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Journal articles on the topic 'Trypanothion reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Tchokouaha Yamthe, Lauve Rachel, Trudy Janice Philips, Dorcas Osei-Safo, et al. "Antileishmanial effects of Sargassum vulgare products and prediction of trypanothione reductase inhibition by fucosterol." Future Drug Discovery 2, no. 3 (2020): FDD41. http://dx.doi.org/10.4155/fdd-2020-0002.

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Aim: To investigate the antileishmanial potency of Sargassum vulgare C. Agardh-derived products and the in silico inhibition of trypanothione reductase by fucosterol. Materials & methods: Sargassum vulgare crude extract and its derived fractions, subfractions and fucosterol were screened against Leishmania major and Leishmania donovani using the MTS and trypanothione reductase colorimetric assays. Macrophages viability was evaluated using the resazurin assay. The inhibition of trypanothione reductase by fucosterol was predicted in silico. Results: The crude extract, fractions 2, 4 and 7, s

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2

Ribeiro, Frederico F., Francisco J. B. M. Junior, Marcelo S. da Silva, Marcus Tullius Scotti, and Luciana Scotti. "Computational and Investigative Study of Flavonoids Active against Trypanosoma cruzi and Leishmania spp." Natural Product Communications 10, no. 6 (2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000630.

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Flavonoid compounds active against Trypanosoma cruzi and Leishmania species were submitted to several methodologies in silico: docking with the enzymes cruzain and trypanothione reductase (from T. cruzi), and N-myristoyltransferase, dihydroorotate dehydrogenase, and trypanothiona reductase (from Leishmania spp). Molecular maps of the complexes and the ligands were calculated. In order to compare and evaluate the antioxidant activity of the flavonoids with their antiprotozoal activity, quantum parameters were calculated. Considering the energies, interactions, and hydrophobic surfaces calculate

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3

MURGOLO, NICHOLAS J., ANTHONY CERAMI, and GRAEME B. HENDERSON. "Trypanothione Reductase." Annals of the New York Academy of Sciences 569, no. 1 Biomedical Sc (1989): 193–200. http://dx.doi.org/10.1111/j.1749-6632.1989.tb27369.x.

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4

Benson, T. J., J. H. McKie, J. Garforth, A. Borges, A. H. Fairlamb, and K. T. Douglas. "Rationally designed selective inhibitors of trypanothione reductase. Phenothiazines and related tricyclics as lead structures." Biochemical Journal 286, no. 1 (1992): 9–11. http://dx.doi.org/10.1042/bj2860009.

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Trypanothione reductase, an essential component of the anti-oxidant defences of parasitic trypanosomes and Leishmania, differs markedly from the equivalent host enzyme, glutathione reductase, in the binding site for the disulphide substrate. Molecular modelling of this region suggested that certain tricyclic compounds might bind selectively to trypanothione reductase without inhibiting host glutathione reductase. This was confirmed by testing 30 phenothiazine and tricyclic antidepressants, of which clomipramine was found to be the most potent, with a K(i) of 6 microM, competitive with respect

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5

Marsh, Ian R., and Mark Bradley. "Substrate Specificity of Trypanothione Reductase." European Journal of Biochemistry 243, no. 3 (1997): 690–94. http://dx.doi.org/10.1111/j.1432-1033.1997.00690.x.

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6

Hunter, William N., Susan Bailey, Jarjis Habash, et al. "Active site of trypanothione reductase." Journal of Molecular Biology 227, no. 1 (1992): 322–33. http://dx.doi.org/10.1016/0022-2836(92)90701-k.

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7

Smith, K., A. Borges, M. R. Ariyanayagam, and A. H. Fairlamb. "Glutathionylspermidine metabolism in Escherichia coli." Biochemical Journal 312, no. 2 (1995): 465–69. http://dx.doi.org/10.1042/bj3120465.

