Unknown

Dataset Information

0

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).

SUBMITTER: Kronenberger T 

PROVIDER: S-EPMC3912857 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

Vitamin B6-dependent enzymes in the human malaria parasite Plasmodium falciparum: a druggable target?

Kronenberger Thales T   Lindner Jasmin J   Meissner Kamila A KA   Zimbres Flávia M FM   Coronado Monika A MA   Sauer Frank M FM   Schettert Isolmar I   Wrenger Carsten C  

BioMed research international 20140109


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-  ...[more]

Similar Datasets

| S-EPMC2634962 | biostudies-literature
| S-EPMC1563505 | biostudies-literature
2006-07-11 | GSE5267 | GEO
2010-07-01 | E-GEOD-5267 | biostudies-arrayexpress
2012-02-07 | E-MTAB-673 | biostudies-arrayexpress
| S-EPMC3337437 | biostudies-literature
| S-EPMC3135974 | biostudies-literature
| S-EPMC5378400 | biostudies-literature
2023-01-30 | GSE208757 | GEO
| S-EPMC3257935 | biostudies-literature