Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target?
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1155/2014/108516 http://hdl.handle.net/11449/112894 |
Resumo: | Malaria is a deadly infectious disease which affects millions of people each year in tropical regions. There is no effective vaccine available and the treatment is based on drugs which are currently facing an emergence of drug resistance and in this sense the search for new drug targets is indispensable. It is well established that vitamin biosynthetic pathways, such as the vitamin B6 de novo synthesis present in Plasmodium, are excellent drug targets. The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes present in the malaria parasite which includes the ornithine decarboxylase (ODC, synthesis of polyamines), the aspartate aminotransferase (AspAT, involved in the protein biosynthesis), and the serine hydroxymethyltransferase (SHMT, a key enzyme within the folate metabolism). |
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Repositório Institucional da UNESP |
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2946 |
spelling |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target?Malaria is a deadly infectious disease which affects millions of people each year in tropical regions. There is no effective vaccine available and the treatment is based on drugs which are currently facing an emergence of drug resistance and in this sense the search for new drug targets is indispensable. It is well established that vitamin biosynthetic pathways, such as the vitamin B6 de novo synthesis present in Plasmodium, are excellent drug targets. The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes present in the malaria parasite which includes the ornithine decarboxylase (ODC, synthesis of polyamines), the aspartate aminotransferase (AspAT, involved in the protein biosynthesis), and the serine hydroxymethyltransferase (SHMT, a key enzyme within the folate metabolism).Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ Sao Paulo, Inst Biomed Sci, Dept Parasitol, Unit Drug Discovery, BR-05508000 Sao Paulo, BrazilSao Paulo State Univ, Dept Phys, Multi User Ctr Biomol Innovat, UNESP IBILCE, BR-15054000 Sao Jose Do Rio Preto, SP, BrazilHeart Inst InCor, Lab Genet & Mol Cardiol, BR-05403000 Sao Paulo, BrazilSao Paulo State Univ, Dept Phys, Multi User Ctr Biomol Innovat, UNESP IBILCE, BR-15054000 Sao Jose Do Rio Preto, SP, BrazilFAPESP: 09/54325-2FAPESP: 10/20647-0FAPESP: 11/13706-3FAPESP: 11/19703-6FAPESP: 12/12807-3FAPESP: 12/12790-3FAPESP: 13/10288-1CAPES: 348/2013Hindawi Publishing CorporationUniversidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Kronenberger, ThalesLindner, JasminMeissner, Kamila A.Zimbres, Flavia M.Coronado, Monika A. [UNESP]Sauer, Frank M.Schettert, IsolmarWrenger, Carsten2014-12-03T13:11:08Z2014-12-03T13:11:08Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11application/pdfhttp://dx.doi.org/10.1155/2014/108516Biomed Research International. New York: Hindawi Publishing Corporation, 11 p., 2014.2314-6133http://hdl.handle.net/11449/11289410.1155/2014/108516WOS:000330391500001WOS000330391500001.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBioMed Research International2.5830,935info:eu-repo/semantics/openAccess2023-09-30T06:03:32Zoai:repositorio.unesp.br:11449/112894Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T13:33:39.000974Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
title |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
spellingShingle |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? Kronenberger, Thales |
title_short |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
title_full |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
title_fullStr |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
title_full_unstemmed |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
title_sort |
Vitamin B6-Dependent Enzymes in the Human Malaria Parasite Plasmodium falciparum: A Druggable Target? |
author |
Kronenberger, Thales |
author_facet |
Kronenberger, Thales Lindner, Jasmin Meissner, Kamila A. Zimbres, Flavia M. Coronado, Monika A. [UNESP] Sauer, Frank M. Schettert, Isolmar Wrenger, Carsten |
author_role |
author |
author2 |
Lindner, Jasmin Meissner, Kamila A. Zimbres, Flavia M. Coronado, Monika A. [UNESP] Sauer, Frank M. Schettert, Isolmar Wrenger, Carsten |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Kronenberger, Thales Lindner, Jasmin Meissner, Kamila A. Zimbres, Flavia M. Coronado, Monika A. [UNESP] Sauer, Frank M. Schettert, Isolmar Wrenger, Carsten |
description |
Malaria is a deadly infectious disease which affects millions of people each year in tropical regions. There is no effective vaccine available and the treatment is based on drugs which are currently facing an emergence of drug resistance and in this sense the search for new drug targets is indispensable. It is well established that vitamin biosynthetic pathways, such as the vitamin B6 de novo synthesis present in Plasmodium, are excellent drug targets. The active form of vitamin B6, pyridoxal 5-phosphate, is, besides its antioxidative properties, a cofactor for a variety of essential enzymes present in the malaria parasite which includes the ornithine decarboxylase (ODC, synthesis of polyamines), the aspartate aminotransferase (AspAT, involved in the protein biosynthesis), and the serine hydroxymethyltransferase (SHMT, a key enzyme within the folate metabolism). |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-12-03T13:11:08Z 2014-12-03T13:11:08Z 2014-01-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1155/2014/108516 Biomed Research International. New York: Hindawi Publishing Corporation, 11 p., 2014. 2314-6133 http://hdl.handle.net/11449/112894 10.1155/2014/108516 WOS:000330391500001 WOS000330391500001.pdf |
url |
http://dx.doi.org/10.1155/2014/108516 http://hdl.handle.net/11449/112894 |
identifier_str_mv |
Biomed Research International. New York: Hindawi Publishing Corporation, 11 p., 2014. 2314-6133 10.1155/2014/108516 WOS:000330391500001 WOS000330391500001.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BioMed Research International 2.583 0,935 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
11 application/pdf |
dc.publisher.none.fl_str_mv |
Hindawi Publishing Corporation |
publisher.none.fl_str_mv |
Hindawi Publishing Corporation |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128247329718272 |