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.
Streptomyces sp. J-350P가 생산하는 세포외 adenine deaminase의 adenine에 대한 Km 값은 5.8$\times$$10^{-5}$M로 측정되었으며 Arrhenius plots에 의한 효소의 활성화 에너지는 3.13 Kcal/mole로 측정되었다. 검토된 purine analogue중에서 6-chloropurine, 2,6-diaminopurine, 6-bromopurine, 4-aminopyrazolo (3,4-d) pyrimidine, 6-iodopurine, 그리고 8-bromoadenine은 본 효소에 의해 기질로 이용되었으며, 6-dimethylaminopurine은 adenine에 대한 경쟁적 저해제로 작용하였다. 본 효소는 0.1mM의 Fe$^{3+}$, Ag$^+$ 등에 의해 저해되었으며, 1mM의 $\alpha$, $\alpha$＇-dipyridyl, Pentachiorophenol, p-CMB 등에 의해 저해되었다.