An enigmatic catalase of Blastocrithidia
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
31276694
DOI
10.1016/j.molbiopara.2019.111199
PII: S0166-6851(19)30068-4
Knihovny.cz E-resources
- Keywords
- Catalase, Oxygen peroxide, Trypanosomatidae,
- 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
- Names of Substances
- Catalase MeSH
- Hydrogen Peroxide MeSH
- Protozoan Proteins 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.
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
References provided by Crossref.org
Comparative Analysis of Three Trypanosomatid Catalases of Different Origin
Catalase impairs Leishmania mexicana development and virulence
Genomics of Trypanosomatidae: Where We Stand and What Needs to Be Done?
The Remarkable Metabolism of Vickermania ingenoplastis: Genomic Predictions
Catalase and Ascorbate Peroxidase in Euglenozoan Protists
