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Mosquito has a single multisubstrate deoxyribonucleoside kinase characterized by unique substrate specificity

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Authors:
  • Knecht, Wolfgang ;
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    Department of Systems Biology, Technical University of Denmark
  • Petersen, G.E. ;
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    unknown
  • Sandrini, Michael ;
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    Department of Systems Biology, Technical University of Denmark
  • Søndergaard, L. ;
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    unknown
  • Munch-Petersen, B. ;
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    unknown
  • Piskur, Jure
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    Department of Systems Biology, Technical University of Denmark
DOI:
10.1093/nar/gkg257
Abstract:
In mammals four deoxyribonucleoside kinases, with a relatively restricted specificity, catalyze the phosphorylation of the four natural deoxyribonucleosides. When cultured mosquito cells, originating from the malaria vector Anopheles gambiae, were examined for deoxyribonucleoside kinase activities, only a single enzyme was isolated. Subsequently, the corresponding gene was cloned and over-expressed. While the mosquito kinase (Ag-dNK) phosphorylated all four natural deoxyribonucleosides, it displayed an unexpectedly higher relative efficiency for the phosphorylation of purine versus pyrimidine deoxyribonucleosides than the fruit fly multisubstrate deoxyribonucleoside kinase (EC 2.7.1.145). In addition, Ag-dNK could also phosphorylate some medically interesting nucleoside analogs, like stavudine (D4T), 2-chloro-deoxyadenosine (CdA) and 5-bromo-vinyl-deoxyuridine (BVDU). Although the biological significance of multisubstrate deoxyribonucleoside kinases and their diversity among insects remains unclear, the observed variation provides a whole range of applications, as species specific and highly selective targets for insecticides, they have a potential to be used in the enzymatic production of various (di-)(deoxy-)ribonucleoside monophosphates, and as suicide genes in gene therapy.
Type:
Journal article
Language:
English
Published in:
Nucleic Acids Research, 2003, Vol 31, Issue 6, p. 1665-1672
Keywords:
Substrate Specificity
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2003
Scientific Level:
Scientific
ID:
40647009

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