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Ligand D-valine

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

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Show Natural Substrate (3 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.3

D-Val + H2O + O2 = 2-oxoisovalerate + NH3 + H2O2

743827

-

1.4.3.3

D-valine + H2O + O2 = alpha-ketoisovaleric acid + NH3 + H2O2

391828, 391830, 391849, 391865, 391840, 391853, 391833, 391852, 391861, 391841, 391847, 391848

-

1.4.3.3

2 entries

2.3.1.36

acetyl-CoA + D-valine = CoA + N-acetyl-D-valine

486807

-

Substrate in Enzyme-catalyzed Reactions (25 results)

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Show Substrate (25 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.19

D-Val + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2

655429

-

1.4.3.19

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

440361

-

1.4.3.19

D-valine + H2O + O2 = 3-methyl-2-oxobutanoic acid + NH3 + H2O2

689934, 701114

-

1.4.3.3

D-Val + H2O + O2 = 2-oxoisovalerate + NH3 + H2O2

743827, 724401, 741688

-

1.4.3.3

D-Val + H2O + O2 = alpha-ketoisovalerate + NH3 + H2O2

674365, 655441, 655274, 654786

-

1.4.3.3

D-valine + H2O + O2 = 2-oxoisovalerate + NH3 + H2O2

763732

-

1.4.3.3

D-valine + H2O + O2 = alpha-ketoisovalerate + NH3 + H2O2

684409

-

1.4.3.3

D-valine + H2O + O2 = alpha-ketoisovaleric acid + NH3 + H2O2

391828, 391830, 391849, 391865, 391840, 391853, 391833, 391852, 391861, 687891, 391841, 391847, 391848, 686020, 686277, 684598, 685750

-

1.4.5.1

D-valine + oxidized 2,6-dichloroindophenol + H2O = 2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol

394971

-

1.4.5.1

D-valine + oxidized 2,6-dichlorophenolindophenol + H2O = 2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol

696481

-

1.4.5.1

D-valine + oxidized acceptor + H2O = 2-oxoisopentanoate + NH3 + reduced acceptor

700217

-

1.4.99.6

D-Val + H2O + oxidized 2,6-dichlorophenolindophenol = 2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol

695533

-

1.4.99.6

D-valine + H2O + 2,6-dichlorophenolindophenol = 2-oxoisopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol

394974

-

1.4.99.6

D-valine + H2O + FAD = 2-oxopentanoate + NH3 + FADH2

748083

-

1.4.99.6

D-valine + H2O + methylene blue = 2-oxoisopentanoate + NH3 + reduced methylene blue

394974

-

1.4.99.6

D-valine + phenazine methosulfate + H2O = 2-oxopentanoate + NH3 + reduced phenazine methosulfate

762668

-

1.4.3.19

3 entries

1.4.3.3

5 entries

1.4.5.1

3 entries

1.4.99.6

5 entries

1.5.99.13

D-valine + oxidized 2,6-dichloroindophenol + H2O = 2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol

684424, 394966

-

2.3.1.36

acetyl-CoA + D-valine = CoA + N-acetyl-D-valine

657695, 486807

-

2.6.1.21

D-valine + 2-oxoglutarate = 2-oxoisovalerate + D-glutamate

636746

-

2.6.1.21

D-valine + pyruvate = 2-oxoisovalerate + D-alanine

636746, 759259

-

2.6.1.21

2 entries

2.6.1.74

D-valine + 2-oxoadipate = 3-methyl-2-oxobutanoate + 2-aminoadipate

640195

-

5.1.1.10

D-Val = L-Val

745414

-

5.1.1.10

D-valine = L-valine

744003, 745414

-

5.1.1.10

2 entries

5.1.1.21

D-valine = L-Val

729935

-

6.3.2.4

ATP + D-Val = ADP + phosphate + D-Val-D-Val

672685

-

Product in Enzyme-catalyzed Reactions (15 results)

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Show Product (15 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.16