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Intracellular levels of glutathione and glutathionylspermidine conjugates have been measured throughout the growth phases of Escherichia coli. Glutathionylspermidine was present in mid-log-phase cells, and under stationary and anaerobic growth conditions accounted for 80% of the total glutathione content. N1,N8-bis(glutathionyl)spermidine (trypanothione) was undetectable under all growth conditions. The catalytic constant kcat/Km of recombinant E. coli glutathione reductase for glutathionylspermidine disulphide was approx. 11,000-fold lower than that for glutathione disulphide. The much higher

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8

Dukhyil, Abdul Aziz A. Bin. "Targeting Trypanothione Reductase of Leishmanial major to Fight Against Cutaneous Leishmaniasis." Infectious Disorders - Drug Targets 19, no. 4 (2019): 388–93. http://dx.doi.org/10.2174/1871526518666180502141849.

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Background: 1.2-2.0 million cases of leishmaniasis occur annually throughout the world. The available drugs like Amphotericin B, antimonials and miltefosine are unable to fulfill the need due to less effectiveness, high toxicity, resistance, high cost and complex route of administration. Leishmania survives inside the macrophages through different evasion mechanisms; one of that is activation of its trypanothione reductase enzyme which neutralizes the reactive oxygen species generated inside the macrophages to kill the parasites. This enzyme is unique and absent in human, therefore in this stu

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9

Zhang, Y., S. Bailey, A. H. Fairlamb, and W. N. Hunter. "Structure of trypanothione reductase fromTrypanosoma cruzi." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (1993): c83. http://dx.doi.org/10.1107/s0108767378097627.

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10

Mezianecherif, D., M. Aumercier, I. Kora, et al. "Trypanosoma cruzi: Immunolocalization of Trypanothione Reductase." Experimental Parasitology 79, no. 4 (1994): 536–41. http://dx.doi.org/10.1006/expr.1994.1114.

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11

Ariyanayagam, Mark R., Sandra L. Oza, Maria Lucia S. Guther, and Alan H. Fairlamb. "Phenotypic analysis of trypanothione synthetase knockdown in the African trypanosome." Biochemical Journal 391, no. 2 (2005): 425–32. http://dx.doi.org/10.1042/bj20050911.

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Trypanothione plays a pivotal role in defence against chemical and oxidant stress, thiol redox homoeostasis, ribonucleotide metabolism and drug resistance in parasitic kinetoplastids. In Trypanosoma brucei, trypanothione is synthesized from glutathione and spermidine by a single enzyme, TryS (trypanothione synthetase), with glutathionylspermidine as an intermediate. To examine the physiological roles of trypanothione, tetracycline-inducible RNA interference was used to reduce expression of TRYS. Following induction, TryS protein was reduced >10-fold and growth rate was reduced 2-fold, with

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12

Čėnas, Narimantas, Aušra Nemeikaitė-Čėnienė, and Lidija Kosychova. "Single- and Two-Electron Reduction of Nitroaromatic Compounds by Flavoenzymes: Mechanisms and Implications for Cytotoxicity." International Journal of Molecular Sciences 22, no. 16 (2021): 8534. http://dx.doi.org/10.3390/ijms22168534.

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Nitroaromatic compounds (ArNO2) maintain their importance in relation to industrial processes, environmental pollution, and pharmaceutical application. The manifestation of toxicity/therapeutic action of nitroaromatics may involve their single- or two-electron reduction performed by various flavoenzymes and/or their physiological redox partners, metalloproteins. The pivotal and still incompletely resolved questions in this area are the identification and characterization of the specific enzymes that are involved in the bioreduction of ArNO2 and the establishment of their contribution to cytoto

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13

Ondarza, Raúl N., Gerardo Hurtado, Elsa Tamayo, Angélica Iturbe, and Eva Hernández. "Naegleria fowleri: A free-living highly pathogenic amoeba contains trypanothione/trypanothione reductase and glutathione/glutathione reductase systems." Experimental Parasitology 114, no. 3 (2006): 141–46. http://dx.doi.org/10.1016/j.exppara.2006.03.001.

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14

MOUTIEZ, Mireille, Eric QUÉMÉNEUR, Christian SERGHERAERT, Valérie LUCAS, André TARTAR, and Elisabeth DAVIOUD-CHARVET. "Glutathione-dependent activities of Trypanosoma cruzi p52 makes it a new member of the thiol:disulphide oxidoreductase family." Biochemical Journal 322, no. 1 (1997): 43–48. http://dx.doi.org/10.1042/bj3220043.

