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Ligand D-proline

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for D-proline

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.1

D-proline + NADH + H+ = 5-aminovalerate + NAD+

704292

-

1.21.4.1

D-proline + NADH = 5-aminopentanoic acid + NAD+

484930, 484931, 484934, 484929

-

1.21.4.1

2 entries

1.4.3.19

D-proline + H2O + O2 = ?

672771, 725913

-

1.4.3.3

D-Pro + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

743827, 743344

-

1.4.3.3

D-proline + H2O + O2 = 2-oxopentanoate + NH3 + H2O2

696158

-

1.4.3.3

D-proline + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

391828, 391838, 391849, 391860, 391853, 391834, 391833, 391844, 391852, 391861, 391841, 391864

-

1.4.3.3

3 entries

1.4.99.6

D-Pro + H2O + coenzyme Q1 = ?

695533

-

2.3.1.36

acetyl-CoA + D-proline = CoA + N-acetyl-D-proline

486807

-

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

5.1.1.4

L-Pro = D-Pro

0

-

5.1.1.4

L-proline = D-proline

0

-

5.1.1.4

2 entries

Substrate in Enzyme-catalyzed Reactions (41 results)

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Show Substrate (41 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.21.4.1

D-proline + 1,3-dimercaptopropanol = 5-aminopentanoic acid + ?

2121

-

1.21.4.1

D-proline + 6,8-dimercaptooctanoate = 5-aminopentanoic acid + ?

2121

-

1.21.4.1

D-proline + beta-mercaptoethanol = ?

2121

-

1.21.4.1

D-proline + dihydrolipoate = delta-aminovaleric acid + lipoate

2121

-

1.21.4.1

D-proline + dithiol (reduced) = 5-aminopentanoic acid + oxidized dithiol

484934, 2121, 484928, 484929

-

1.21.4.1

D-proline + dithiothreitol = 5-amino pentanoic acid + ?

484929, 484930, 484932, 484934, 484935

-

1.21.4.1

D-proline + DL-lipoic acid = 5-aminopentanoic acid + ?

2121

-

1.21.4.1

D-proline + NADH + H+ = 5-aminovalerate + NAD+

704292

-

1.21.4.1

D-proline + NADH = 5-aminopentanoic acid + NAD+

484930, 484931, 484934, 484929

-

1.4.3.1

D-Pro + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

742035

-

1.4.3.1

D-proline + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

391705, 391719, 391720, 391714

-

1.4.3.1

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

763008

-

1.4.3.1

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

762756

-

1.4.3.19

D-Pro + H2O + O2 = ? + H2O2

655429

-

1.4.3.19

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

440362, 701114, 440361, 698957

-

1.4.3.19

D-proline + H2O + O2 = ?

672771, 685414, 689934, 687878, 725913, 743136

-

1.4.3.19

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

764081

-

1.4.3.3

D-Pro + H2O + O2 = 2-oxopentanoate + NH3 + H2O2

673646, 677016, 674365, 655441, 655274

-

1.4.3.3

D-Pro + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

743827, 391705, 743344

-

1.4.3.3

D-proline + H2O + O2 = 2-oxopentanoate + NH3 + H2O2

696158, 763089, 763216, 657350, 686020, 686277, 724793

-

1.4.3.3

D-proline + H2O + O2 = 2-oxopentanoic acid + NH3 + H2O2

723920, 724965, 391828, 391838, 391849, 391860, 687145, 391853, 391834, 391833, 391844, 391852, 391861, 687891, 391841, 391864, 686020, 654786, 656415, 684598, 685750, 724793

-

1.4.5.1

D-proline + oxidized 2,6-dichloroindophenol = DELTA1-pyrroline-2-carboxylate + reduced 2,6-dichloroindophenol

394971

-

1.4.5.1

D-proline + oxidized 2,6-dichlorophenolindophenol = DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol

696481

-

1.4.5.1

D-proline + oxidized acceptor = DELTA1-pyrroline-2-carboxylate + reduced acceptor

700217

-

1.4.5.1

D-proline + oxidized coenzyme Q1 + H2O = DELTA1-pyrroline-2-carboxylate + NH3 + reduced coenzyme Q1

695533

-

1.4.99.6

D-Pro + H2O + coenzyme Q1 = ?

