catalytic and structural roles of gly313 and thr317

2002

Setoyama, C.; Nishina,Y.; Tamaoki, H.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Shiga, K.; Miura, R.

J. Biochem.

131

59-69

394966

11823469

Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase

2002

Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T.

J. Biol. Chem.

277

12861-12867

394968

6131836

Effects of solubilization on some properties of the membrane-bound respiratory enzyme D-amino acid dehydrogenase of Escherichia coli

1983

Jones, H.; Venables, W.A.

FEBS Lett.

151

189-192

394971

6102989

Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B

1980

Olsiewski, P.J.; Kaczorowski, G.J.; Walsh, C.

J. Biol. Chem.

255

4487-4494

394974

-

D-Amino acid dehydrogenase (Pseudomonas fluorescens)

1971

Tsukada, K.

Methods Enzymol.

17B

623-624

485776

-

alpha-Methylserine transhydroxymethylase (Pseudomonas)

1971

Wilson Miles, E.

Methods Enzymol.

17B

341-346

485777

14001018

Metabolism of alpha-methylserine. I. Alpha-methylserine hydroxymethyltransferase

1962

Wilson, E.M.; Snell, E.E.

J. Biol. Chem.

237

3171-3179

486807

5847960

Purification and properties of acetyl-CoA: D-amino acid-alpha-N-acetyltransferase from yeast

1965

Zenk, M.H.; Schmitt, J.H.

Biochem. Z.

342

54-65

487962

8784770

Purification and characterization of gamma-glutamyl transpeptidase from Ascaris suum

1996

Hussein, A.S.; Walter, R.D.

Mol. Biochem. Parasitol.

77

41-47

636694

1814136

Some properties of serine: glyoxylate aminotransferase from rye seedlings (Secale cereale L.)

1991

Paszkowski, A.

Acta Biochim. Pol.

38

437-448

636736

4953710

D-Alanine-D-glutamate transaminase. I. Purification and characterization

1965

Martinez-Carrion, M.; Jenkins, W.T.

J. Biol. Chem.

240

3538-3546

636737

5835935

D-Alanine-D-glutamate transaminase. II. Inhibitors and the mechanism of transamination of D-amino acids

1965

Martinez-Carrion, M.; Jenkins, W.T.

J. Biol. Chem.

240

3547-3552

636746

9792912

Construction and properties of a fragmentary D-amino acid aminotransferase

1998

Fuchikami, Y.; Yoshimura, T.; Gutierrez, A.; Soda, K.; Esaki, N.

J. Biochem.

124

905-910

639082

9028042

A novel NADP+ dependent serine dehydrogenase from Agrobacterium tumefaciens

1997

Chowdhury, E.K.; Higuchi, K.; Nagata, S.; Misono, H.

Biosci. Biotechnol. Biochem.

61

152-157

639084

12535615

Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)

2003

Fujisawa, H.; Nagata, S.; Misono, H.

Biochim. Biophys. Acta

1645

89-94

640195

3228235

Novel D-amino acid transaminase

1988

Aretz, W.; Sauber, K.

Ann. N. Y. Acad. Sci.

542

366-370

641562

7115773

Purification and properties of pyruvate kinase type M2 from rat lung

1982

Schering, B.; Eigenbrodt, E.; Linder, D.; Schoner, W.

Biochim. Biophys. Acta

717

337-347

642033

4337852

Enzymatic phosphorylation of serine

1972

Cagen, L.M.; Friedmann, H.C.

J. Biol. Chem.

247

3382-3392

644481

-

D-Glucosaminate

1984

Iwamoto, R.; Imanaga, Y.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

5

253-262

648246

-

Reaction of 1-aminocyclopropane-1-carboxylate deaminase with beta-chloro-D-alanine

1986

Honma, M.

Agric. Biol. Chem.

50

3189-3190

648252

-

Enzymatic deamination of d-coronamic acid: stereoselectivity of 1-aminocyclopropane-1-carboxylate deaminase

1979

Honma, M.; Shimomura, T.; Shiraishi, K.; Ichihara, A.; Sakamura, S.

Agric. Biol. Chem.

43

1677-1679

648260

9604000

Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus

1998

Minami, R.; Uchiyama, K.; Murakami, T.; Kawai, J.; Mikami, K.; Yamada, T.; Yokoi, D.; Ito, H.; Matsui, H.; Honma, M.

J. Biochem.

123

1112-1118

649578

11676496

Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei

2001

Yokoigawa, K.; Hirasawa, R.; Ueno, H.; Okubo, Y.; Umesako, S.; Soda, K.

Biochem. Biophys. Res. Commun.

288

676-684

649621

12821154

Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella typhimurium

2003

Khan, F.; Jala, V.R.; Rao, N.A.; Savithri, H.S.

Biochem. Biophys. Res. Commun.

306

1083-1088

650819

9545431

Active-site mutants of the VanC2 D-alanyl-D-serine ligase, characteristic of one vancomycin-resistant bacterial phenotype, revert towards wild-type D-alanyl-D-alanine ligases

1998

Healy, V.L.; Park, I.S.; Walsh, C.T.

Chem. Biol.

5

197-207

651494

14688104

L-serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni

2004

Velayudhan, J.; Jones, M.A.; Barrow, P.A.; Kelly, D.J.

Infect. Immun.

72

260-268

651680

11244061

Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase

2001

Uo, T.; Yoshimura, T.; Tanaka, N.; Takegawa, K.; Esaki, N.

