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An enigmatic catalase of Blastocrithidia
C. Bianchi, AY. Kostygov, N. Kraeva, K. Záhonová, E. Horáková, R. Sobotka, J. Lukeš, V. Yurchenko,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Phylogeny MeSH
- Catalase chemistry genetics metabolism MeSH
- Evolution, Molecular MeSH
- Hydrogen Peroxide chemistry metabolism MeSH
- Protozoan Proteins chemistry genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Trypanosomatina classification enzymology genetics metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Here we report that trypanosomatid flagellates of the genus Blastocrithidia possess catalase. This enzyme is not phylogenetically related to the previously characterized catalases in other monoxenous trypanosomatids, suggesting that their genes have been acquired independently. Surprisingly, Blastocrithidia catalase is less enzymatically active, compared to its counterpart from Leptomonas pyrrhocoris, posing an intriguing biological question why this gene has been retained in the evolution of trypanosomatids.
Department of Parasitology Faculty of Science Charles University BIOCEV Prague Czech Republic
Faculty of Sciences University of South Bohemia České Budějovice Czech Republic
Institute of Microbiology Czech Academy of Sciences Třeboň Czech Republic
Institute of Parasitology Biology Centre Czech Academy of Sciences České Budějovice Czech Republic
Life Science Research Centre Faculty of Science University of Ostrava Ostrava Czech Republic
Zoological Institute of the Russian Academy of Sciences St Petersburg Russia
References provided by Crossref.org
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