Purification and Properties of Trans-N-Deoxyribosylase

MacNutt (I) was the first to demonstrate the presence of an enzyme that catalyzes the transfer of the deosyribosyl radical of deoxyribonucleosides to purines and pyrimidines in extracts of three bacterial species that require deoxyribonucleosides for growth. In addition, the presence of a deoxyribonucleoside hydrolase was noted in Lactobacillus helveticus extracts. The reaction products were identified by chromatographic methods and microbiological assays; Kalckar et al. (2) verified the transfer nature of the reaction with the aid of U4-adenine. Hoffmann (3) and Lampen (4) have reported briefly on similar enzymes in Escherichia coli. The present paper describes some of the properties of a partly purified enzyme from L. helveticus extracts which we call “transN-deoxyribosylase” (MacNutt (I) named the enzyme “transN-glycosidase”). Auxiliary enzymes have been used to detect and determine the products of the reaction.