J. Bacteriol.

183

2226-2233

651817

-

Characterization of thermostable tyrosine phenol-lyase from an obligatory symbiotic thermophile, Symbiobacterium sp. SC-1

1999

Lee, S.G.; Hong, S.P.; Kwak, M.S.; Esaki, N.; Sung, M.H.

J. Biochem. Mol. Biol.

32

480-485

651822

-

Molecular cloning of an extremely thermostable alanine racemase from Aquifex pyrophilus and enzymatic characterization of the expressed protein

2000

Kim, S.S.; Yu, Y.G.

J. Biochem. Mol. Biol.

33

82-88

651969

10601247

Substitution of pyridoxal 5'-phosphate in D-serine dehydratase from Escherichia coli by cofactor analogues provides information on cofactor binding and catalysis

1999

Schnackerz, K.D.; Tai, C.H.; Potsch, R.K.W.; Cook, P.F.

J. Biol. Chem.

274

36935-36943

652947

-

Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon

2001

Uo, T.; Ueda, M.; Nishiyama, T.; Yoshimura, T.; Esaki, N.

J. Mol. Catal. B

12

137-144

653275

12823810

Uropathogenic Escherichia coli use d-serine deaminase to modulate infection of the murine urinary tract

2003

Roesch, P.L.; Redford, P.; Batchelet, S.; Moritz, R.L.; Pellett, S.; Haugen, B.J.; Blattner, F.R.; Welch, R.A.

Mol. Microbiol.

49

55-67

654786

15701048

D-Amino acid oxidase: structure, catalytic mechanism, and practical application

2005

Tishkov, V.I.; Khoronenkova, S.V.

Biochemistry

70

40-54

655274

15694590

Catalytic and structural characteristics of carp hepatopancreas D-amino acid oxidase expressed in Escherichia coli

2005

Sarower, M.G.; Okada, S.; Abe, H.

Comp. Biochem. Physiol. B

140

417-425

655441

12354107

Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study

2002

Boselli, A.; Sacchi, S.; Job, V.; Pilone, M.S.; Pollegioni, L.

Eur. J. Biochem.

269

4762-4771

657695

15375647

D-amino acid N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free D-amino acids

2004

Yow, G.Y.; Uo, T.; Yoshimura, T.; Esaki, N.

Arch. Microbiol.

182

396-403

660824

-

The presence of two serine racemases in Streptomyces garyphalus, a D-cycloserine producer

1981

Svensson, M.L.; Gatenbeck, S.

Arch. Microbiol.

129

213-215

661002

15796715

A novel assay method for an amino acid racemase reaction based on circular dichroism

2005

Noda, M.; Matoba, Y.; Kumagai, T.; Sugiyama, M.

Biochem. J.

389

491-496

661012

16008521

Diversification in substrate usage by glutathione synthetases from soya bean (Glycine max), wheat (Triticum aestivum) and maize (Zea mays)

2005

Skipsey, M.; Davis, B.G.; Edwards, R.

Biochem. J.

391

567-574

661171

16185077

Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity

2005

Strisovsky, K.; Jiraskova, J.; Mikulova, A.; Rulisek, L.; Konvalinka, J.

Biochemistry

44

13091-13100

661725

12560076

Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate

2003

Strisovsky, K.; Jiraskova, J.; Barinka, C.; Majer, P.; Rojas, C.; Slusher, B.S.; Konvalinka, J.

FEBS Lett.

535

44-48

662359

15536068

Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity

2005

Foltyn, V.N.; Bendikov, I.; De Miranda, J.; Panizzutti, R.; Dumin, E.; Shleper, M.; Li, P.; Toney, M.D.; Kartvelishvily, E.; Wolosker, H.

J. Biol. Chem.

280

1754-1763

662483

16233841

D-Amino acid dipeptide production utilizing D-alanine-D-alanine ligases with novel substrate specificity

2005

Sato, M.; Kirimura, K.; Kino, K.

J. Biosci. Bioeng.

99

623-628

662958

16182447

Regulation of serine racemase activity by D-serine and nitric oxide in human glioblastoma cells

2006

Shoji, K.; Mariotto, S.; Ciampa, A.R.; Suzuki, H.

Neurosci. Lett.

392

75-78

663264

9892700

Purification of serine racemase: biosynthesis of the neuromodulator D-serine

1999

Wolosker, H.; Sheth, K.N.; Takahashi, M.; Mothet, J.P.; Brady, R.O., Jr.; Ferris, C.D.; Snyder, S.H.

Proc. Natl. Acad. Sci. USA

96

721-725

663788

1695086

Choline derivatives increase two different acid phosphatases in Rhizobium meliloti and Pseudomonas aeruginosa

1990

Lucchini, A.E.; Lisa, T.A.; Domenech, C.E.

Arch. Microbiol.

153

596-599

664227

16290167

Ionization state of pyridoxal 5'-phosphate in d-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by (31)P NMR spectroscopy

2006

Schnackerz, K.D.; Keller, J.; Phillips, R.S.; Toney, M.D.

Biochim. Biophys. Acta

1764

230-238

665546

15155761

Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis

2004

Cicchillo, R.M.; Baker, M.A.; Schnitzer, E.J.; Newman, E.B.; Krebs, C.; Booker, S.J.

J. Biol. Chem.

279

32418-32425

666133

16221850

D-Serine is the dominant endogenous coagonist for NMDA receptor neurotoxicity in organotypic hippocampal slices

2005

Shleper, M.; Kartvelishvily, E.; Wolosker, H.

J. Neurosci.

25

9413-9417

666610

15830131

The dsdA gene from Escherichia coli provides a novel selectable marker for plant transformation

2005

Erikson, O.; Hertzberg, M.; Naesholm, T.

Plant Mol. Biol.

