Enzymatic Properties of Extracellular Cytosine Deaminase

세포외 Cytosine Deaminase의 효소학적 성질

  • 유대식 (계명대학교 자연과학대학 미생물학과) ;
  • 김대현 (계명대학교 자연과학대학 미생물학과) ;
  • 박정문 (계명대학교 자연과학대학 미생물학과) ;
  • 송형익 (경북대학교 농과대학 식품공학과) ;
  • 정기택 (경북대학교 농과대학 식품공학과)
  • Published : 1988.12.01


Enzymological proprties of an extracellular cytosine deaminase from Bacellus polymyxa YL 38-3 were investigated. The extracellular enzyme was very stable, and optimum pH and temperature for the enzyme activity were found to be near pH 6.0 in 0.2M potassium phosphate buffer and at $30^{\circ}C$, respectively. 5-Fluorocytosine was converyed to 5-fluorouracil by the enzyme, but 5-methylcytosine was not to thymine by it. The enzyme activity was completely inhibited by some heavy metal ion such as 1mM of $Cd^{2-}$ and $Hg^{2+}$, and by 1mM of p-chloromercuribenzoate, respectively. The enzyme activity was inactivated about 75% by 1mM of o-phenanthroline and monoiodoacetate. But the enzyme activity was stimulated up to 200% by 1mM of 2-mercaptoethanol.


Bacilus polymyxa YL38-3;extracelluarl cytosine deaminase