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Ligand D-Leu

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (6 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.3

D-Leu + H2O + O2 = 4-methyl-2-oxopentanoate + NH3 + H2O2

743827

-

1.4.3.3

D-leucine + H2O + O2 = 4-methyl-2-oxopentanoic acid + NH3 + H2O2

391830, 391865, 391840, 391853, 391834, 391833, 391844, 391852, 391841, 391839, 391847

-

2.3.1.36

acetyl-CoA + D-leucine = CoA + N-acetyl-D-leucine

486807

-

2.3.1.36

propionyl-CoA + D-leucine = CoA + N-propionyl-D-leucine

486807

-

1.4.3.3

2 entries

2.3.1.36

2 entries

2.6.1.21

D-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + D-glutamate

759235, 759812

-

5.1.1.10

D-Leu = L-Leu

744003

-

Substrate in Enzyme-catalyzed Reactions (22 results)

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Show Substrate (22 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.3.1

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

742805

-

1.4.3.19

D-Leu + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2

655429

-

1.4.3.3

D-Leu + H2O + O2 = 4-methyl-2-oxopentanoate + NH3 + H2O2

743827, 655274, 654786, 741626, 741688

-

1.4.3.3

D-Leu + H2O + O2 = 4-methyl-2-oxopentanoic acid + NH3 + H2O2

724401

-

1.4.3.3

D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + NH3 + H2O2

763732

-

1.4.3.3

D-leucine + H2O + O2 = 4-methyl-2-oxopentanoic acid + NH3 + H2O2

391830, 391865, 391840, 391853, 391834, 391833, 391844, 391852, 687891, 391841, 391839, 391847, 686020, 684598, 685750, 724793

-

1.4.3.3

4 entries

1.4.5.1

D-leucine + oxidized acceptor + H2O = 4-methyl-2-oxopentanoate + NH3 + reduced acceptor

700217

-

1.4.99.6

D-leucine + H2O + 2,6-dichlorophenolindophenol = 4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichlorophenolindophenol

394974

-

1.4.99.6

D-leucine + H2O + methylene blue = 4-methyl-2-oxopentanoate + NH3 + reduced methylene blue

394974

-

1.4.99.6

D-leucine + phenazine methosulfate + H2O = 4-methyl-2-oxopentanoate + NH3 + reduced phenazine methosulfate

762668

-

1.4.99.6

D-leucine + phenazine methosulfate = ? + NH3 + reduced phenazine methosulfate

733215, 733326, 734025

-

1.4.99.6

4 entries

1.5.99.13

D-leucine + oxidized 2,6-dichloroindophenol + H2O = 4-methyl-2-oxopentanoate + NH3 + reduced 2,6-dichloroindophenol

684424, 394966

-

2.3.1.36

acetyl-CoA + D-leucine = CoA + N-acetyl-D-leucine

486807

-

2.3.1.36

propionyl-CoA + D-leucine = CoA + N-propionyl-D-leucine

486807

-

2.6.1.21

D-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + D-glutamate

759235, 759812, 636742

-

2.6.1.21

D-leucine + pyruvate = 4-methyl-2-oxopentanoate + D-alanine

759259

-

2.3.1.36

2 entries

2.6.1.21

2 entries

2.6.1.74

D-leucine + 2-oxoadipate = 4-methyl-2-oxopentanoate + 2-aminoadipate

640195

-

3.4.16.4

S2a + D-leucine = ?

670827

-

5.1.1.10

D-Leu = L-Leu

745414, 744003

-

5.1.1.10

D-leucine = L-leucine

744003, 745414

-

5.1.1.10

2 entries

5.1.1.21

D-leucine = L-leucine

729935

-

6.3.2.4

ATP + D-Leu = ADP + phosphate + D-Leu-D-Leu

672685

-

Product in Enzyme-catalyzed Reactions (35 results)

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Show Product (35 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.16

4-methyl-2-oxopentanoate + NH3 + NADPH + H+ = D-leucine + NADP+

0

3wgz, 3D-view

1.4.3.5

5'-phospho-pyridoxyl-D-leucine + H2O + O2 = pyridoxal 5'-phosphate + D-leucine + H2O2

391890

-

1.4.3.5

N-(5'-phospho-4'-pyridoxyl)-D-leucine + H2O + O2 = pyridoxal 5'-phosphate + D-leucine + H2O2

