Deoxyribosyl Transfer Catalysis with trans‐N‐Deoxyribosylase
- 1 February 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 62 (2) , 365-372
- https://doi.org/10.1111/j.1432-1033.1976.tb10168.x
Abstract
Kinetic studies were carried out in order to investigate the enzymic mechanism of a 215-fold-purified purine(pyrimidine) nucleoside:purine(pyrimidine) deoxyribosyl transferase fraction from Lactobacillus helveticus. A variety of natural deoxyribonucleosides and bases were used as substrates. Initial velocity, product inhibition and isotopic exchange studies are consistent with a ping-pong bi-bi mechanism. The kinetic parameters are used to show that this fraction is free from any contamination by a specific purine nucleoside:purine deoxyribosyl transferase also found in the same strain of L. helveticus.This publication has 10 references indexed in Scilit:
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