A multisubstrate deoxyribonucleoside kinase from plants.
Deoxyribonucleoside kinases catalyze the rate limiting step during the salvage of deoxyribonucleosides and convert them into the corresponding monophosphate compounds. We have identified and characterized a unique multisubstrate deoxyribonucleoside kinase from plants. The phylogenetic relationship and biochemical properties suggest that this deoxyribonucleoside kinase represents a living fossil resembling the progenitor of the modern animal deoxycytidine, deoxyguanosine and thymidine 2 kinases. The broad substrate specificity makes this enzyme an interesting candidate to be evaluated as a suicide gene in anti-cancer therapy.
Clausen
Anders Ranegaard
AR
Department of Cell and Organism Biology, Lund University, SE - 223 62 Lund, Sweden. anders.clausen@cob.lu.se
Girandon
Lenart
L
Knecht
Wolfgang
W
Survery
Sabeen
S
Andreasson
Erik
E
Munch-Petersen
Birgitte
B
Piskur
Jure
J
D017360:Arabidopsis / Q000201:enzymology; D029681:Arabidopsis Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D013379:Substrate Specificity
D029681:Arabidopsis Proteins; D017853:Phosphotransferases (Alcohol Group Acceptor); C020018:deoxyribonucleoside kinases