57

425-433

668271

16009141

Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: comparison with prolidase I and II purified from normal human erythrocytes

2005

Liu, G.; Nakayama, K.; Sagara, Y.; Awata, S.; Yamashita, K.; Manabe, M.; Kodama, H.

Clin. Biochem.

38

625-631

672685

17090922

Substrate specificity of thermostable D-alanine-D-alanine ligase from Thermotoga maritima ATCC 43589

2006

Sato, M.; Kirimura, K.; Kino, K.

Biosci. Biotechnol. Biochem.

70

2790-2792

672703

16245349

Thermostabilization of porcine kidney D-amino acid oxidase by a single amino acid substitution

2006

Bakke, M.; Setoyama, C.; Miura, R.; Kajiyama, N.

Biotechnol. Bioeng.

93

1023-1027

673646

16616139

Characterization of human D-amino acid oxidase

2006

Molla, G.; Sacchi, S.; Bernasconi, M.; Pilone, M.S.; Fukui, K.; Polegioni, L.

FEBS Lett.

580

2358-2364

674360

16452318

Potential role for astroglial D-amino acid oxidase in extracellular D-serine metabolism and cytotoxicity

2006

Park, H.K.; Shishido, Y.; Ichise-Shishido, S.; Kawazoe, T.; Ono, K.; Iwana, S.; Tomita, Y.; Yorita, K.; Sakai, T.; Fukui, K.

J. Biochem.

139

295-304

674365

16751595

Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the active-site lid

2006

Setoyama, C.; Nishina, Y.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Kamiya, N.; Shiga, K.; Miura, R.

J. Biochem.

139

873-879

677016

17088322

Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring

2006

Kawazoe, T.; Tsuge, H.; Pilone, M.S.; Fukui, K.

Protein Sci.

15

2708-2717

677529

17254537

Simultaneous measurement of D-serine dehydratase and d-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase high-performance liquid chromatography

2007

Tanaka, H.; Yamamoto, A.; Ishida, T.; Horiike, K.

Anal. Biochem.

362

83-88

677539

17869212

Enzymatic assay of D-serine using D-serine dehydratase from Saccharomyces cerevisiae

2007

Ito, T.; Takahashi, K.; Naka, T.; Hemmi, H.; Yoshimura, T.

Anal. Biochem.

371

167-172

678079

17937657

A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae

2008

Ito, T.; Hemmi, H.; Kataoka, K.; Mukai, Y.; Yoshimura, T.

Biochem. J.

409

399-406

679652

17880399

D-Amino acid oxidase and serine racemase in human brain: normal distribution and altered expression in schizophrenia

2007

Verrall, L.; Walker, M.; Rawlings, N.; Benzel, I.; Kew, J.N.; Harrison, P.J.; Burnet, P.W.

Eur. J. Neurosci.

26

1657-1669

679665

17109841

Effects of MK-801 on the expression of serine racemase and D-amino acid oxidase mRNAs and on the D-serine levels in rat brain

2007

Hashimoto, A.; Yoshikawa, M.; Andoh, H.; Yano, H.; Matsumoto, H.; Kawaguchi, M.; Oka, T.; Kobayashi, H.

Eur. J. Pharmacol.

555

17-22

680142

17785472

Roles of serine accumulation and catabolism in the colonization of the murine urinary tract by Escherichia coli CFT073

2007

Anfora, A.T.; Haugen, B.J.; Roesch, P.; Redford, P.; Welch, R.A.

Infect. Immun.

75

5298-5304

680516

17965169

Purification and characterization of serine racemase from a hyperthermophylum Pyrobaculum islandicum

2007

Ohnishi, M.; Saito, M.; Wakabayashi, S.; Ishizuka, M.; Nishimura, K.; Nagata, Y.; Kasai, S.

J. Bacteriol.

190

1359-1365

680567

17977854

D-serine dehydratase from chicken kidney: A vertebral homologue of the cryptic enzyme from Burkholderia cepacia

2008

Tanaka, H.; Yamamoto, A.; Ishida, T.; Horiike, K.

J. Biochem.

143

49-57

684409

18191464

High-throughput screening assay for D-amino acid oxidase

2008

Khoronenkova, S.V.; Tishkov, V.I.

Anal. Biochem.

374

405-410

684417

18229946

Characterization of a yeast D-amino acid oxidase microbiosensor for D-serine detection in the central nervous system

2008

Pernot, P.; Mothet, J.P.; Schuvailo, O.; Soldatkin, A.; Pollegioni, L.; Pilone, M.; Adeline, M.T.; Cespuglio, R.; Marinesco, S.

Anal. Chem.

80

1589-1597

684835

17303072

Structural basis of D-DOPA oxidation by D-amino acid oxidase: altersodiumtive pathway for dopamine biosynthesis

2007

Kawazoe, T.; Tsuge, H.; Imagawa, T.; Aki, K.; Kuramitsu, S.; Fukui, K.

Biochem. Biophys. Res. Commun.

355

385-391

685602

18455394

The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors

2008

Sparey, T.; Abeywickrema, P.; Almond, S.; Brandon, N.; Byrne, N.; Campbell, A.; Hutson, P.H.; Jacobson, M.; Jones, B.; Munshi, S.; Pascarella, D.; Pike, A.; Prasad, G.S.; Sachs, N.; Sakatis, M.; Sardana, V.; Venkatraman, S.; Young, M.B.

Bioorg. Med. Chem. Lett.

18

3386-3391

685750

18330517

Subunit fusion of two yeast D-amino acid oxidases enhances their thermostability and resistance to H2O2

2008

Wang, S.J.; Yu, C.Y.; Lee, C.K.; Chern, M.K.; Kuan, I.C.

