Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10099222" target="_blank" >RIV/00216208:11310/11:10099222 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.molbiopara.2010.10.004" target="_blank" >http://dx.doi.org/10.1016/j.molbiopara.2010.10.004</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.molbiopara.2010.10.004" target="_blank" >10.1016/j.molbiopara.2010.10.004</a>
Alternative languages
Result language
angličtina
Original language name
Hydrogenosome-localization of arginine deiminase in Trichomonas vaginalis
Original language description
The arginine dihydrolase (ADH) pathway has an analogous function to the urea cycle in mitochondria-containing cells, by removing nitrogen from amino acids and generating ATP. Subcellular localization of the ADH pathway enzymes in Trichomonas vagina lis revealed that arginine deiminase (ADI) localizes to the hydrogenosome, a mitochondrion-like organelle of anaerobic protists. However the other enzymes of the ADH pathway, ornithine carbamyltransferase and carbamate kinase localize to the cytosol. Three gene sequences of T. vaginalis ADI (ADI 1-3) were identified in the T. vaginalis genome, all having putative mitochondrial targeting sequences. The ADI sequences were cloned and used to probe T. vaginalis using a carboxyterminal di-hemogglutinin epitope tag which demonstrated co-localization with malic enzyme confirming the hydrogenosome localization of this enzyme.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
<a href="/en/project/LC07032" target="_blank" >LC07032: Center for Functional Genetics</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecular and Biochemical Parasitology
ISSN
0166-6851
e-ISSN
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Volume of the periodical
176
Issue of the periodical within the volume
1
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
4
Pages from-to
51-54
UT code for WoS article
000287284800007
EID of the result in the Scopus database
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