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  • Sum Formula
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  • InChIKey
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• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
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Ligand trypanothione

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for trypanothione

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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

4.4.1.5

trypanothione + 2 methylglyoxal = 5,5'-bi((R)-lactoyl)trypanothione

729176

-

4.4.1.5

trypanothione + methylglyoxal = (R)-S-lactoylglutathione

729177

-

4.4.1.5

trypanothione + methylglyoxal = 5,5'-bi((R)-lactoyl)trypanothione

729176, 729177

-

4.4.1.5

3 entries

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

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Show Natural Product (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.12

trypanothione disulfide + NADPH + H+ = trypanothione + NADP+

-

2wow, 3D-view

1.8.1.12

trypanothione disulfide + NADPH + H+ = trypanothione + NADP+

-

4adw, 3D-view

1.8.1.12

trypanothione disulfide + NADPH = trypanothione + NADP+

, 394785, 394789, 394791, 394797, 394792

2wow, 3D-view

1.8.1.12

trypanothione disulfide + NADPH = trypanothione + NADP+

, 394785, 394789, 394791, 394797, 394792

4adw, 3D-view

3.1.2.6

S-acetyltrypanothione + H2O = acetate + trypanothione

-

-

3.1.2.6

S-bis-lactoyltrypanothione + 2 H2O = 2 D-lactate + trypanothione

-

-

3.1.2.6

S-glycolyltrypanothione + H2O = glycolate + trypanothione

-

-

3.1.2.6

S-hydroxyglutaryltrypanothione + H2O = hydroxyglutarate + trypanothione + 2 H+

-

-

3.1.2.6

S-propionyltrypanothione + H2O = propionate + trypanothione + H+

-

-

6.3.1.9

2 glutathione + spermidine + 2 ATP = N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate

-

-

6.3.1.9

glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

glutathione + spermidine + 2 ATP = N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate

-

-

6.3.1.9

N1-glutathionylspermidine + glutathione + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

N8-glutathionylspermidine + glutathione + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

gamma-L-Glu-L-Cys-Gly + N1-(gamma-Glu-L-Cys-Gly)-spermidine + ATP = N1,N8-bis-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate

-

-

6.3.1.9

gamma-L-glutamyl-L-cysteinyl-glycine + N1-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ATP = N1,N8-bis-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate

650657, 652306

-

1.8.1.12

4 entries

3.1.2.6

5 entries

6.3.1.9

7 entries

Substrate in Enzyme-catalyzed Reactions (13 results)

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Show Substrate (13 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.12

trypanothione + 5,5'-dithiobis-(2-nitrobenzoic acid) = trypanothione disulfide + thionitrobenzoate

697339, 686809, 688813, 686095, 700087, 685553, 684759, 685567

2wow, 3D-view

1.8.1.12

trypanothione + 5,5'-dithiobis-(2-nitrobenzoic acid) = trypanothione disulfide + thionitrobenzoate

697339, 686809, 688813, 686095, 700087, 685553, 684759, 685567

4adw, 3D-view

1.8.1.12

trypanothione + NADP+ = trypanothione disulfide + NADPH + H+

697339, 685553, 686809, 688813, 686095, 672614, 688034, 684759, 690113, 684776

2wow, 3D-view

1.8.1.12

trypanothione + NADP+ = trypanothione disulfide + NADPH + H+

697339, 685553, 686809, 688813, 686095, 672614, 688034, 684759, 690113, 684776

4adw, 3D-view

1.8.1.12

4 entries

1.8.1.7

trypanothione + NADPH = reduced trypanothione + NADP+

663260, 394776

-

3.5.1.78

trypanothione + H2O = glutathione + glutathionylspermidine

693074, 649733

-

4.4.1.5

methylglyoxal + reduced trypanothione = S-D-lactoyltrypanothione

706992

-

4.4.1.5

methylglyoxal + trypanothione = S,S'-bis((R)-lactoyl)trypanothione

692049

-

4.4.1.5

trypanothione + 2 methylglyoxal = 5,5'-bi((R)-lactoyl)trypanothione

729176

-

4.4.1.5

trypanothione + methylglyoxal = (R)-S-lactoylglutathione

729177

-

4.4.1.5

trypanothione + methylglyoxal = 5,5'-bi((R)-lactoyl)trypanothione

729176, 729177

-

4.4.1.5

trypanothione + methylglyoxal = S,S'-bis((R)-lactoyl)trypanothione

678043, 663884, 681984, 692329

-

4.4.1.5

trypanothione + phenylglyoxal = S-mandoyltrypanothione

678043

-

4.4.1.5

7 entries

Product in Enzyme-catalyzed Reactions (34 results)