3-methyl-2-oxobutanoate + NH3 + NADPH + H+ = D-valine + NADP+

0

-

1.4.99.6

2-oxo-3-methylbutyric acid + NH3 + NADPH + H+ = D-valine + H2O + NADP+

0

-

2.6.1.21

D-alanine + 2-oxoisovalerate = pyruvate + D-valine

636745

-

3.1.1.1

3'-D-valyl-gemcitabine + H2O = D-valine + gemcitabine

0

-

3.1.1.1

5'-D-valyl-gemcitabine + H2O = D-valine + gemcitabine

0

-

3.1.1.1

2 entries

3.5.1.77

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

0

-

3.5.1.81

N-acetyl-D-Val + H2O = acetate + D-Val

0

-

3.5.1.81

N-Chloroacetyl-D-Val + H2O = Chloroacetate + D-Val

0

-

3.5.1.81

N-acetyl-D-valine + H2O = acetate + D-valine

0

-

3.5.1.81

N-acetyl-DL-valine + H2O = acetate + D-valine

0

-

3.5.1.81

4 entries

5.1.1.1

L-valine = D-valine

0

-

5.1.1.10

L-Val = D-Val

0

-

5.1.1.10

L-valine = D-valine

0

-

5.1.1.21

L-valine = D-Val

0

-

5.1.1.21

L-valine = D-valine

0

-

5.1.1.10

2 entries

5.1.1.21

2 entries

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.13.18

enhances activity at concentrations below 50 mM

664626

-

3.4.13.9

activation of isoforms prolidase I and prolidase II

668271

-

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.20

10 mM, 11% inhibition

349634

-

1.4.1.9

-

349665

-

2.1.2.11

5 mM, 16% inhibition

485700

-

3D Structure of Enzyme-Ligand-Complex (PDB) (11 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (11 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.2.27

7kjm, 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

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (19 results)

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Show Turnover Number (19 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.3

0.25

-

mutant enzyme G222D/Y224G

674365

1.4.3.3

0.433

-

mutant enzymeY224G

674365

1.4.3.3

0.75

-

mutant enzyme R221D/Y224G

674365

1.4.3.3

0.9

-

mutant T317A

391854

1.4.3.3

1.05

-

mutant enzyme E220D/Y224G

674365

1.4.3.3

2.5

-

wild-type enzyme

674365

1.4.3.3

2.5

-

wild-type

391854

1.4.3.3

6

-

D isotope

391858

1.4.3.3

8.67

-

D isotope

391858

1.4.3.3

11.5

-

mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

14.6

-

mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

28.8

-

-

391858

1.4.3.3

31.4

-

at pH 8.0 and 60°C

741688

1.4.3.3

41.7

-

-

391858

1.4.3.3

85.3

-

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

724401

1.4.3.3

170

-

pH 8.0, 37°C

655274

1.4.3.3

225

-

pH 8, 55°C

763732

1.4.3.3

523

-

-

391833

1.4.3.3

18 entries

1.4.99.6

0.78

-

pH 8.7, 37°C

748083

K_M Value (25 results)

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Show KM Value (25 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.3

0.094

-

at pH 8.0 and 60°C

741688

1.4.3.3

0.263

-

pH 8.0, 37°C

655274

1.4.3.3

0.63

-

wild-type enzyme

674365

1.4.3.3

0.63

-

pH 8, 55°C

763732

1.4.3.3

0.67

-

wild-type

391854

1.4.3.3

1.3

-

immobilized wild type enzyme, at 25°C

687891

1.4.3.3

1.4

-

-

391828, 391865

1.4.3.3

3

-

-

391848

1.4.3.3

3.1

-

mutant enzyme E220D/Y224G

674365

1.4.3.3

3.5

-

free enzyme

391842

1.4.3.3

3.7

-

mutant enzyme R221D/Y224G

674365

1.4.3.3

3.95

-

-

391853

1.4.3.3

4.3

-

mutant T317A

391854

1.4.3.3

6

-

pH 8.5, 25°C, mutant enzyme Y238F

655441

1.4.3.3

6.1

-

pH 8.5, 25°C, mutant enzyme Y238S

655441

1.4.3.3

14.4

-

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

724401

1.4.3.3

18.89

-

-

391833

1.4.3.3

18.9

-

pH 8.5, 25°C, wild-type enzyme

655441

1.4.3.3

18.9

-

free wild type enzyme, at 25°C

687891

1.4.3.3

20

-

-

391847

1.4.3.3

41

-

mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

46

-

mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

22 entries

1.4.99.6

3.01

-

pH 8.7, 37°C

748083

5.1.1.10

9.82

-

pH 7.0, 80°C

745414

5.1.1.10

9.82

-

pH 7.0, 80°C, recombinant enzyme

745414

5.1.1.10

2 entries

K_i Value (1 result)

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Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.1.9

10.8

-

inhibition of deamination of D-Leu

349665

References & Links

Literature References (57)

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Show Reference (57 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

349634

3112142

Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization

1987

Asano, Y.; Nakazawa, A.; Endo, K.

J. Biol. Chem.

262

10346-10354

349665

670223

Properties of crystalline leucine dehydrogenase from Bacillus sphaericus

1978

Ohshima, T.; Misono, H.; Soda, K.

