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Biochem Biophys Res Commun. 1990 Dec 31;173(3):781-7.

9-Beta-D-arabinofuranosyladenine 5'-monophosphate (araAMP) is converted directly to its antivirally active 5'-triphosphate form by 5-phosphoribosyl-1-pyrophosphate (PRPP) synthetase.

Author information

1
Rega Institute for Medical Research, Katholieke Universiteit Leuven, Belgium.

Abstract

The antiherpetic agent 9-beta-D-arabinofuranosyladenine (araA) needs to be phosphorylated to its 5'-triphosphate to be effective as an inhibitor of herpes simplex virus replication. Adenosine kinase and deoxycytidine kinase are assumed to convert araA to its 5'-monophosphate. We now found that araAMP is converted to its 5'-triphosphate through a direct pyrophosphate transfer from 5-phosphoribosyl-1-pyrophosphate (PRPP) by PRPP synthetase. The efficiency of phosphorylation of araAMP to araATP is about 5% of that of AMP, as estimated from their Vmax/Km ratios for PRPP synthetase. AraATP is converted to araAMP by PRPP synthetase at a 4-fold higher Km but similar Vmax as ATP.

PMID:
1702630
DOI:
10.1016/s0006-291x(05)80855-1
[Indexed for MEDLINE]

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