Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F24%3A00584660" target="_blank" >RIV/60077344:_____/24:00584660 - isvavai.cz</a>
Alternative codes found
RIV/61988987:17310/24:A2502O8S RIV/00216208:11310/24:10479660
Result on the web
<a href="https://doi.org/10.1093/gbe/evae042" target="_blank" >https://doi.org/10.1093/gbe/evae042</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/gbe/evae042" target="_blank" >10.1093/gbe/evae042</a>
Alternative languages
Result language
angličtina
Original language name
Distribution and Functional Analysis of Isocitrate Dehydrogenases across Kinetoplastids
Original language description
Isocitrate dehydrogenase is an enzyme converting isocitrate to alpha-ketoglutarate in the canonical tricarboxylic acid (TCA) cycle. There are three different types of isocitrate dehydrogenase documented in eukaryotes. Our study points out the complex evolutionary history of isocitrate dehydrogenases across kinetoplastids, where the common ancestor of Trypanosomatidae and Bodonidae was equipped with two isoforms of the isocitrate dehydrogenase enzyme: the NADP(+)-dependent isocitrate dehydrogenase 1 with possibly dual localization in the cytosol and mitochondrion and NADP(+)-dependent mitochondrial isocitrate dehydrogenase 2. In the extant trypanosomatids, isocitrate dehydrogenase 1 is present only in a few species suggesting that it was lost upon separation of Trypanosoma spp. and replaced by the mainly NADP+-dependent cytosolic isocitrate dehydrogenase 3 of bacterial origin in all the derived lineages. In this study, we experimentally demonstrate that the omnipresent isocitrate dehydrogenase 2 has a dual localization in both mitochondrion and cytosol in at least four species that possess only this isoform. The apparent lack of the NAD(+)-dependent isocitrate dehydrogenase activity in trypanosomatid mitochondrion provides further support to the existence of the noncanonical TCA cycle across trypanosomatids and the bidirectional activity of isocitrate dehydrogenase 3 when operating with NADP(+) cofactor instead of NAD(+). This observation can be extended to all 17 species analyzed in this study, except for Leishmania mexicana, which showed only low isocitrate dehydrogenase activity in the cytosol. The variability in isocitrate oxidation capacity among species may reflect the distinct metabolic strategies and needs for reduced cofactors in particular environments.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LUASK22033" target="_blank" >LUASK22033: Trypanosomatid biochemistry: an insight from the neglected groups</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Genome Biology and Evolution
ISSN
1759-6653
e-ISSN
1759-6653
Volume of the periodical
16
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
evae042
UT code for WoS article
001186413600001
EID of the result in the Scopus database
2-s2.0-85188150345