695533

-

1.4.99.6

D-Pro + H2O + oxidized 2,6-dichlorophenolindophenol = DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol

695533

-

1.4.99.6

D-proline + H2O + 2,6-dichlorophenolindophenol = DELTA1-pyrroline-2-carboxylate + NH3 + reduced 2,6-dichlorophenolindophenol

705545

-

1.4.99.6

D-proline + H2O + coenzyme Q1 = DELTA1-pyrroline-2-carboxylate + NH3 + reduced coenzyme Q1

705545

-

1.4.99.6

D-proline + H2O + FAD = 2-oxopentanoic acid + NH3 + FADH2

748083

-

1.4.99.6

D-proline + phenazine methosulfate + H2O = DELTA1-pyrroline-2-carboxylate + NH3 + reduced phenazine methosulfate

762668

-

1.4.99.B4

D-proline + acceptor + acceptor = ?

764324

-

1.4.99.B4

D-proline + acceptor = ?

748266

-

1.5.99.13

D-proline + 2,6-dichlorophenolindophenol = 1-pyrroline-2-carboxylate + reduced 2,6-dichlorophenolindophenol

394966

-

1.5.99.13

D-proline + oxidized 2,6-dichloroindophenol = DELTA1-pyrroline 2-carboxylate + reduced 2,6-dichloroindophenol

684424, 394966

-

1.5.99.13

D-proline + oxidized 2,6-dichlorophenolindophenol = DELTA1-pyrroline-2-carboxylate + reduced 2,6-dichlorophenolindophenol

695578

-

1.5.99.13

D-proline + oxidized 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide = DELTA1-pyrroline 2-carboxylate + reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

394966

-

1.5.99.13

D-proline + oxidized phenazine methosulfate = DELTA1-pyrroline 2-carboxylate + reduced phenazine methosulfate

394966

-

1.21.4.1

9 entries

1.4.3.1

4 entries

1.4.3.19

4 entries

1.4.3.3

4 entries

1.4.5.1

4 entries

1.4.99.6

6 entries

1.4.99.B4

2 entries

1.5.99.13

5 entries

2.3.1.36

acetyl-CoA + D-proline = CoA + N-acetyl-D-proline

486807

-

5.1.1.4

D-proline = L-proline

730678

-

6.3.2.4

ATP + D-Pro = ADP + phosphate + D-Pro-D-Pro

672685

-

Product in Enzyme-catalyzed Reactions (4 results)

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Show Product (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.3.1

N-methyl-D-proline + O2 + H2O = formaldehyde + D-proline + H2O2

0

-

5.1.1.1

L-proline = D-proline

0

-

5.1.1.4

L-Pro = D-Pro

2121, 2122, 2123, 2124, 2125, 2126, 2127, 2128, 2129, 2130, 2131, 0

-

5.1.1.4

L-proline = D-proline

0, 652377

-

5.1.1.4

2 entries

Inhibitor in Enzyme-catalyzed Reactions (3 results)

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Show Inhibitors (3 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.88

weak inhibitor

762677

6x99, 3D-view

1.4.3.3

-

763216

-

3.2.1.180

-

731656

-

3D Structure of Enzyme-Ligand-Complex (PDB) (28 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (28 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.2.1.88

