当前位置： SCI文献检索 > BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS期刊下所有文献 > 9-Beta-D-arabinofuranosyladenine 5'-monophosphate (araAMP) is converted directly to its antivirally active 5'-triphosphate form by 5-phosphoribosyl-1-pyrophosphate (PRPP) synthetase.

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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Balzarini J,De Clercq E

doi

10.1016/s0006-291x(05)80855-1

subject

Has Abstract

pub_date

1990-12-31 00:00:00

pages

781-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)80855-1

journal_volume

173

pub_type

杂志文章

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