Biotechnol. Lett.

30

1415-1422

686020

17396222

Physiological functions of D-amino acid oxidases: from yeast to humans

2007

Pollegioni, L.; Piubelli, L.; Sacchi, S.; Pilone, M.S.; Molla, G.

Cell. Mol. Life Sci.

64

1373-1394

686069

17924443

Human D-amino acid oxidase: an update and review

2007

Kawazoe, T.; Park, H.K.; Iwana, S.; Tsuge, H.; Fukui, K.

Chem. Rec.

7

305-315

686567

18448092

Mice lacking D-amino acid oxidase activity exhibit marked reduction of methamphetamine-induced stereotypy

2008

Hashimoto, A.; Konno, R.; Yano, H.; Yoshikawa, M.; Tamaki, R.; Matsumoto, H.; Kobayashi, H.

Eur. J. Pharmacol.

586

221-225

686570

17681761

In vitro and in vivo pharmacological profile of AS057278, a selective D-amino acid oxidase inhibitor with potential anti-psychotic properties

2008

Adage, T.; Trillat, A.C.; Quattropani, A.; Perrin, D.; Cavarec, L.; Shaw, J.; Guerassimenko, O.; Giachetti, C.; Greco, B.; Chumakov, I.; Halazy, S.; Roach, A.; Zaratin, P.

Eur. Neuropsychopharmacol.

18

200-214

687746

18544534

pLG72 modulates intracellular D-serine levels through its interaction with D-amino acid oxidase: Effect on schizophrenia susceptibility

2008

Sacchi, S.; Bernasconi, M.; Martineau, M.; Mothet, J.P.; Ruzzene, M.; Pilone, M.S.; Pollegioni, L.; Molla, G.

J. Biol. Chem.

283

22244-22256

687891

18588925

A biosensor for all D-amino acids using evolved D-amino acid oxidase

2008

Rosini, E.; Molla, G.; Rossetti, C.; Pilone, M.S.; Pollegioni, L.; Sacchi, S.

J. Biotechnol.

135

377-384

688278

18507366

Synthesis and biological evaluation of D-amino acid oxidase inhibitors

2008

Ferraris, D.; Duvall, B.; Ko, Y.S.; Thomas, A.G.; Rojas, C.; Majer, P.; Hashimoto, K.; Tsukamoto, T.

J. Med. Chem.

51

3357-3359

688608

18603832

Long-term treatment with morphine increases the D-serine content in the rat brain by regulating the mRNA and protein expressions of serine racemase and D-amino acid oxidase

2008

Yoshikawa, M.; Shinomiya, T.; Takayasu, N.; Tsukamoto, H.; Kawaguchi, M.; Kobayashi, H.; Oka, T.; Hashimoto, A.

J. Pharmacol. Sci.

107

270-276

689217

17890006

D-amino acid oxidase (DAO) genotype and mood symptomatology in schizophrenia

2007

Corvin, A.; Donohoe, G.; McGhee, K.; Murphy, K.; Kenny, N.; Schwaiger, S.; Nangle, J.M.; Morris, D.; Gill, M.

Neurosci. Lett.

426

97-100

690048

18378121

Increased brain D-amino acid oxidase (DAAO) activity in schizophrenia

2008

Madeira, C.; Freitas, M.E.; Vargas-Lopes, C.; Wolosker, H.; Panizzutti, R.

Schizophr. Res.

101

76-83

692924

19193709

Gene cloning and expression of pyridoxal 5-phosphate-dependent L-threo-3-hydroxyaspartate dehydratase from Pseudomonas sp. T62, and characterization of the recombinant enzyme

2009

Murakami, T.; Maeda, T.; Yokota, A.; Wada, M.

J. Biochem.

145

661-668

693175

18784082

Crystal structure of DltA: implications for the reaction mechanism of non-ribosomal peptide synthetase (NRPS) adenylation domains

2008

Yonus, H.; Neumann, P.; Zimmermann, S.; May, J.J.; Marahiel, M.A.; Stubbs, M.T.

J. Biol. Chem.

283

32484-32491

694606

19251290

Substrate specificity in phospholipid transformations by plant phospholipase D isoenzymes

2009

Dippe, M.; Ulbrich-Hofmann, R.

Phytochemistry

70

361-365

694974

18812225

Recombinant human serine racemase: enzymologic characterization and comparison with its mouse ortholog

2009

Hoffman, H.E.; Jiraskova, J.; Ingr, M.; Zvelebil, M.; Konvalinka, J.

Protein Expr. Purif.

63

62-67

695533

19212808

D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637

2010

Tanigawa, M.; Shinohara, T.; Saito, M.; Nishimura, K.; Hasegawa, Y.; Wakabayashi, S.; Ishizuka, M.; Nagata, Y.D

Amino Acids

38

247-255

696139

19591808

Commentary: genome-based CNS drug discovery: D-amino acid oxidase (DAAO) as a novel target for antipsychotic medications: progress and challenges

2009

Williams, M.

Biochem. Pharmacol.

78

1360-1365

696158

19216715

D-amino acid oxidase: physiological role and applications

2008

Khoronenkova, S.V.; Tishkov, V.I.

Biochemistry (Moscow)

73

1511-1518

696568

19217074

Co-administration of a D-amino acid oxidase inhibitor potentiates the efficacy of D-serine in attenuating prepulse inhibition deficits after administration of dizocilpine

2009

Hashimoto, K.; Fujita, Y.; Horio, M.; Kunitachi, S.; Iyo, M.; Ferraris, D.; Tsukamoto, T.

