4hx9
From Proteopedia
Designed Phosphodeoxyribosyltransferase
Structural highlights
FunctionNTD_LACLE Catalyzes the cleavage of the glycosidic bond of 2'-deoxyribonucleosides and the transfer of the deoxyribosyl moiety to an acceptor purine or pyrimidine base.[1] [2] Publication Abstract from PubMedA large number of nucleoside analogs and 2'- deoxynucleoside triphosphates (dNTPs) have been synthesized in order to interfere with DNA metabolism. However, in vivo the concentration and phosphorylation of these analogues are key limiting factors. In this context, we designed enzymes to switch nucleobases attached to a deoxyribose monophosphate. Active chimeras were made from two distantly related enzymes: a nucleoside deoxyribosyltransferase (NDT) from lactobacilli and a 5'-monophosphate-2'-deoxyribonucleoside hydrolase (Rcl) from rat. Then, their unprecedented activity was further extended to deoxyribose triphosphate and, in vitro biosyntheses could be successfully performed with several base analogues. These new enzymes provide new tools to synthesize dNTPs analogs and to deliver them into cells. Phosphodeoxyribosyltransferases: designed enzymes for deoxyribonucleotide synthesis.,Kaminski PA, Labesse G J Biol Chem. 2013 Jan 16. PMID:23325804[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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