Lyase activity of nucleoside 2-deoxyribosyltransferase: transient generation of ribal and its use in the synthesis of 2'-deoxynucleosides

In the absence of acceptors nucleoside 2-deoxyribosyltransferase catalyzes the slow hydrolysis of 2'-deoxynucleosides. During this hydrolytic reaction, D-ribal (1,4-anhydro-2-deoxy-D-erythro-pent-1-enitol), a glycal of ribose hitherto encountered only as a reagent in organic synthesis, is generated spontaneously, disappearing later as 2'-deoxynucleoside hydrolysis approaches completion. Nucleoside 2-deoxyribosyltransferase is found to catalyze the hydration of D-ribal in the absence of nucleic acid bases and the synthesis of deoxyribonucleosides from ribal in their presence, affording a new method for the preparation of 2'-deoxyribonucleosides. The stereochemistry of nucleoside formation from ribal supports the intervention of deoxyribosyl-enzyme intermediate. The equilibrium constant for the covalent hydration of ribal is found to be approximately 65.