Biol. Psychiatry

65

1103-1106

698099

19751394

Genetic loss of D-amino acid oxidase activity reverses schizophrenia-like phenotypes in mice

2009

Labrie, V.; Wang, W.; Barger, S.W.; Baker, G.B.; Roder, J.C.

Genes Brain Behav.

9

11-25

699164

19586804

Determination of D-serine and D-alanine in the tissues and physiological fluids of mice with various D-amino-acid oxidase activities using two-dimensional high-performance liquid chromatography with fluorescence detection

2009

Miyoshi, Y.; Hamase, K.; Tojo, Y.; Mita, M.; Konno, R.; Zaitsu, K.

J. Chromatogr. B

877

2506-2512

699464

19438227

Discovery, SAR, and pharmacokinetics of a novel 3-hydroxyquinolin-2(1H)-one series of potent D-amino acid oxidase (DAAO) inhibitors

2009

Duplantier, A.J.; Becker, S.L.; Bohanon, M.J.; Borzilleri, K.A.; Chrunyk, B.A.; Downs, J.T.; Hu, L.Y.; El-Kattan, A.; James, L.C.; Liu, S.; Lu, J.; Maklad, N.; Mansour, M.N.; Mente, S.; Piotrowski, M.A.; Sakya, S.M.; Sheehan, S.; Steyn, S.J.; Strick, C.A.; Williams, V.A.; Zhang, L.

J. Med. Chem.

52

3576-3585

699758

19088300

The behavioral and neurochemical effects of a novel D-amino acid oxidase inhibitor compound 8 [4H-thieno [3,2-b]pyrrole-5-carboxylic acid] and D-serine

2009

Smith, S.M.; Uslaner, J.M.; Yao, L.; Mullins, C.M.; Surles, N.O.; Huszar, S.L.; McNaughton, C.H.; Pascarella, D.M.; Kandebo, M.; Hinchliffe, R.M.; Sparey, T.; Brandon, N.J.; Jones, B.; Venkatraman, S.; Young, M.B.; Sachs, N.; Jacobson, M.A.; Hutson, P.H.

J. Pharmacol. Exp. Ther.

328

921-930

700217

6113535

D-Amino acid dehydrogenase of Escherichia coli K12: positive selection of mutants defective in enzyme activity and localization of the structural gene

1981

Wild, J.; Klopotowski, T.

Mol. Gen. Genet.

181

373-378

700312

19786963

The neurobiology of D-amino acid oxidase and its involvement in schizophrenia

2009

Verrall, L.; Burnet, P.W.; Betts, J.F.; Harrison, P.J.

Mol. Psychiatry

15

122-137

700611

18940194

Mutant mice with reduced NMDA-NR1 glycine affinity or lack of D-amino acid oxidase function exhibit altered anxiety-like behaviors

2009

Labrie, V.; Clapcote, S.J.; Roder, J.C.

Pharmacol. Biochem. Behav.

91

610-620

702425

19264108

Detection of a gem-diamine and a stable quinonoid intermediate in the reaction catalyzed by serine-glyoxylate aminotransferase from Hyphomicrobium methylovorum

2009

Karsten, W.E.; Cook, P.F.

Biochim. Biophys. Acta

1790

575-580

702966

19733154

In vitro evidence that D-serine disturbs the citric acid cycle through inhibition of citrate synthase activity in rat cerebral cortex

2009

Zanatta, A.; Schuck, P.F.; Viegas, C.M.; Knebel, L.A.; Busanello, E.N.; Moura, A.P.; Wajner, M.

Brain Res.

1298

186-193

703653

19549189

Serine hydroxymethyltransferase from Plasmodium vivax is different in substrate specificity from its homologues

2009

Sopitthummakhun, K.; Maenpuen, S.; Yuthavong, Y.; Leartsakulpanich, U.; Chaiyen, P.

FEBS J.

276

4023-4036

704093

19582219

Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate

2009

Shimada, A.; Ozaki, H.; Saito, T.; Noriko, F.

Int. J. Mol. Sci.

10

2578-2590

705545

19720515

Heterologous expression of the Bacillus subtilis (natto) alanine dehydrogenase in Escherichia coli and Lactococcus lactis

2009

Ye, W.; Huo, G.; Chen, J.; Liu, F.; Yin, J.; Yang, L.; Ma, X.

Microbiol. Res.

165

268-275

705602

19591881

Characterization of Plasmodium falciparum serine hydroxymethyltransferase-A potential antimalarial target

2009

Maenpuen, S.; Sopitthummakhun, K.; Yuthavong, Y.; Chaiyen, P.; Leartsakulpanich, U.

Mol. Biochem. Parasitol.

168

63-73

706960

19851013

Crystallization and preliminary X-ray analysis of a D-Ala:D-Ser ligase associated with VanG-type vancomycin resistance

2009

Weber, P.; Meziane-Cherif, D.; Haouz, A.; Saul, F.A.; Courvalin, P.

Acta Crystallogr. Sect. F

65

1024-1026

710442

9294159

Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC2 from Enterococcus casseliflavus as a D-Ala-D-Ser ligase

1997

Park, I.S.; Lin, C.H.; Walsh, C.T.

Proc. Natl. Acad. Sci. USA

94

10040-10044

711529

19945264

Development of an implantable D-serine biosensor for in vivo monitoring using mammalian D-amino acid oxidase on a poly (o-phenylenediamine) and Nafion-modified platinum-iridium disk electrode

2010

Zain, Z.M.; ONeill, R.D.; Lowry, J.P.; Pierce, K.W.; Tricklebank, M.; Dewa, A.; Ab Ghani, S.