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Trypanothione:glutathione disulphide thioltransferase of Trypanosoma cruzi (p52) is a key enzyme in the regulation of the intracellular thiolŐdisulphide redox balance by reducing glutathione disulphide. Here we show that p52, like other disulphide oxidoreductases possessing the CXXC active site motif, catalyses the reduction of low-molecular-mass disulphides (hydroxyethyldisulphide) as well as protein disulphides (insulin). However, p52 seems to be a poor oxidase under physiological conditions as evidenced by its very low rate for oxidative renaturation of reduced ribonuclease A. Like thioltra

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15

Lu, Jun, Suman K. Vodnala, Anna-Lena Gustavsson, et al. "Ebsulfur Is a Benzisothiazolone Cytocidal Inhibitor Targeting the Trypanothione Reductase of Trypanosoma brucei." Journal of Biological Chemistry 288, no. 38 (2013): 27456–68. http://dx.doi.org/10.1074/jbc.m113.495101.

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Trypanosoma brucei is the causing agent of African trypanosomiasis. These parasites possess a unique thiol redox system required for DNA synthesis and defense against oxidative stress. It includes trypanothione and trypanothione reductase (TryR) instead of the thioredoxin and glutaredoxin systems of mammalian hosts. Here, we show that the benzisothiazolone compound ebsulfur (EbS), a sulfur analogue of ebselen, is a potent inhibitor of T. brucei growth with a favorable selectivity index over mammalian cells. EbS inhibited the TryR activity and decreased non-protein thiol levels in cultured para

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16

Hunter, W. N., M. S. Alphey, C. S. Bond, and A. W. Schüttelkopf. "Targeting metabolic pathways in microbial pathogens: oxidative stress and anti-folate drug resistance in trypanosomatids." Biochemical Society Transactions 31, no. 3 (2003): 607–10. http://dx.doi.org/10.1042/bst0310607.

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The large quantity of genomic, biochemical and metabolic data on microbial pathogens provides information that helps us to select biological problems of interest and to identify targets, metabolic pathways or constituent enzymes, for therapeutic intervention. One area of potential use in developing novel anti-parasitic agents concerns the regulation of oxidative stress, and we have targeted the trypanothione peroxidase pathway in this respect. In order to characterize this pathway, we have determined crystal structures for each of its components, and are now studying enzyme–ligand complexes of

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17

Hunter, William N., Keith Smith, Zygmunt Derewenda, et al. "Initiating a crystallographic study of trypanothione reductase." Journal of Molecular Biology 216, no. 2 (1990): 235–37. http://dx.doi.org/10.1016/s0022-2836(05)80314-6.

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18

TAYLOR, M. C., J. M. KELLY, A. H. FAIRLAMB, and M. A. MILES. "The trypanothione reductase gene of Leishmania donovani." Biochemical Society Transactions 18, no. 5 (1990): 869–70. http://dx.doi.org/10.1042/bst0180869.

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19

EL-WAER, ABDUSSALAM F., TIMOTHY BENSON, and KENNETH T. DOUGLAS. "Synthesis of substrate analogues for trypanothione reductase." International Journal of Peptide and Protein Research 41, no. 2 (2009): 141–46. http://dx.doi.org/10.1111/j.1399-3011.1993.tb00124.x.

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20

Aumercier, M., D. Mezianecherif, M. Moutiez, A. Tartar, and C. Sergheraert. "A Microplate Assay for Trypanothione Reductase Inhibitors." Analytical Biochemistry 223, no. 1 (1994): 161–64. http://dx.doi.org/10.1006/abio.1994.1563.

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21

Garrard, Elizabeth A., Emily C. Borman, Brian N. Cook, Emily J. Pike, and David G. Alberg. "Inhibition of Trypanothione Reductase by Substrate Analogues." Organic Letters 2, no. 23 (2000): 3639–42. http://dx.doi.org/10.1021/ol0065423.

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22

Moutiez, M., M. Aumercier, R. Schöneck, et al. "Purification and characterization of a trypanothione-glutathione thioltransferase from Trypanosoma cruzi." Biochemical Journal 310, no. 2 (1995): 433–37. http://dx.doi.org/10.1042/bj3100433.