0

-

1.4.3.5

2 entries

1.4.99.6

2-oxo-4-methylvaleric acid + NH3 + NADPH + H+ = D-leucine + H2O + NADP+

0

-

2.6.1.B21

(R)-1-phenylethylamine + 2-oxoisocaproate = acetophenone + D-leucine

0

-

3.1.1.43

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

80934

-

3.4.13.17

D-Leu-D-Leu + H2O = D-Leu + D-Leu

81206

-

3.4.13.17

D-Leu-Gly-Gly + H2O = D-Leu + Gly-Gly

81206

-

3.4.13.17

D-Leu-Leu + H2O = D-Leu + Leu

81206

-

3.4.13.17

Gly-D-Leu + H2O = Gly + D-Leu

81206

-

3.4.13.17

Gly-Gly-D-Leu + H2O = Gly-Gly + D-Leu

81206

-

3.4.13.17

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

81206

-

3.4.13.17

6 entries

3.4.13.18

D-Leu-Gly + H2O = D-Leu + Gly

0

-

3.4.13.19

Gly-D-Leu + H2O = Gly + D-Leu

0

-

3.4.13.19

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

0

-

3.4.13.19

L-Met-D-Leu + H2O = L-Met + D-Leu

0

-

3.4.13.19

L-Tyr-D-Leu + H2O = L-Tyr + D-Leu

0

-

3.4.13.22

D-Leu-4-nitroanilide + H2O = D-Leu + 4-nitroaniline

0

-

3.4.13.22

D-leucine-p-nitroanilide + H2O = D-leucine + p-nitroaniline

0

-

3.4.13.19

4 entries

3.4.13.22

2 entries

3.4.16.4

glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-leucine + H2O = glycyl-L-alpha-amino-epsilon-pimelyl-D-alanine + D-leucine

0

-

3.4.19.3

pyroglutamyl-D-Leu + H2O = pyroglutamate + D-Leu

0

-

3.4.21.26

benzyloxycarbonyl-Gly-Pro-D-Leu + H2O = benzyloxycarbonyl-Gly-Pro + D-Leu

653873

-

3.4.22.40

Gly-D-Leu + H2O = Gly + D-Leu

0

-

3.5.1.77

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

0

-

3.5.1.81

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

0, 31912

-

3.5.1.81

N-Benzoyl-D-Leu + H2O = Benzoate + D-Leu

0

-

3.5.1.81

N-Benzyloxycarbonyl-D-Leu + H2O = Benzyloxycarbonate + D-Leu

0

-

3.5.1.81

N-Butyl-D-Leu + H2O = Butanoate + D-Leu

0

-

3.5.1.81

N-Formyl-D-Leu + H2O = Formate + D-Leu

0

-

3.5.1.81

N-Propionyl-D-Leu + H2O = Propanoate + D-Leu

0

-

3.5.1.81

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

0

-

3.5.1.81

7 entries

5.1.1.1

L-leucine = D-leucine

0

-

5.1.1.10

L-Leu = D-Leu

2040, 0

-

5.1.1.10

L-leucine = D-leucine

0

-

5.1.1.10

2 entries

5.1.1.21

L-leucine = D-leucine

0

-

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 20 mM

664626

-

3.4.13.9

activation of isoforms prolidase I and prolidase II

668271

-

Inhibitor in Enzyme-catalyzed Reactions (6 results)

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Show Inhibitors (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.4.1.20

10 mM, 17% inhibition

349634

-

1.4.1.20

10 mM, 31% inhibition

349634

-

1.4.1.20

2 entries

1.4.1.9

-

349665

-

2.3.3.6

weak

488179

-

3.4.11.1

-

95188

-

7.4.2.11

98% residual activity at 5 mM with L-methionine as substrate, 90% residual activity at 50 mM with D-methionine as substrate

749753

-

3D Structure of Enzyme-Ligand-Complex (PDB) (9 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (9 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.14.11.30

4jaa, 3D-view

1.4.1.16

3wgz, 3D-view

2.3.2.27

6kzu, 3D-view

2.3.2.27

7kjm, 3D-view

2.3.2.27

6kzu, 3D-view

2.3.2.27

7kjm, 3D-view

2.3.2.27

4 entries

3.4.21.91

7oc2, 3D-view

3.6.1.15

7oc2, 3D-view

3.6.4.13

7oc2, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (10 results)

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Show Turnover Number (10 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.1

0.7

-

mutant enzyme H56N, at pH 7.5 and 37°C

742805

1.4.3.3

24

-

at pH 8.0 and 60°C

741688

1.4.3.3

29.1

-

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

724401

1.4.3.3

46

-

mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

56

-

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

724401

1.4.3.3

66.6

-

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

724401

1.4.3.3

116

-

pH 8.0, 37°C

655274

1.4.99.6

0.061

-

wild-type, pH 6.0, 25°C

733215

1.4.99.6

6.4

-

pH 8.7, 25°C

733326, 762668

1.4.99.6

55

-

wild-type, pH 10.0, 25°C

733215

1.4.3.3

6 entries

1.4.99.6

3 entries

K_M Value (17 results)

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Show KM Value (17 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.1

8.8

-

mutant enzyme H56N, at pH 7.5 and 37°C

742805

1.4.3.3

0.049

-

at pH 8.0 and 60°C

741688

1.4.3.3

0.08

-

-

391847

1.4.3.3

0.227

-

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

724401

1.4.3.3

0.23

-

-

391865

1.4.3.3

0.28

-

-

391840, 391839

1.4.3.3

0.5

-

-

391833

1.4.3.3

0.78

-

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

724401

1.4.3.3

1.19

-

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

724401

1.4.3.3

1.81

-

mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

724401

1.4.3.3

6.5

-

pH 8.0, 37°C

655274

1.4.3.3

10.9

-

-

391853

1.4.99.6

1.8

-

wild-type, pH 6.0, 25°C

733215

1.4.99.6

4.6

-

wild-type, pH 10.0, 25°C

733215

1.4.99.6

12

-

pH 8.7, 25°C

733326, 762668

5.1.1.10

4.19

-

pH 7.0, 80°C

745414

5.1.1.10

4.19

-

pH 7.0, 80°C, recombinant enzyme

745414

1.4.3.3

11 entries

1.4.99.6

3 entries

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

2.2

-

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

2040

5788493

Crystalline amino acid racemase with low substrate specificity

1969

Soda, K.; Osumi, T.

