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Hydrolytic cleavage of N-6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases
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SYSNO ASEP 0324946 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Hydrolytic cleavage of N-6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases Překlad názvu Hydrolytické štěpení N6-substituovaných derivátů adeninu eukaryontními adenin- a adenosindeaminasami Tvůrce(i) Pospíšilová, H. (CZ)
Šebela, M. (CZ)
Novák, Ondřej (UEB-Q) RID, ORCID, SAI
Frébort, I. (CZ)Zdroj.dok. Bioscience Reports. - : Portland Press - ISSN 0144-8463
Roč. 28, č. 6 (2008), s. 335-347Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova adenine deaminase ; adenosine deaminase (ADA) ; aminohydrolase Vědní obor RIV EB - Genetika a molekulární biologie CEP GA522/06/0022 GA ČR - Grantová agentura ČR CEZ AV0Z50380511 - UEB-Q (2005-2011) UT WOS 000262397300005 DOI 10.1042/BSR20080081 Anotace Synopsis 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 k(cat) 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 NB-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 for a reference sample of human ADA1. ADA1, however, showed a different reaction mechanism to that of the yeast enzymes, hydrolysing the compounds to an adenine derivative and a side chain alcohol. The reaction products were identified using reference compounds on HPLC coupled to UV and Q-TOF (quadrupole-time-of-flight) detectors. The ADA1 activity may constitute the debenzylation metabolic route already described for bohemine and, as a consequence, it may compromise the physiological or therapeutic effects of exogenously applied cytokinin derivatives. Pracoviště Ústav experimentální botaniky Kontakt David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Rok sběru 2009
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