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Although trypanothione [T(S)2] is the major thiol component in trypanosomatidae, significant amounts of glutathione are present in Trypanosoma cruzi. This could be explained by the existence of enzymes using glutathione or both glutathione and T(S)2 as cofactors. To assess these hypotheses, a cytosolic fraction of T. cruzi epimastigotes was subjected to affinity chromatography columns using as ligands either S-hexylglutathione or a non-reducible analogue of trypanothione disulphide. A similar protein of 52 kDa was eluted in both cases. Its partial amino acid sequence indicated that it was iden

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23

Ponasik, J. A., C. Strickland, C. Faerman, S. Savvides, P. A. Karplus, and B. Ganem. "Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase." Biochemical Journal 311, no. 2 (1995): 371–75. http://dx.doi.org/10.1042/bj3110371.

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The enzyme trypanothione reductase (TR), together with its substrate, the glutathione-spermidine conjugate trypanothione, plays an essential role in protecting parasitic trypanosomatids against oxidative stress and is a target for drug design. Here we show that a naturally occurring spermine derivative, the antihypertensive agent kukoamine A [N1N12-bis(dihydrocaffeoyl)-spermine] inhibits TR as a mixed inhibitor (Ki = 1.8 microM, Kii = 13 microM). Kukoamine shows no significant inhibition of human glutathione reductase (Ki > 10 mM) and thus provides a novel selective drug lead. The correspon

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24

Lenz, Krauth-Siegel, and Schmidt. "Natural Sesquiterpene Lactones of the 4,15-iso-Atriplicolide Type are Inhibitors of Trypanothione Reductase." Molecules 24, no. 20 (2019): 3737. http://dx.doi.org/10.3390/molecules24203737.

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In the course of our investigations on the antitrypanosomal potential of sesquiterpene lactones (STL), we have recently reported on the exceptionally strong activity of 4,15-iso-Atriplicolide tiglate, which demonstrated an IC50 value of 15 nM against Trypanosoma brucei rhodesiense, the etiologic agent responsible for East African human trypanosomiasis (HAT). Since STLs are known to often interact with their biological targets (e.g., in anti-inflammatory and anti-tumor activity) by means of the covalent modification of biological nucleophiles—most prominently free cysteine thiol groups in prote

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25

Fournet, Alain, Alba Inchausti, Gloria Yaluff, et al. "Trypanocidal Bisbenzylisoquinoline Alkaloids are Inhibitors of Trypanothione Reductase." Journal of Enzyme Inhibition 13, no. 1 (1998): 1–9. http://dx.doi.org/10.3109/14756369809035823.

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26

Oliveira, Renata B. de, Aline BM Vaz, Rosana O. Alves, et al. "Arylfurans as potential Trypanosoma cruzi trypanothione reductase inhibitors." Memórias do Instituto Oswaldo Cruz 101, no. 2 (2006): 169–73. http://dx.doi.org/10.1590/s0074-02762006000200009.

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27

Dormeyer, Matthias, Nina Reckenfelderbäumer, Heike Lüdemann, and R. Luise Krauth-Siegel. "Trypanothione-dependent Synthesis of Deoxyribonucleotides byTrypanosoma bruceiRibonucleotide Reductase." Journal of Biological Chemistry 276, no. 14 (2001): 10602–6. http://dx.doi.org/10.1074/jbc.m010352200.

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28

Singh, Bishal K., Nandini Sarkar, M. V. Jagannadham, and Vikash K. Dubey. "Modeled structure of trypanothione reductase of Leishmania infantum." BMB Reports 41, no. 6 (2008): 444–47. http://dx.doi.org/10.5483/bmbrep.2008.41.6.444.

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29

CHAN, CECIL, HONG YIN, JACQUI GARFORTH, et al. "Inhibitors of trypanothione reductase as potential antitrypanosomal drugs." Biochemical Society Transactions 23, no. 4 (1995): 511S. http://dx.doi.org/10.1042/bst023511s.

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30

ENTRALA, E., C. MASCARO, and J. BARRETT. "Anti-oxidant enzymes in Cryptosporidium parvum oocysts." Parasitology 114, no. 1 (1997): 13–17. http://dx.doi.org/10.1017/s0031182096008037.

