Trans-N-deoxyribosylase: purification by affinity chromatography and characterization.
trans-N-Deoxyribosylase (EC 2.4.2.6) is usually considered as a single protein catalyzing indifferently the transfer of the deoxyribosyl moiety to and from a purine or a pyrimidine base. Affinity chromatography of an extract from Lactobacillus helveticus with two types of ligands allowed the separation and purification of two distinct trans-N-deoxyribosylases. One catalyzes specifically the deoxyribosyl transfer to and from purine bases exclusively: trans-N-deoxyribosylase-I, the other catalyzes the transfer to and from pyrimidine and purine bases: trans-N-deoxyribosylase-II. A Tris inhibition study showed a markedly different susceptibility of the two enzymes. Preliminary results indicate that the purine-specific enzyme is a polymeric enzyme of molecular weight 86 000 (+/- 4000).
D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003853:Deoxyribonucleosides; D004589:Electrophoresis, Disc; D007778:Lactobacillus / Q000201:enzymology; D008970:Molecular Weight; D010430:Pentosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D010655:Phenylenediamines; D011687:Purines; D014325:Tromethamine / Q000494:pharmacology
D003853:Deoxyribonucleosides; D010655:Phenylenediamines; D011687:Purines; D014325:Tromethamine; D010430:Pentosyltransferases; C021888:nucleoside deoxyribosyltransferase