Biosens. Bioelectron.

25

1454-1459

711718

20564561

Comparative characterization of three D-aspartate oxidases and one D-amino acid oxidase from Caenorhabditis elegans

2010

Katane, M.; Saitoh, Y.; Seida, Y.; Sekine, M.; Furuchi, T.; Homma, H.

Chem. Biodivers.

7

1424-1434

711720

20564563

Mutant mice and rats lacking D-amino acid oxidase

2010

Konno, R.; Hamase, K.; Maruyama, R.; Zaitsu, K.

Chem. Biodivers.

7

1450-1458

712323

20843822

Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23

2010

Maeda, T.; Takeda, Y.; Murakami, T.; Yokota, A.; Wada, M.

J. Biochem.

148

705-712

712324

20876609

Potential cytotoxic effect of hydroxypyruvate produced from D-serine by astroglial D-amino acid oxidase

2010

Chung, S.P.; Sogabe, K.; Park, H.K.; Song, Y.; Ono, K.; Abou El-Magd, R.M.; Shishido, Y.; Yorita, K.; Sakai, T.; Fukui, K.

J. Biochem.

148

743-753

713477

20521334

Effect of ligand binding on human D-amino acid oxidase: implications for the development of new drugs for schizophrenia treatment

2010

Caldinelli, L.; Molla, G.; Bracci, L.; Lelli, B.; Pileri, S.; Cappelletti, P.; Sacchi, S.; Pollegioni, L.

Protein Sci.

19

1500-1512

713970

21878319

Kinetic, mutagenic, and structural homology analysis of L-serine dehydratase from Legionella pneumophila

2011

Xu, X.L.; Chen, S.; Grant, G.A.

Arch. Biochem. Biophys.

515

28-36

714348

21224019

Serine racemase and the serine shuttle between neurons and astrocytes

2011

Wolosker, H.

Biochim. Biophys. Acta

1814

1558-1566

714697

20564571

Site-directed mutagenesis of rice serine racemase: evidence that Glu219 and Asp225 mediate the effects of Mg2+ on the activity

2010

Gogami, Y.; Kobayashi, A.; Ikeuchi, T.; Oikawa, T.

Chem. Biodivers.

7

1579-1590

714985

21668644

Crystal structures of open and closed forms of D-serine deaminase from Salmonella typhimurium - implications on substrate specificity and catalysis

2011

Bharath, S.R.; Bisht, S.; Savithri, H.S.; Murthy, M.R.

FEBS J.

278

2879-2891

715591

21343289

A novel pyridoxal 5'-phosphate-dependent amino acid racemase in the Aplysia californica central nervous system

2011

Wang, L.; Ota, N.; Romanova, E.V.; Sweedler, J.V.

J. Biol. Chem.

286

13765-13774

715627

21676877

Crystal structure of a zinc-dependent D-serine dehydratase from chicken kidney

2011

Tanaka, H.; Senda, M.; Venugopalan, N.; Yamamoto, A.; Senda, T.; Ishida, T.; Horiike, K.

J. Biol. Chem.

286

27548-27558

715733

21601540

Reaction pathway of tryptophanase-catalyzed L-tryptophan synthesis from D-serine

2011

Shimada, A.; Ozaki, H.; Saito, T.; Fujii, N.

J. Chromatogr. B

879

3289-3295

723920

22865246

Structure-function relationships in human D-amino acid oxidase

2012

Sacchi, S.; Caldinelli, L.; Cappelletti, P.; Pollegioni, L.; Molla, G.

Amino Acids

43

1833-1850

723921

22990841

Alteration of intrinsic amounts of D-serine in the mice lacking serine racemase and D-amino acid oxidase

2012

Miyoshi, Y.; Konno, R.; Sasabe, J.; Ueno, K.; Tojo, Y.; Mita, M.; Aiso, S.; Hamase, K.

Amino Acids

43

1919-1931

724401

23157298

Engineering of substrate specificity of D-amino acid oxidase from the yeast Trigonopsis variabilis: directed mutagenesis of Phe258 residue

2012

Komarova, N.V.; Golubev, I.V.; Khoronenkova, S.V.; Chubar, T.A.; Tishkov, V.I.

Biochemistry

77

1181-1189

724793

23994361

D-Amino acid oxidase and presence of D-proline in Xenopus laevis

2013

Soma, H.; Furuya, R.; Kaneko, R.; Tsukamoto, A.; Sirasu, K.; Tanigawa, M.; Nagata, Y.

Comp. Biochem. Physiol. B

166

165-171

724965

21981077

Is rat an appropriate animal model to study the involvement of D-serine catabolism in schizophrenia? Insights from characterization of D-amino acid oxidase

2011

Frattini, L.F.; Piubelli, L.; Sacchi, S.; Molla, G.; Pollegioni, L.

FEBS J.

278

4362-4373

725474

22128181

Biochemical and structural studies of uncharacterized protein PA0743 from Pseudomonas aeruginosa revealed NAD+-dependent L-serine dehydrogenase

2012

Tchigvintsev, A.; Singer, A.; Brown, G.; Flick, R.; Evdokimova, E.; Tan, K.; Gonzalez, C.F.; Savchenko, A.; Yakunin, A.F.

J. Biol. Chem.

287

1874-1883

725676

23566269

4-Hydroxypyridazin-3(2H)-one derivatives as novel D-amino acid oxidase inhibitors

2013

Hondo, T.; Warizaya, M.; Niimi, T.; Namatame, I.; Yamaguchi, T.; Nakanishi, K.; Hamajima, T.; Harada, K.; Sakashita, H.; Matsumoto, Y.; Orita, M.; Takeuchi, M.