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Show Product (34 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.1.12

NADPH + trypanothione disulfide + H+ = trypanothione + NADP+

-

2wow, 3D-view

1.8.1.12

NADPH + trypanothione disulfide + H+ = trypanothione + NADP+

-

4adw, 3D-view

1.8.1.12

trypanothione disulfide + beta-thio-NADPH = trypanothione + beta-thio-NADP+

-

2wow, 3D-view

1.8.1.12

trypanothione disulfide + beta-thio-NADPH = trypanothione + beta-thio-NADP+

-

4adw, 3D-view

1.8.1.12

trypanothione disulfide + NADPH + H+ = trypanothione + NADP+

-

2wow, 3D-view

1.8.1.12

trypanothione disulfide + NADPH + H+ = trypanothione + NADP+

-

4adw, 3D-view

1.8.1.12

trypanothione disulfide + NADPH = trypanothione + NADP+

394778, , 394803, 394780, 394761, 394785, 394789, 394798, 394802, 394775, 394781, 394787, 394797, 394807, 394776, 394779, 394791, 394793, 394794, 394800, 394804, 394805, 394808, 394784, 394788, 394790, 394792, 394786, 394782, 394799

2wow, 3D-view

1.8.1.12

trypanothione disulfide + NADPH = trypanothione + NADP+

394778, , 394803, 394780, 394761, 394785, 394789, 394798, 394802, 394775, 394781, 394787, 394797, 394807, 394776, 394779, 394791, 394793, 394794, 394800, 394804, 394805, 394808, 394784, 394788, 394790, 394792, 394786, 394782, 394799

4adw, 3D-view

1.8.1.12

trypanothione disulfide + reduced 3-acetylpyridine adenine dinucleotide = trypanothione + oxidized 3-acetylpyridine adenine dinucleotide

-

2wow, 3D-view

1.8.1.12

trypanothione disulfide + reduced 3-acetylpyridine adenine dinucleotide = trypanothione + oxidized 3-acetylpyridine adenine dinucleotide

-

4adw, 3D-view

1.8.1.12

trypanothione disulfide + thio-NADPH + H+ = trypanothione + thio-NADP+

-

2wow, 3D-view

1.8.1.12

trypanothione disulfide + thio-NADPH + H+ = trypanothione + thio-NADP+

-

4adw, 3D-view

1.8.1.12

12 entries

1.8.1.7

trypanothione + NADPH = reduced trypanothione + NADP+

, 394776

-

3.1.2.6

bis-(lactoyl)trypanothione + H2O = D-lactate + trypanothione

-

-

3.1.2.6

bis-(lactoyl)trypanothione + H2O = trypanothione + D-lactate

652537

-

3.1.2.6

D-lactoyltrypanothione + H2O = D-lactate + trypanothione

-

-

3.1.2.6

mono-(lactoyl)trypanothione + H2O = D-lactate + trypanothione

-

-

3.1.2.6

mono-(lactoyl)trypanothione + H2O = trypanothione + D-lactate

652537

-

3.1.2.6

S-acetyltrypanothione + H2O = acetate + trypanothione

-

-

3.1.2.6

S-bis-lactoyltrypanothione + 2 H2O = 2 D-lactate + trypanothione

-

-

3.1.2.6

S-D-lactoyltrypanothione + H2O = D-lactate + trypanothione

-

-

3.1.2.6

S-glycolyltrypanothione + H2O = glycolate + trypanothione

-

-

3.1.2.6

S-hydroxyglutaryltrypanothione + H2O = hydroxyglutarate + trypanothione + 2 H+

-

-

3.1.2.6

S-propionyltrypanothione + H2O = propionate + trypanothione + H+

-

-

4.4.1.5

S-D-lactoyltrypanothione = methylglyoxal + reduced trypanothione

-

-

4.4.1.5

S-mandoyltrypanothione = phenylglyoxal + trypanothione

-

-

3.1.2.6

11 entries

4.4.1.5

2 entries

6.3.1.8

2 glutathione + spermidine + 2 ATP = N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate

-

-

6.3.1.9

2 glutathione + spermidine + 2 ATP = N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate

-

-

6.3.1.9

glutathione + glutathionylspermidine + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

glutathione + spermidine + 2 ATP = N1,N8-bis(glutathionyl)spermidine + 2 ADP + 2 phosphate

-

-

6.3.1.9

N1-glutathionylspermidine + glutathione + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

N8-glutathionylspermidine + glutathione + ATP = N1,N8-bis(glutathionyl)spermidine + ADP + phosphate

-

-

6.3.1.9

gamma-L-Glu-L-Cys-Gly + N1-(gamma-Glu-L-Cys-Gly)-spermidine + ATP = N1,N8-bis-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate

-

-

6.3.1.9

gamma-L-glutamyl-L-cysteinyl-glycine + N1-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ATP = N1,N8-bis-(gamma-L-glutamyl-L-cysteinyl-glycyl)-spermidine + ADP + phosphate

650657, 652306

-

6.3.1.9

7 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

6.3.1.8

-

964

-

6.3.1.9

competitive feedback inhibition

727951

-

3D Structure of Enzyme-Ligand-Complex (PDB) (12 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (12 entries)

EC NUMBER

ENZYME 3D STRUCTURE

1.6.4.2

4grt, 3D-view

1.6.4.8

1bzl, 3D-view

1.8.1.12

2wow, 3D-view

1.8.1.12

4adw, 3D-view

1.8.1.12

2wow, 3D-view

1.8.1.12

4adw, 3D-view

1.8.1.12

2wow, 3D-view

1.8.1.12

4adw, 3D-view

1.8.1.12

2wow, 3D-view

1.8.1.12

4adw, 3D-view

1.8.1.12

2wow, 3D-view

1.8.1.12

4adw, 3D-view

1.8.1.12

10 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (8 results)

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Show Turnover Number (8 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.8.1.7

0.16

-

pH 7.5

663260

1.8.1.7

20.8

-

recombinant glutathione-trypanothione reductase-like enzyme

394776

1.8.1.7

85

-

pH 7.5, mutant enzyme N21R

663260

1.8.1.7

101.7

-

pH 7.5, wild-type enzyme

663260

4.4.1.5

104

-

-

681984

4.4.1.5

265

-

with phenylglyoxal

678043

4.4.1.5

363

-

with methylglyoxal

678043

4.4.1.5

1070

-

-

681984

1.8.1.7

4 entries

4.4.1.5

4 entries

K_M Value (12 results)

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Show KM Value (12 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.8.1.7

0.21

-

pH 7.5, mutant enzyme A18E/N21W/R22N/N101D/K105D/R319A

663260

1.8.1.7

0.33

-

pH 7.5, mutant enzyme A18E/N21W/R22N/N101D/K105D

663260

1.8.1.7

0.5

-

recombinant glutathione-trypanothione reductase-like enzyme

394776

1.8.1.7

0.66

-

pH 7.5, mutant enzyme A18E/N21W/R22N

663260

1.8.1.7

2

-

pH 7.5, wild-type enzyme

663260

1.8.1.7

2.3

-

pH 7.5, mutant enzyme N101D/K105D

663260

1.8.1.7

4.58

-

pH 7.5, mutant enzyme N21R

663260

4.4.1.5

0.0284

-

recombinant enzyme, pH 7.2, room temperature

663884

4.4.1.5

0.071

-

-

681984

4.4.1.5

0.109

-

with methylglyoxal

678043

4.4.1.5

0.13

-

-

681984

4.4.1.5

0.207

-

with phenylglyoxal

678043

1.8.1.7

7 entries

4.4.1.5

5 entries

K_i Value (4 results)

