해녀콩(Canavalia lineata)의 뿌리에서 분리한 Rhizobium sp. SNU 003은 arginine에 의해서는 생육이 촉진되나 canavanine에 의해서는 생육이 억제된다. 또한 2mM의 canavanine에 의해 억제된 생육은 2~20 mM의 arginine 첨가에 의해 약 78~95%의 회복을 보여주었다. Rhizobium에서 arginine의 대사는 arginine deiminase의 작용으로 시작되며, arginine의 존재로 이 효소의 활성은 약 10배 증가하였다. Arginine deiminase는 protamine sulfate에 의한 침전, DEAE-Sephacel 이온교환 크로마토그래피와 Sephacryl S-300 gel 크로마토그래피에 의하여 45배로 정제되었으며, 회수율은 11%였다. Sephacryl S-300 gel 컬럼 크로마토그래피로 분자량은 190,000임을 알았다. Sodiumacetate 완충용액에서의 활성 최적온도는 $30^{circ}C$, 최적 pH는 6.0으로 밝혀졌다. Canavanine은 기질로서 이용될 수 없으며, arginine의 이용을 경쟁적으로 억제하였다. 효소의 활성은 $Co^{2+}$, $Al^{3+}$, $Pb^{2+}$ 및 $Zn^{2+}$에 의해서는 억제되었으나, 10 mM의 $Mg^{2+}$와 $Mn^{2+}$에 의해서는 30~40% 증가하였다.
The growth of Rhizobium sp. SNU 003 isolated from the nodule of Canaialia lineata was inhibited by canavanine and promoted by arginine. The growth inhibited by 2 mM canavanine was approximately shown 78 - 95% recovery by the addition of 2 - 20 mM arginine. Arginine deiminase of this Rhizobium is an active catabolic enzyme of arginine and the enzyme activity was promoted about 10-times when arginine was added into the medium. Arginine deminase was purified 45-fold and the yield was 11% by the following steps: Protamine sulfate and ammonium sulfate precipitation, DEAE-Sephacel chromatography, and Sephacryl S-300 gel chromatography. The molecular weight of the native enzyme was 190,000 by gel filtration and optimum temperature for activity was $30^{circ}C$. Enzyme showed the highest activity at pH 6.0 in the sodium-acetate buffer. Canavanine was not catabolized by arginine deiminase and competitively inhibited the degradation of arginine. The activity of enzyme was inhibited by $Co^{2+}$, $Al^{3+}$, $Cu^{2+}$, $Pb^{2+}$ and $Zn^{2+}$, however promoted by 10 mM of $Mg^{2+}$ and $Mn^{2+}$ approximately 30 - 40%.