Biochem. Biophys. Res. Commun.

35

363-368

31912

8541651

Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in Escherichia coli

1995

Wakayama, M.; Katsuno, Y.; Hayashi, S.; Miyamoto, Y.; Sakai, K.; Moriguchi, M.

Biosci. Biotechnol. Biochem.

59

2115-2119

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

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

95188

6432050

Isolation and characterization of an aminopeptidase from Lactobacillus acidophilus

1984

Machuga, E.J.; Ives, D.H.

Biochim. Biophys. Acta

789

26-36

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

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

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

391839

5908

Purification of D-amino oxidase from Trigonopsis variabilis

1976

Berg, C.P.; Rodden, F.A.

Anal. Biochem.

71

214-222

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

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

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

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

391890

4711161

N-(5-phospho-4-pyridoxyl)amines as substrates for pyridoxine (pyridoxamine) 5-phosphate oxidase

1973

Kazarinoff, M.N.; McCormick, D.B.

Biochem. Biophys. Res. Commun.

52

440-446

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

394974

-

D-Amino acid dehydrogenase (Pseudomonas fluorescens)

1971

Tsukada, K.

Methods Enzymol.

17B

623-624

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

488179

4320440

Metabolism of ethylmalic acids by Pseudomonas aeruginosa

1968

Rabin, R.; Salomon, I.I.; Bleiweis, A.S.; Carlin, J.; Ajl, S.J.

Biochem. J.

7

377-389

636742

1158891

D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties

1975

Yonaha, K.; Misono, H.; Yamamoto, T.; Soda, K.

J. Biol. Chem.

250

6983-6989

640195

3228235

Novel D-amino acid transaminase

1988

Aretz, W.; Sauber, K.

Ann. N. Y. Acad. Sci.

542

366-370

653873

-

Proline-specific endopeptidases

2003

Besedin, D.V.; Rudenskaya, G.N.

Russ. J. Bioorg. Chem.

29

1-17

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

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

670827

16199665

Specificity and reversibility of the transpeptidation reaction catalyzed by the Streptomyces R61 D-Ala-D-Ala peptidase

2005

Rhazi, N.; Delmarcelle, M.; Sauvage, E.; Jacquemotte, F.; Devriendt, K.; Tallon, V.; Ghosez, L.; Frere, J.M.

Protein Sci.

14

2922-2928

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

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

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

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

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

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724793

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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

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729935

24039265

Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species

2013

Mutaguchi, Y.; Ohmori, T.; Wakamatsu, T.; Doi, K.; Ohshima, T.

J. Bacteriol.

195

5207-5215

733215

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Importance of glutamate 87 and the substrate alpha-amine for the reaction catalyzed by D-arginine dehydrogenase

2015

Ball, J.; Bui, Q.V.; Gannavaram, S.; Gadda, G.

Arch. Biochem. Biophys.

568

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733326

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Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase

2010

Fu, G.; Yuan, H.; Li, C.; Lu, C.D.; Gadda, G.; Weber, I.T.

Biochemistry

49

8535-8545

734025

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Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects

2011

Yuan, H.; Xin, Y.; Hamelberg, D.; Gadda, G.

J. Am. Chem. Soc.

133

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741626

25900453

A novel D-amino acid oxidase from a contaminated agricultural soil metagenome and its characterization

2015

Ou, Q.; Liu, Y.; Deng, J.; Chen, G.; Yang, Y.; Shen, P.; Wu, B.; Jiang, C.

Antonie van Leeuwenhoek

107

1615-1623

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

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742805

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Possible role of a histidine residue in the substrate specificity of yeast D-aspartate oxidase

2016

Takahashi, S.; Shimada, K.; Nozawa, S.; Goto, M.; Abe, K.; Kera, Y.

J. Biochem.

159

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743827

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

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

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2994

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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

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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

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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.

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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.

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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.

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Molecular mechanism of stereospecificity toward D-leucine of the transaminase from Desulfohalobium retbaense revealed by molecular dynamic simulations

2020

Khrenova, M.; Zavyalova, S.; Bezsudnova, E.

Moscow Univ. Chem. Bull.

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762668

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Amine oxidation by D-arginine dehydrogenase in Pseudomonas aeruginosa

2017

Ouedraogo, D.; Ball, J.; Iyer, A.; Reis, R.A.G.; Vodovoz, M.; Gadda, G.

Arch. Biochem. Biophys.

632

192-201

763732

31420577

A novel thermostable D-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA

2019

Shimekake, Y.; Furuichi, T.; Abe, K.; Kera, Y.; Takahashi, S.

Sci. Rep.

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11948

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