The Enzymatic Properties of Extracellular Adenine Deaminnse from Streptomyces sp. J-350P

Streptomyces sp. J-350P가 생산하는 세포외 Adenine Deaminase의 효소학적 성질

  • 전홍기 (부산대학교 자연과학대학 미생물학과) ;
  • 박정혜 (부산대학교 자연과학대학 미생물학과) ;
  • 김태숙 (부산대학교 자연과학대학 미생물학과)
  • Published : 1987.10.01

Abstract

The apparent Michaelis constant Km of extracellular adenine deaminase from Streptomyces sp. J-350P was 5.8$\times$10$^{-5}$M. The activation energy or the enzyme was calculated from Arrhenius plots for adenine and the value was 3.13 Kcal/mole. The purine analogues, 6-chloropurine, 2,6-diaminopurine, 6-bromopurine, 4-aminopyrazolo[3,4-d] pyrimidine, 6-iodopurine, and 8-bromoadenine were substrates for the enzyme. 6-Dimethylaminopurine was a competitive inhibitor of the enzyme. The enzyme was inhibited by 0.1mM of Fe$^{3+}$, Ag+, and Hg$^{2+}$ and 1 mM of $\alpha$, $\alpha$'-dipyridyl, Penta-chiorophenol, and p-chloromercuribenzoate.

Keywords

Extracellular adenine deaminase;enzymatic properties