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Show KI Value (4 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

6.3.1.9

0.223

-

recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with glutathione as substrate, versus spermidine

727951

6.3.1.9

0.228

-

recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with spermidine as substrate, versus spermidine

727951

6.3.1.9

0.346

-

recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with glutathione as substrate, versus glutathione

727951

6.3.1.9

0.377

-

recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with spermidine as substrate, versus glutathione

727951

6.3.1.9

4 entries

References & Links

Literature References (57)

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Show Reference (57 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

964

1304372

Purification of glutathionylspermidine and trypanothione synthetase from Crithidia fasciculata

1992

Smith, K.; Nadeau, K.; Bradley, M.; Walsh, C.; Fairlamb, A.H.

Protein Sci.

1

874-883

394761

8168518

Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals

1994

Cunningham, M.L.; Zvelebil, M.J.J.M.; Fairlamb, A.H.

Eur. J. Biochem.

221

285-295

394775

2666188

NADPH-dependent disulphide reductases

1989

Krauth-Siegel, R.L.; Jockers-Scheruebl, M.C.; Becker, K.; Schirmer, R.H.

Biochem. Soc. Trans.

17

315-317

394776

9174360

Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity

1997

Stoll, V.S.; Simpson, S.J.; Krauth-Siegel, R.L.; Walsh, C.T.; Pai, E.F.

Biochemistry

36

6437-6447

394778

9923598

Evidence for the co-existence of glutathione reductase and trypanothione reductase in the non-trypanosomatid Euglenozoa: Euglena gracilis Z

1999

Montrichard, F.; Le Guen, F.; Laval-Martin, D.L.; Davioud-Charvet, E.

FEBS Lett.

442

29-33

394779

9986706

Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies

1999

Gallwitz, H.; Bonse, S.; Martinez-Cruz, A.; Schlichting, I.; Schumacher, K.; Krauth-Siegel, R.L.

J. Med. Chem.

42

364-372

394780

-

Cloning by expression of a cDNA corresponding to Leishmania donovani trypanothione reductase

1989

Taylor, M.C.; Chapman, C.J.; Kelly, J.M.; Fairlamb, A.H.; Miles, M.A.

Biochem. Soc. Trans.

17

579-580

394781

2669965

Expression of Trypanosoma congolense trypanothione reductase in Escherichia coli: overproduction, purification, and characterization

1989

Sullivan, F.X.; Shames, S.L.; Walsh, C.T.

Biochemistry

28

4986-4992

394782

2704738

Trypanothione is the primary target for arsenical drugs against African trypanosomes

1989

Fairlamb, A.H.; Henderson, G.B.; Cerami, A.

Proc. Natl. Acad. Sci. USA

86

2607-2611

394784

2647489

Trypanothione reductase from Trypanosoma cruzi. Catalytic properties of the enzyme and inhibition studies with trypanocidal compounds

1989

Jockers-Scheruebl, M.C.; Schirmer, R.H.; Krauth-Siegel, R.L.

Eur. J. Biochem.

180

267-272

394785

3135548

Subversive substrates for the enzyme trypanothione disulfide reductase: alternative approach to chemotherapy of Chagas disease

1988

Henderson, G.B.; Ulrich, P.; Fairlamb, A.H.; Rosenberg, I.; Pereira, M.; Sela, M.; Cerami, A.

Proc. Natl. Acad. Sci. USA

85

5374-5378

394786

3167026

Trypanothione reductase of Trypanosoma congolense: gene isolation, primary sequence determination, and comparison to glutathione reductase

1988

Shames, S.L.; Kimmel, B.E.; Peoples, O.P.; Agabian, N.; Walsh, C.T.

Biochemistry

27

5014-5019

394787

3607007

Substrate specificity of the flavoprotein trypanothione disulfide reductase from Crithidia fasciculata

1987

Henderson, G.B.; Fairlamb, A.H.; Ulrich, P.; Cerami, A.

Biochemistry

26

3023-3027

394788

3549299

Trypanothione reductase from Trypanosoma cruzi. Purification and characterization of the crystalline enzyme

1987

Krauth-Siegel, R.L.; Enders, B.; Henderson, G.B.; Fairlamb, A.H.; Schirmer, R.H.