6x99, 3D-view

1.5.1.12

2ej6, 3D-view

1.5.5.2

6x99, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.14

1h0g, 3D-view

3.2.1.14

1w9u, 3D-view

3.2.1.14

1waw, 3D-view

3.2.1.17

3oe0, 3D-view

3.2.1.17

4pjz, 3D-view

3.2.1.17

4pk0, 3D-view

3.2.1.17

3oe0, 3D-view

3.2.1.17

4pjz, 3D-view

3.2.1.17

4pk0, 3D-view

3.2.1.17

3oe0, 3D-view

3.2.1.17

4pjz, 3D-view

3.2.1.17

4pk0, 3D-view

3.4.23.46

5mbw, 3D-view

3.4.23.46

5mcq, 3D-view

3.4.23.46

5mbw, 3D-view

3.4.23.46

5mcq, 3D-view

3.4.23.46

5mbw, 3D-view

3.4.23.46

5mcq, 3D-view

3.2.1.14

9 entries

3.2.1.17

9 entries

3.4.23.46

6 entries

3.5.1.98

5efj, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (45 results)

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Show Turnover Number (45 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.4.3.1

1.2

-

wild-type, pH 8.3, 25°C

763008

1.4.3.1

5.5

-

pH 8.3, 25°C

762756

1.4.3.19

0.3

-

apparent value for mutant enzyme H244N, at 25°C and pH 8.5

685414

1.4.3.19

0.38

-

apparent value for mutant enzyme M261Y, at 25°C and pH 8.5

685414

1.4.3.19

0.5

-

apparent value for wild type enzyme, at 25°C and pH 8.5

685414

1.4.3.19

0.62

-

apparent value for mutant enzyme M261H, at 25°C and pH 8.5

685414

1.4.3.19

1.23

-

apparent value for mutant enzyme H244Q, at 25°C and pH 8.5

685414

1.4.3.19

1.3

-

-

440361

1.4.3.19

1.35

-

apparent value for mutant enzyme H244F, at 25°C and pH 8.5

685414

1.4.3.19

1.69

-

pH 8.2, 23°C

764081

1.4.3.19

3.5

-

-

440362

1.4.3.3

0.052

2.1

wild-type enzyme

674365

1.4.3.3

1.67

-

mutant enzymeY224G

674365

1.4.3.3

3.5

-

mutant enzyme G222D/Y224G

674365

1.4.3.3

3.83

-

mutant enzyme R221D/Y224G

674365

1.4.3.3

4.33

-

mutant enzyme E220D/Y224G

674365

1.4.3.3

9.7

-

mutant T317A

391854

1.4.3.3

10.2

-

pH 8.5, 25°C

673646

1.4.3.3

10.2

-

at pH 7.0 and 25°C

723920

1.4.3.3

10.33

-

wild-type enzyme

674365

1.4.3.3

11.7

-

mutant Y228F

391860

1.4.3.3

15

-

pH 8.3, 25°C

677016

1.4.3.3

21

-

wild-type

391854

1.4.3.3

26.57

-

wild-type, pH 8.0, 25°C

763216

1.4.3.3

29.53

-

mutant P219L, pH 8.0, 25°C

763216

1.4.3.3

43.3

-

at pH 8.5 and 37°C

743827

1.4.3.3

47

-

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

724965

1.4.3.3

50.2

-

at pH 7.5 and 37°C

743827

1.4.3.3

83.7

-

mutant Y224F

391860

1.4.3.3

87.2

-

wild-type

391860

1.4.3.3

107.3

-

at pH 8.0 and 37°C

743827

1.4.3.3

142

-

pH 8.0, 37°C

655274

1.4.3.3

1615

-

pH 8.5, 25°C, mutant enzyme M213R

391705

1.4.3.3

4640

-

pH 8.5, 25°C, wild-type enzyme

391705

1.4.3.1

2 entries

1.4.3.19

9 entries

1.4.3.3

23 entries

1.4.5.1

8.33

-

-

394971

1.4.99.6

0.97

-

pH 8.7, 37°C

748083

1.4.99.B4

1.12

-

pH 9.0, 30°C, acceptor: phenazine methosulfate/nitroblue tetrazolium

764324

1.4.99.B4

1.92

-

pH 9.0, 30°C, acceptor: phenazine methosulfate/p-iodonitrotetrazolium violet

764324

5.1.1.4

0.0235

-

pH 8.0, 50°C, mutant enzyme F62V

730678

5.1.1.4

0.026

-

pH 8.0, 50°C, mutant enzyme F62S

730678

5.1.1.4

0.119

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

0.29

-

pH 8.0, 50°C, mutant enzyme L221H

730678

5.1.1.4

2.22

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

2.48

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

3.18

-

pH 8.0, 50°C, mutant enzyme W241F

730678

1.4.99.B4

2 entries

5.1.1.4

7 entries

K_M Value (73 results)