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Oocysts of Cryptosporidium parvum showed relatively low levels of SOD activity. The SOD which had a pI of 4.8 and an approximate molecular weight of 35 kDa appeared to be iron dependent. Catalase, glutathione transferase, glutathione reductase and glutathione peroxidase activity could not be detected, nor could trypanothione reductase. No NADH or NADPH oxidase activity could be detected, nor could peroxidase activity be demonstrated using o-dianisidine, guaiacol, NADPH or NADH as co-substrates. However, an NADPH-dependent H2O2 scavenging system was detected in the insoluble fraction.

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31

Blackie, Margaret A. L., Ahilan Saravanamuthu, Alan H. Fairlamb, and Kelly Chibale. "Inhibition of trypanothione reductase and glutathione reductase by ferrocenic 4-aminoquinoline ureas." Arkivoc 2008, no. 6 (2008): 52–60. http://dx.doi.org/10.3998/ark.5550190.0009.605.

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32

Bradley, Mark, Uwe S. Buecheler, and Christopher T. Walsh. "Redox enzyme engineering: conversion of human glutathione reductase into a trypanothione reductase." Biochemistry 30, no. 25 (1991): 6124–27. http://dx.doi.org/10.1021/bi00239a006.

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33

Iribarne, Federico, Margot Paulino, Sara Aguilera, Miguel Murphy, and Orlando Tapia. "Docking and molecular dynamics studies at trypanothione reductase and glutathione reductase active sites." Journal of Molecular Modeling 8, no. 5 (2002): 173–83. http://dx.doi.org/10.1007/s00894-002-0082-0.

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34

CUNNINGHAM, Mark L., Marketa J. J. M. ZVELEBIL, and Alan H. FAIRLAMB. "Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenicals." European Journal of Biochemistry 221, no. 1 (1994): 285–95. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18740.x.

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35

Kliukiené, Regina, Audrone Maroziené, Narimantas Cénas, Katja Becker, and John S. Blanchard. "Photoinactivation of Trypanothione Reductase and Glutathione Reductase by A1-Phthalocyanine Tetrasulfonate and Hematoporphyrin." Biochemical and Biophysical Research Communications 218, no. 2 (1996): 629–32. http://dx.doi.org/10.1006/bbrc.1996.0111.

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36

Faerman, Carlos H., Savvas N. Savvides, Corey Strickland, et al. "Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors." Bioorganic & Medicinal Chemistry 4, no. 8 (1996): 1247–53. http://dx.doi.org/10.1016/0968-0896(96)00120-4.

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37

Chitkul, Bordin, and Mark Bradley. "Optimising inhibitors of Trypanothione reductase using solid-phase chemistry." Bioorganic & Medicinal Chemistry Letters 10, no. 20 (2000): 2367–69. http://dx.doi.org/10.1016/s0960-894x(00)00471-6.

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38

Kuriyan, John, Lim Wong, Brian D. Guenther, Nicholas J. Murgolo, Anthony Cerami, and Graeme B. Henderson. "Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata." Journal of Molecular Biology 215, no. 3 (1990): 335–37. http://dx.doi.org/10.1016/s0022-2836(05)80353-5.

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39

Matadamas-Martínez, Félix, Alicia Hernández-Campos, Alfredo Téllez-Valencia, et al. "Leishmania mexicana Trypanothione Reductase Inhibitors: Computational and Biological Studies." Molecules 24, no. 18 (2019): 3216. http://dx.doi.org/10.3390/molecules24183216.

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Leishmanicidal drugs have many side effects, and drug resistance to all of them has been documented. Therefore, the development of new drugs and the identification of novel therapeutic targets are urgently needed. Leishmania mexicana trypanothione reductase (LmTR), a NADPH-dependent flavoprotein oxidoreductase important to thiol metabolism, is essential for parasite viability. Its absence in the mammalian host makes this enzyme an attractive target for the development of new anti-Leishmania drugs. Herein, a tridimensional model of LmTR was constructed and the molecular docking of 20 molecules

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40

Ortalli, Margherita, Andrea Ilari, Gianni Colotti, et al. "Identification of chalcone-based antileishmanial agents targeting trypanothione reductase." European Journal of Medicinal Chemistry 152 (May 2018): 527–41. http://dx.doi.org/10.1016/j.ejmech.2018.04.057.