J. Biol. Chem.

253

5719-5725

391828

-

D-Amino acid oxidase II. specificity, competitive inhibition and reaction sequence

1965

Dixon, M.; Kleppe, K.

Biochim. Biophys. Acta

96

368-382

391830

-

Immobilized D-amino acid oxidase. Preparation, some enzymatic properties, and potential uses

1974

Tosa, T.; Sano, R.; Chibata, I.

Agric. Biol. Chem.

38

1529-1534

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

391840

13919

Isolation and characterization of a mitochondrial D-amino acid oxidase from Neurospora crassa

1977

Rosenfeld, M.G.; Leiter, E.H.

Can. J. Biochem.

55

66-74

391841

15607

A D-amino acid oxidase from Chlorella vulgaris

1977

Pistorius, E.K.; Voss, H.

Biochim. Biophys. Acta

481

395-406

391842

35257

Immobilization and characterization of D-amino acid oxidase

1979

Parkin, K.; Hultin, H.O.

Biotechnol. Bioeng.

21

939-953

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

391849

-

D-Aminosäure-Oxydase

1974

Bergmeyer, H.U.

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

1

460-461

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

391858

8100225

Kinetic mechanism of D-amino acid oxidases from Rhodotorula gracilis and Trigonopsis variabilis

1993

Pollegioni, L.; Langkau, B.; Tischer, W.; Ghisla, S.; Pilone, M.S.

J. Biol. Chem.

268

13850-13857

391861

7654197

Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis

1995

Pollegioni, L.; Ceciliani, F.; Curti, B.; Ronchi, S.; Pilone, M.S.

Biochem. J.

310

577-583

391865

8882005

Inhibition of D-amino acid oxidase by alpha-keto acids analogs of amino acids

1996

Moreno, J.A.; Montes, F.J.; Catalan, J.; Galan, M.A.

Enzyme Microb. Technol.

18

379-382

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

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

440361

9827558

Purification and characterization of a novel glycine oxidase from Bacillus subtilis

1998

Nishiya, Y.; Imanaka, T.

FEBS Lett.

438

263-266

485700

6463

Ketopantoate hydroxymethyltransferase. II. Physical, catalytic, and regulatory properties

1976

Powers, S.G.; Snell, E.E.

J. Biol. Chem.

251

3786-3793

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

636745

8977094

Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1

1996

Ro, H.S.; Hong, S.P.; Seo, H.J.; Yoshimura, T.; Esaki, N.; Soda, K.; Kim, H.S.; Sung, M.H.

FEBS Lett.

398

141-145

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

640195

3228235

Novel D-amino acid transaminase

1988

Aretz, W.; Sauber, K.

Ann. N. Y. Acad. Sci.

542

366-370

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

655429

11874460

Overexpression of a recombinant wild-type anf His-tagged Bacillus subtilis glycine oxidase in Escherichia coli

2002

Job, V.; Molla, G.; Pilone, M.S.; Pollegioni, L.

Eur. J. Biochem.

269

1456-1463

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

664626

15552267

Characteristics of prolinase against various iminodipeptides in erythrocyte lysates from a normal human and a patient with prolidase deficiency

2004

Wang, W.; Liu, G.; Yamashita, K.; Manabe, M.; Kodama, H.

Clin. Chem. Lab. Med.

42

1102-1108

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

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

684409

18191464

High-throughput screening assay for D-amino acid oxidase

2008

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

Anal. Biochem.

374

405-410

684424

18558115

Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane

2008

Tani, Y.; Tanaka, K.; Yabutani, T.; Mishima, Y.; Sakuraba, H.; Ohshima, T.; Motonaka, J.

Anal. Chim. Acta

619

215-220

684598

17279391

Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae

2007

Geueke, B.; Weckbecker, A.; Hummel, W.

Appl. Microbiol. Biotechnol.

74

1240-1247

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

686277

18220846

Engineering the properties of D-amino acid oxidases by a rational and a directed evolution approach

2007

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

Curr. Protein Pept. Sci.

8

600-618

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

689934

17894345

Characterization and structural modeling of a novel thermostable glycine oxidase from Geobacillus kaustophilus HTA426

2008

Martinez-Martinez, I.; Navarro-Fernandez, J.; Garcia-Carmona, F.; Takami, H.; Sanchez-Ferrer, A.

Proteins

70

1429-1441

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

696481

3101751

Solubilization, purification and characterization of D-alanine dehydrogenase from Pseudomonas aeruginosa and effects of solubilization on its properties

1987

Magor, A.M.; Venables, W.A.

Biochimie

69

63-69

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.

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