title: Vitamin B6-dependent enzymes in the human malaria parasite Plasmodium falciparum: a druggable target?
abstract: 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).
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Thales
authors: T
authors: Kronenberger
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Jasmin
authors: J
authors: Lindner
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Kamila A
authors: KA
authors: Meissner
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Flávia M
authors: FM
authors: Zimbres
authors: Multi User Center for Biomolecular Innovation, Department of Physics, São Paulo State University, UNESP/IBILCE, C. Postal 136, 15054-000 São José do Rio Preto, SP, Brazil.
authors: Monika A
authors: MA
authors: Coronado
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Frank M
authors: FM
authors: Sauer
authors: Laboratory of Genetics and Molecular Cardiology, Heart Institute (InCor), Avenida Doctor Eneas de Carvalho Aguiar 44, 05403-000 São Paulo, SP, Brazil.
authors: Isolmar
authors: I
authors: Schettert
authors: Unit for Drug Discovery, Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 São Paulo, SP, Brazil.
authors: Carsten
authors: C
authors: Wrenger
mesh_terms: D000818:Animals; D000975:Antioxidants / Q000378:metabolism; D001219:Aspartate Aminotransferases / Q000235:genetics / Q000378:metabolism*; D012696:Glycine Hydroxymethyltransferase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008288:Malaria / Q000201:enzymology* / Q000235:genetics / Q000469:parasitology; D009955:Ornithine Decarboxylase / Q000235:genetics / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity; D025101:Vitamin B 6 / Q000378:metabolism
chemical_list: D000975:Antioxidants; D025101:Vitamin B 6; D012696:Glycine Hydroxymethyltransferase; D001219:Aspartate Aminotransferases; D009955:Ornithine Decarboxylase