Phosphorylation of 9-(2-phosphonomethoxyethyl)adenine and 9-(S)-(3-hydroxy-2-phosphonomethoxypropyl)adenine by AMP(dAMP) kinase from L1210 cells
Jazyk angličtina Země Velká Británie, Anglie Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
1449524
DOI
10.1016/0006-2952(92)90110-5
PII: 0006-2952(92)90110-5
Knihovny.cz E-zdroje
- MeSH
- adenin analogy a deriváty metabolismus MeSH
- adenylátkinasa chemie izolace a purifikace metabolismus MeSH
- časové faktory MeSH
- izoelektrický bod MeSH
- kreatinkinasa metabolismus MeSH
- leukemie L1210 enzymologie MeSH
- molekulová hmotnost MeSH
- myši MeSH
- nádorové buňky kultivované MeSH
- organofosfonáty * MeSH
- organofosforové sloučeniny metabolismus MeSH
- substrátová specifita MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- 9-(S)-(3-hydroxy-2-(phosphonomethoxy)propyl)adenine MeSH Prohlížeč
- adefovir MeSH Prohlížeč
- adenin MeSH
- adenylátkinasa MeSH
- kreatinkinasa MeSH
- organofosfonáty * MeSH
- organofosforové sloučeniny MeSH
Acyclic nucleotide analogues 9-(2-phosphonomethoxyethyl)adenine (PMEA) and 9-(S)-(3-hydroxy-2-phosphonomethoxypropyl)adenine ((S)-HPMPA) which display potent antiviral activity are transformed in the cells to their mono- and disphosphoryl derivatives. We purified from mouse L1210 cells the enzyme that in two steps phosphorylates PMEA and (S)-HPMPA to their diphosphoryl derivatives and found that it co-purifies with AMP(dAMP) kinase activity; the best substrates of this enzyme were AMP, ADP and dAMP. Other nucleoside 5'-triphosphates or creatine phosphate could not be substituted for ATP as a phosphate donor. Our results also indicated that at least one other enzyme (creatine kinase) is capable of transforming the monophosphoryl derivatives of the studied compounds to their respective diphosphates.
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