Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F08%3A00005307" target="_blank" >RIV/61989592:15310/08:00005307 - isvavai.cz</a>
Alternative codes found
RIV/61389030:_____/08:00324946
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases.
Original language description
Homogeneous adenine deaminases (EC 3.5.4.2) from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and a putative ADA (adenosine deaminase; EC 3.5.4.4) from Arabidopsis thaliana were obtained for the first time as purified recombinant proteins by molecular cloning of the corresponding genes and their overexpression in Escherichia coli. The enzymes showed comparable molecular properties with well known mammalian ADAs, but exhibited much lower kcat values. Adenine was the most favoured substrate for the yeast enzymes, whereas the plant enzyme showed only very low activities with either adenine, adenosine, AMP or ATP. Interestingly, the yeast enzymes also hydrolysed N6-substituted adenines from cytokinins, a group of plant hormones, cleaving them to inosine and the corresponding side chain amine. The hydrolytic cleavage of synthetic cytokinin 2,6-di-substituted analogues that are used in cancer therapy, such as olomoucine, roscovitine and bohemine, was subsequently shown f
Czech name
Hydrolytické štěpení N6-substituovaných derivátů adeninu eukaryontními adenin- a adenosindeaminasami
Czech description
Expresí v E. coli byly připraveny tři rekombinantní enzymy - adenindeaminasy (EC 3.5.4.2) z kvasinek Saccharomyces cerevisiae a Schizosaccharomyces pombe a domnělá adenosindeaminasa ( EC 3.5.4.4) z Arabidopsis thaliana. Tyto enzymy byly charakterizoványenzymologickými postupy a bylo zjištěno, že mají podobné molekulové vlastnosti jako savčí adenosindeaminasy, ale přitom podstatně nižší katalytickou aktivitu. Enzymy z kvasinek působily kromě adeninu i na N6-substituované deriváty adeninu ze skupiny cytokininů. S použitím referenční lidské adenosindeaminasy byl studován hydrolytický účinek vůči 2,6-disubstituovaným cytokininovým analogům, které se používají v protinádorové terapii. Byl zjištěn odlišný mechanismus hydrolýzy.
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA522%2F06%2F0022" target="_blank" >GA522/06/0022: Alternative pathway of cytokinin catabolism</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2008
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Bioscience Reports
ISSN
0144-8463
e-ISSN
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Volume of the periodical
28
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
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UT code for WoS article
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EID of the result in the Scopus database
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