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Show KM Value (73 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.4.3.1

0.9

-

-

391705

1.4.3.1

169

-

pH 8.3, 25°C

762756

1.4.3.1

339

-

wild-type, pH 8.3, 25°C

763008

1.4.3.1

440

-

-

391714

1.4.3.19

2.06

-

M261Y mutant

672771

1.4.3.19

3.91

-

M261H mutant

672771

1.4.3.19

7.9

-

mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C

687878

1.4.3.19

8.58

-

pH 8.2, 23°C

764081

1.4.3.19

8.9

-

M261 wild type

672771

1.4.3.19

8.9

-

wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C

687878

1.4.3.19

9.3

-

in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate, at pH 8.5 and 37°C

689934

1.4.3.19

9.3

-

pH 8.5, 37°C

701114

1.4.3.19

17

-

apparent value for wild type enzyme, at 25°C and pH 8.5

685414

1.4.3.19

26

-

apparent value for mutant enzyme H244F, at 25°C and pH 8.5

685414

1.4.3.19

26

-

apparent value for mutant enzyme H244N, at 25°C and pH 8.5

685414

1.4.3.19

27

-

apparent value for mutant enzyme H244Q, at 25°C and pH 8.5

685414

1.4.3.19

31.7

-

at pH 8.5 and 40°C

743136

1.4.3.19

46

-

-

440361

1.4.3.19

76.5

-

-

440362

1.4.3.19

280

-

apparent value for mutant enzyme M261H, at 25°C and pH 8.5

685414

1.4.3.19

285

-

apparent value for mutant enzyme M261Y, at 25°C and pH 8.5

685414

1.4.3.3

0.33

-

at pH 8.0 and 37°C

743827

1.4.3.3

0.38

-

at pH 7.5 and 37°C

743827

1.4.3.3

0.56

-

wild-type enzyme

674365

1.4.3.3

0.73

-

mutant P219L, pH 8.0, 25°C

763216

1.4.3.3

0.85

-

at pH 8.5 and 37°C

743827

1.4.3.3

1.1

-

wild-type

391854

1.4.3.3

1.13

-

pH 8.0, 37°C

655274

1.4.3.3

1.2

-

mutant T317A

391854

1.4.3.3

1.23

-

wild-type, pH 8.0, 25°C

763216

1.4.3.3

1.7

-

pH 8.3, 25°C

677016

1.4.3.3

1.7

-

-

391828

1.4.3.3

4.1

-

mutant enzyme E220D/Y224G

674365

1.4.3.3

5.6

-

immobilized wild type enzyme, at 25°C

687891

1.4.3.3

7.7

-

mutant enzyme R221D/Y224G

674365

1.4.3.3

8.5

-

pH 8.5, 25°C

673646

1.4.3.3

8.5

-

at pH 7.0 and 25°C

723920

1.4.3.3

9.1

-

mutant Y224F

391860

1.4.3.3

9.5

-

wild-type

391860

1.4.3.3

12.2

-

mutant Y228F

391860

1.4.3.3

12.3

-

pH 8.5, 25°C, mutant enzyme Y238S

655441

1.4.3.3

12.5

-

free wild type enzyme, at 25°C

687891

1.4.3.3

13.5

-

pH 8.5, 25°C, mutant enzyme Y238F

655441

1.4.3.3

15.5

-

38.3 kDa form

391861

1.4.3.3

21.47

-

-

391833

1.4.3.3

21.5

-

pH 8.5, 25°C, wild-type enzyme

391705, 655441

1.4.3.3

21.5

-

-

391861

1.4.3.3

86

-

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

724965

1.4.3.3

1280

-

pH 8.5, 25°C, mutant enzyme M213R

391705

1.4.5.1

40

-

with 2,6-dichlorophenolindophenol

394971

1.4.5.1

40.2

-

pH 8.0, 37°C

695533

1.4.99.6

0.0082

-

