| Title | Phosphorylation of 9-(2-phosphonomethoxyethyl)adenine and 9-(S)-(3-hydroxy-2-phosphonomethoxypropyl)adenine by AMP (dAMP) kinase from L1210 cells |
| Publication Type | Journal Article |
| Year of Publication | 1992 |
| Authors | Merta A, Votruba I, Jindrich J, Holy A, Cihlar T, Rosenberg I, Otmar M, Herve TY |
| Journal | Biochemical Pharmacology |
| Volume | 44 |
| Issue | 10 |
| Pagination | 2067 - 2077 |
| Date Published | 1992/11/07/ |
| ISBN Number | 0006-2952 |
| Keywords | duplicate |
| Abstract | 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. |
| URL | http://apps.isiknowledge.com/full_record.do?product=WOS&search_mode=GeneralSearch&qid=2&SID=Q2aIOAe32iKPO787Bf4&page=1&doc=29&cacheurlFromRightClick=no |
| Short Title | Biochem. Pharmacol. |