Eur. J. Biochem.

164

123-128

394789

3718941

Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases

1986

Shames, S.L.; Fairlamb, A.H.; Cerami, A.; Walsh, C.T.

Biochemistry

25

3519-3526

394790

11073664

Inhibition of trypanothione reductase by substrate analogues

2000

Garrard, E.A.; Borman, E.C.; Cook, B.N.; Pike, E.J.; Alberg, D.G.

Org. Lett.

2

3639-3642

394791

10571254

Nitrofuran drugs as common subversive substrates of Trypanosoma cruzi lipoamide dehydrogenase and trypanothione reductase

1999

Blumenstiel, K.; Schoneck, R.; Yardley, V.; Croft, S.L.; Krauth-Siegel, R.L.

Biochem. Pharmacol.

58

1791-1799

394792

7548022

Catalytic and potentiometric characterization of E201D and E201Q mutants of Trypanosoma congolense trypanothione reductase

1995

Zheng, R.; Cenas, N.; Blanchard, J.S.

Biochemistry

34

12697-12703

394793

10368274

Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors

1999

Bond, C.S.; Zhang, Y.; Berriman, M.; Cunningham, M.L.; Fairlamb, A.H.; Hunter, W.N.

Structure

7

81-89

394794

10036154

Synthesis of 5,5'-dithiobis(2-nitrobenzamides) as alternative substrates for trypanothione reductase and thioredoxin reductase: a microtiter colorimetric assay for inhibitor screening

1999

Davioud-Charvet, E.; Becker, K.; Landry, V.; Gromer, S.; Loge, C.; Sergheraert, C.

Anal. Biochem.

268

1-8

394797

8243474

Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase. Sensitivity towards agents that are thought to induce oxidative stress

1993

Kelly, J.M.; Taylor, M.C.; Smith, K.; Hunter, K.J.; Fairlamb, A.H.

Eur. J. Biochem.

218

29-37

394798

-

Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase

1995

Ponasik, J.A.; Strickland, C.; Faerman, C.; Savvides, S.; Karplus, P.A.; Ganem, B.

Biochem. J.

311

371-375

394799

7607216

Trypanothione reductase from Leishmania donovani. Purification, characterization and inhibition by trivalent antimonials

1995

Cunningham, M.L.; Fairlamb, A.H.

Eur. J. Biochem.

230

460-468

394800

7737173

Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase

1995

Borges, A.; Cunningham, M.L.; Tovar, J.; Fairlamb, A.H.

Eur. J. Biochem.

228

745-752

394802

8105896

The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzyme kinetic properties of.gamma-glutamyl-modified substrate analogs

1993

El-Waer, A.F.; Smith, K.; McKie, J.H.; Benson, T.; Fairlamb, A.H.; Douglas, K.T.

Biochim. Biophys. Acta

1203

93-98

394803

11170645

2- And 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity

2001

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Discovery of 2-iminobenzimidazoles as a new class of trypanothione reductase inhibitor by high-throughput screening

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Cloning and expression of trypanothione reductase from a New World Leishmania species

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Inhibition of trypanothione reductase and glutathione reductase by ferrocenic 4-aminoquinoline ureas

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The use of natural product scaffolds as leads in the search for trypanothione reductase inhibitors

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Betraying the parasites redox system: diaryl sulfide-based inhibitors of trypanothione reductase: subversive substrates and antitrypanosomal properties

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Altenusin, a biphenyl isolated from the endophytic fungus Alternaria sp., inhibits trypanothione reductase from Trypanosoma cruzi

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Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities

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Synthesis and evaluation of 1-(1-(benzo[b]thiophen-2-yl)cyclohexyl)piperidine (BTCP) analogues as inhibitors of trypanothione reductase

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Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of glyoxalase I from Leishmania infantum

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Barata, L.; Sousa Silva, M.; Schuldt, L.; da Costa, G.; Tomas, A.M.; Ferreira, A.E.; Weiss, M.S.; Ponces Freire, A.; Cordeiro, C.

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