Vmax: 12.3 micromol/min/mg

705545

1.4.99.6

1.82

-

pH 8.7, 37°C

748083

1.4.99.6

40.2

-

with Q1 as the electron acceptor, in 50 mM sodium-phosphate buffer (pH 8.0), at 37°C

695533

1.4.99.6

40.2

-

Vmax: 25 micromol/min/mg

705545

1.4.99.B4

0.0224

-

pH 8.0, 30°C, AbLhpBEF protein

748266

1.4.99.B4

0.401

-

pH 9.0, 30°C, acceptor: phenazine methosulfate/nitroblue tetrazolium

764324

1.4.99.B4

0.942

-

pH 9.0, 30°C, acceptor: phenazine methosulfate/p-iodonitrotetrazolium violet

764324

1.5.99.13

0.83

-

carbon nanotube gel/D-Pro dehydrogenase electrode

695578

1.5.99.13

1.8

-

Ketjen Black/D-Pro dehydrogenase electrode

695578

1.5.99.13

4.2

-

pH 8.0, 50°C

394966

1.5.99.13

5.2

-

carbon powder/D-Pro dehydrogenase electrode

695578

1.5.99.13

7.9

-

-

684424

1.5.99.13

7.9

-

D-Pro dehydrogenase-only electrode

695578

5.1.1.4

0.092

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

0.156

-

pH 8.0, 50°C, mutant enzyme F62V

730678

5.1.1.4

0.194

-

pH 8.0, 50°C, mutant enzyme W241F

730678

5.1.1.4

0.612

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

1.17

-

pH 8.0, 50°C, wild-type enzyme

730678

5.1.1.4

2.54

-

pH 8.0, 50°C, mutant enzyme L221H

730678

5.1.1.4

3.8

-

-

2122

5.1.1.4

4

-

pH 8.0, 50°C, mutant enzyme F62S

730678

5.1.1.4

106

-

40 mM substrate in 0.2 M sodium acetate, for 30 min at 37°C

705596

1.4.3.1

4 entries

1.4.3.19

17 entries

1.4.3.3

28 entries

1.4.5.1

2 entries

1.4.99.6

4 entries

1.4.99.B4

3 entries

1.5.99.13

6 entries

5.1.1.4

9 entries

K_i Value (4 results)

top print hide

Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.2.1.88

1.5

-

competitive inhibition model, at pH 7.5, temperature not specified in the publication

762677

1.2.1.88

4.5

-

uncompetitive inhibition model, at pH 7.5, temperature not specified in the publication

762677

1.4.3.3

0.0009

-

mutant P219L, pH 8.0, 25°C

763216

1.4.3.3

0.0017

-

wild-type, pH 8.0, 25°C

763216

1.2.1.88

2 entries

1.4.3.3

2 entries

References & Links

Literature References (92)

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Show Reference (92 entries)

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Comp. Biochem. Physiol. B

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Structural basis for stereospecificity to D-amino acid of glycine oxidase from Bacillus cereus ATCC 14579

2020

Seok, J.; Kim, Y.J.; Kim, I.K.; Kim, K.J.

Biochem. Biophys. Res. Commun.

533

824-830

764324

29191113

Characterization of cis-4-hydroxy-D-proline dehydrogenase from Sinorhizobium meliloti

2018

Watanabe, S.; Morimoto, D.; Fukumori, F.; Watanabe, Y.

Biosci. Biotechnol. Biochem.

82

110-113

Links to other databases for D-proline

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ChEBI

PubChem