Avtor/Urednik		Knecht, Wolfang; Petersen, Gitte Ebert; Sandrini, Michael P; Sondergaard, Leif; Munch-Petersen, Birgitte; Piškur, Jure
Naslov		Mosquito has a single multisubstrate deoxyribonucleoside kinase characterized by unique substrate specificity
Tip		članek
Vir		Nucleic Acids Res purification/*metabolism
Vol. in št.		Letnik 31, št. 6
Leto izdaje		2003
Obseg		str. 1665-72
Jezik		eng
Abstrakt		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.
Deskriptorji		AMINO ACID SEQUENCE ANIMALS ANOPHELES CELL LINE CHROMATOGRAPHY, DEAE-CELLULOSE CLONING, MOLECULAR DNA, COMPLEMENTARY ELECTROPHORESIS, POLYACRYLAMIDE GEL KINETICS MOLECULAR SEQUENCE DATA PHOSPHORYLATION PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR) RECOMBINANT PROTEINS SEQUENCE ANALYSIS, DNA SEQUENCE HOMOLOGY SUBSTRATE SPECIFICITY