Deoxyribosyl transfer catalysis with trans-N-deoxyribosylase. Kinetic study of purine(pyrimidine) to pyrimidine(purine) trans-N-deoxyribosylase

Eur J Biochem. 1976 Feb 16;62(2):365-72. doi: 10.1111/j.1432-1033.1976.tb10168.x.


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.

MeSH terms

  • Adenine / pharmacology
  • Deoxyadenosines / pharmacology
  • Deoxycytidine / pharmacology
  • Deoxyribonucleosides / metabolism*
  • Lactobacillus / enzymology
  • Mathematics
  • Pentosyltransferases / isolation & purification
  • Pentosyltransferases / metabolism*


  • Deoxyadenosines
  • Deoxyribonucleosides
  • Deoxycytidine
  • Pentosyltransferases
  • Adenine