J. Med. Chem.

56

3582-3592

726688

21807981

D-Ala-d-Ser VanN-type transferable vancomycin resistance in Enterococcus faecium

2011

Lebreton, F.; Depardieu, F.; Bourdon, N.; Fines-Guyon, M.; Berger, P.; Camiade, S.; Leclercq, R.; Courvalin, P.; Cattoir, V.

Antimicrob. Agents Chemother.

55

4606-4612

727482

23992455

ATP binding to human serine racemase is cooperative and modulated by glycine

2013

Marchetti, M.; Bruno, S.; Campanini, B.; Peracchi, A.; Mai, N.; Mozzarelli, A.

FEBS J.

280

5853-5863

729282

22197591

Crystal structure of D-serine dehydratase from Escherichia coli

2012

Urusova, D.V.; Isupov, M.N.; Antonyuk, S.; Kachalova, G.S.; Obmolova, G.; Vagin, A.A.; Lebedev, A.A.; Burenkov, G.P.; Dauter, Z.; Bartunik, H.D.; Lamzin, V.S.; Melik-Adamyan, W.R.; Mueller, T.D.; Schnackerz, K.D.

Biochim. Biophys. Acta

1824

422-432

729705

22176976

Role of zinc ion for catalytic activity in D-serine dehydratase from Saccharomyces cerevisiae

2012

Ito, T.; Koga, K.; Hemmi, H.; Yoshimura, T.

FEBS J.

279

612-624

729822

24082071

Significance of the D-serine-deaminase and D-serine metabolism of Staphylococcus saprophyticus for virulence

2013

Korte-Berwanger, M.; Sakinc, T.; Kline, K.; Nielsen, H.V.; Hultgren, S.; Gatermann, S.G.

Infect. Immun.

81

4525-4533

729923

22904288

Functional analysis of the genes encoding diaminopropionate ammonia lyase in Escherichia coli and Salmonella enterica serovar Typhimurium

2012

Kalyani, J.N.; Ramachandra, N.; Kachroo, A.H.; Mahadevan, S.; Savithri, H.S.

J. Bacteriol.

194

5604-5612

729953

24881047

Reaction mechanism of Zn2+-dependent D-serine dehydratase: role of a conserved tyrosine residue interacting with pyridine ring nitrogen of pyridoxal 5-phosphate

2014

Ito, T.; Matsuoka, M.; Koga, K.; Hemmi, H.; Yoshimura, T.

J. Biochem.

156

173-180

730889

22519530

D-serine-dehydratase from Saccaromyces cerevisiae: a pyridoxal 5- phosphate-dependent enzyme for advanced biotech applications

2012

Staiano, M.; Strianese, M.; Varriale, A.; Di Giovanni, S.; di Mase, D.S.; DellAngelo, V.; Ruggiero, G.; Labella, T.; Pellecchia, C.; DAuria, S.

Protein Pept. Lett.

19

592-595

735145

24905353

New insights into 1-aminocyclopropane-1-carboxylate (ACC) deaminase phylogeny, evolution and ecological significance

2014

Nascimento, F.; Rossi, M.; Soares, C.; McConkey, B.; Glick, B.

PLoS ONE

9

e99168

736084

24698160

Distinct biochemical properties of human serine hydroxymethyltransferase compared with the Plasmodium enzyme: implications for selective inhibition

2014

Pinthong, C.; Maenpuen, S.; Amornwatcharapong, W.; Yuthavong, Y.; Leartsakulpanich, U.; Chaiyen, P.

FEBS J.

281

2570-2583

741688

25217016

A highly stable d-amino acid oxidase of the thermophilic bacterium Rubrobacter xylanophilus

2014

Takahashi, S.; Furukawara, M.; Omae, K.; Tadokoro, N.; Saito, Y.; Abe, K.; Kera, Y.

Appl. Environ. Microbiol.

80

7219-7229

741867

24256253

D-Serine metabolism new insights into the modulation of D-amino acid oxidase activity

2013

Sacchi, S.

Biochem. Soc. Trans.

41

1551-1556

742077

26965861

D-Amino acid oxidase inhibitors based on the 5-hydroxy-1,2,4-triazin-6(1H)-one scaffold

2016

Hin, N.; Duvall, B.; Berry, J.F.; Ferraris, D.V.; Rais, R.; Alt, J.; Rojas, C.; Slusher, B.S.; Tsukamoto, T.

Bioorg. Med. Chem. Lett.

26

2088-2091

743058

23631755

Structural, kinetic, and pharmacodynamic mechanisms of D-amino acid oxidase inhibition by small molecules

2013

Hopkins, S.C.; Heffernan, M.L.; Saraswat, L.D.; Bowen, C.A.; Melnick, L.; Hardy, L.W.; Orsini, M.A.; Allen, M.S.; Koch, P.; Spear, K.L.; Foglesong, R.J.; Soukri, M.; Chytil, M.; Fang, Q.K.; Jones, S.W.; Varney, M.A.; Panatier, A.; Oliet, S.H.; Pollegioni, L.; Piubelli, L.; Molla, G.; Nardini, M.; Large, T.H.

J. Med. Chem.

56

3710-3724

743062

26309148

6-Hydroxy-1,2,4-triazine-3,5(2H,4H)-dione derivatives as novel D-amino acid oxidase inhibitors

2015

Hin, N.; Duvall, B.; Ferraris, D.; Alt, J.; Thomas, A.G.; Rais, R.; Rojas, C.; Wu, Y.; Wozniak, K.M.; Slusher, B.S.; Tsukamoto, T.