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41

Fernandez-Gomez, R. "2-Amino diphenylsulfides as new inhibitors of trypanothione reductase." International Journal of Antimicrobial Agents 6, no. 2 (1995): 111–18. http://dx.doi.org/10.1016/0924-8579(95)00029-x.

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42

Moreno, Silvia N. J., Eva G. S. Carnieri, and Roberto Docampo. "Inhibition of Trypanosoma cruzi trypanothione reductase by crystal violet." Molecular and Biochemical Parasitology 67, no. 2 (1994): 313–20. http://dx.doi.org/10.1016/0166-6851(94)00140-5.

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43

Krauth-Siegel, R. Luise, and Oliver Inhoff. "Parasite-specific trypanothione reductase as a drug target molecule." Parasitology Research 90 (June 1, 2003): S77—S85. http://dx.doi.org/10.1007/s00436-002-0771-8.

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44

WILKINSON, Shane R., David J. MEYER, and John M. KELLY. "Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity." Biochemical Journal 352, no. 3 (2000): 755–61. http://dx.doi.org/10.1042/bj3520755.

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In most eukaryotes, glutathione-dependent peroxidases play a key role in the metabolism of peroxides. Numerous studies have reported that trypanosomatids lack this activity. Here we show that this is not the case, at least for the American trypanosome Trypanosoma cruzi. We have isolated a single-copy gene from T. cruzi with the potential to encode an 18kDa enzyme, the sequence of which has highest similarity with glutathione peroxidases from plants. A recombinant form of the protein was purified following expression in Escherichia coli. The enzyme was shown to have peroxidase activity in the p

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45

Iribarne, F., M. González, H. Cerecetto, S. Aguilera, O. Tapia, and M. Paulino. "Interaction energies of nitrofurans with trypanothione reductase and glutathione reductase studied by molecular docking." Journal of Molecular Structure: THEOCHEM 818, no. 1-3 (2007): 7–22. http://dx.doi.org/10.1016/j.theochem.2007.04.035.

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46

da Rocha Pita, Samuel Silva, José Jair Vianna Cirino, Ricardo Bicca de Alencastro, Helena Carla Castro, Carlos Rangel Rodrigues, and Magaly Girão Albuquerque. "Molecular docking of a series of peptidomimetics in the trypanothione binding site of T. cruzi Trypanothione Reductase." Journal of Molecular Graphics and Modelling 28, no. 4 (2009): 330–35. http://dx.doi.org/10.1016/j.jmgm.2009.08.011.

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47

Chibale, Kelly, and Chitalu Musonda. "The Synthesis of Parasitic Cysteine Protease and Trypanothione Reductase Inhibitors." Current Medicinal Chemistry 10, no. 18 (2003): 1863–89. http://dx.doi.org/10.2174/0929867033456963.

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48

Kothandan, Ram, Muthusaravanan Sivaramakrishnan, Vivek Jagadeesan Sharavanan, Ramakrishnan Sivasubramanian, and Vinohar Stephen Rapheal. "MOLECULAR DOCKING STUDIES OF PHYTOCHEMICALS AGAINST LEISHMANIA DONOVANI TRYPANOTHIONE REDUCTASE." International Research Journal of Pharmacy 9, no. 1 (2018): 61–65. http://dx.doi.org/10.7897/2230-8407.0919.

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49

Duyzend, Michael H., Christopher T. Clark, Shayna L. Simmons, et al. "Synthesis and evaluation of substrate analogue inhibitors of trypanothione reductase." Journal of Enzyme Inhibition and Medicinal Chemistry 27, no. 6 (2011): 784–94. http://dx.doi.org/10.3109/14756366.2011.604319.

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50

Girault, Sophie, Elisabeth Davioud-Charvet, Louis Maes, et al. "Potent and specific inhibitors of trypanothione reductase from Trypanosoma cruzi." Bioorganic & Medicinal Chemistry 9, no. 4 (2001): 837–46. http://dx.doi.org/10.1016/s0968-0896(00)00312-6.

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