J. Med. Chem.

58

7258-7272

743191

24821597

Selective oxidation of D-amino acids catalyzed by oligolamellar liposomes intercalated with D-amino acid oxidase

2014

Yoshimoto, M.; Okamoto, M.; Ujihashi, K.; Okita, T.

Langmuir

30

6180-6186

743827

28592826

pH-Dependent enantioselectivity of D-amino acid oxidase in aqueous solution

2017

Liu, Q.; Chen, L.; Zhang, Z.; Du, B.; Xiao, Y.; Yang, K.; Gong, L.; Wu, L.; Li, X.; He, Y.

Sci. Rep.

7

2994

744003

25963389

Identification of a novel amino acid racemase from a hyperthermophilic archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids

2015

Kawakami, R.; Ohmori, T.; Sakuraba, H.; Ohshima, T.

Amino Acids

47

1579-1587

745414

28343923

First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3

2017

Kawakami, R.; Sakuraba, H.; Ohmori, T.; Ohshima, T.

J. Biosci. Bioeng.

124

23-27

745545

15328614

Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii

2004

Fujino, A.; Ose, T.; Yao, M.; Tokiwano, T.; Honma, M.; Watanabe, N.; Tanaka, I.

J. Mol. Biol.

341

999-1013

746724

28744579

Triple serine loop region regulates the aspartate racemase activity of the serine/aspartate racemase family

2017

Uda, K.; Abe, K.; Dehara, Y.; Mizobata, K.; Edashige, Y.; Nishimura, R.; Radkov, A.D.; Moe, L.A.

Amino Acids

49

1743-1754

746900

26189018

Expanding the threonine aldolase toolbox for the asymmetric synthesis of tertiary alpha-amino acids

2015

Fesko, K.; Strohmeier, G.A.; Breinbauer, R.

Appl. Microbiol. Biotechnol.

99

9651-9661

747007

30173889

Structural and biochemical studies on the role of active site Thr166 and Asp236 in the catalytic function of D-Serine deaminase from Salmonella typhimurium

2018

Deka, G.; Bharath, S.R.; Savithri, H.S.; Murthy, M.R.N.

Biochem. Biophys. Res. Commun.

504

40-45

747622

26957519

The cryptic dsdA gene encodes a functional D-serine dehydratase in Pseudomonas aeruginosa PAO1

2016

Li, G.; Lu, C.D.

Curr. Microbiol.

72

788-794

747858

29740415

D-Serine metabolism and its importance in development of Dictyostelium discoideum

2018

Ito, T.; Hamauchi, N.; Hagi, T.; Morohashi, N.; Hemmi, H.; Sato, Y.; Saito, T.; Yoshimura, T.

Front. Microbiol.

9

784

748083

21378189

Regulation and characterization of the dadRAX locus for D-amino acid catabolism in Pseudomonas aeruginosa PAO1

2011

He, W.; Li, C.; Lu, C.-D.

J. Bacteriol.

193

2107-2115

748453

25617179

PEGylated D-serine dehydratase as a D-serine reducing agent

2015

Ito, T.; Takada, H.; Isobe, K.; Suzuki, M.; Kitaura, Y.; Hemmi, H.; Matsuda, T.; Sasabe, J.; Yoshimura, T.

J. Pharm. Biomed. Anal.

116

34-39

748612

26475231

Distribution of eukaryotic serine racemases in the bacterial domain and characterization of a representative protein in Roseobacter litoralis Och 149

2016

Kubota, T.; Shimamura, S.; Kobayashi, T.; Nunoura, T.; Deguchi, S.

Microbiology

162

53-61

749753

12819857

A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily

2003

Zhang, Z.; Feige, J.N.; Chang, A.B.; Anderson, I.J.; Brodianski, V.M.; Vitreschak, A.G.; Gelfand, M.S.; Saier, M.H.

Arch. Microbiol.

180

88-100

751157

28347768

Identification of a novel phospholipase D with high transphosphatidylation activity and its application in synthesis of phosphatidylserine and DHA-phosphatidylserine

2017

Mao, X.; Liu, Q.; Qiu, Y.; Fan, X.; Han, Q.; Liu, Y.; Zhang, L.; Xue, C.

J. Biotechnol.

249

51-58

755784

25611820

Engineered L-serine hydroxymethyltransferase from Streptococcus thermophilus for the synthesis of alpha,alpha-dialkyl-alpha-amino acids

2015

Hernandez, K.; Zelen, I.; Petrillo, G.; Uson, I.; Wandtke, C.M.; Bujons, J.; Joglar, J.; Parella, T.; Clapes, P.

Angew. Chem. Int. Ed. Engl.

54

3013-3017

757380

30792183

Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase

2019

Harrison, P.J.; Gable, K.; Somashekarappa, N.; Kelly, V.; Clarke, D.J.; Naismith, J.H.; Dunn, T.M.; Campopiano, D.J.

J. Lipid Res.

60

953-962

759235

31998270

Diversity of D-amino acid utilizing bacteria from Kongsfjorden, Arctic, and the metabolic pathways for seven D-amino acids

2020

Yu, Y.; Yang, J.; Zheng, L.; Sheng, Q.; Li, C.; Wang, M.; Zhang, X.; McMinn, A.; Zhang, Y.; Song, X.; Chen, X.

Front. Microbiol.

10

2983

759259

31921255

AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana

2019

Suarez, J.; Hener, C.; Lehnhardt, V.A.; Hummel, S.; Stahl, M.; Kolukisaoglu, U.e.

Front. Plant Sci.

10

1609