Siddiqui K A, Banerjee A K
Folia Microbiol (Praha). 1975;20(5):412-7. doi: 10.1007/BF02877044.
FDP aldolase was found to be present in the cell-free extracts of Rhizobium leguminosarum, Rhizobium phaseoli, Rhizobium trifolii, Rhizobium meliloti, Rhizobium lupini, Rhizobium japonicum and Rhizobium species from Arachis hypogaea and Sesbania cannabina. The enzyme in 3 representative species has optimal activity at pH 8.4 in 0.2M veronal buffer. The enzyme activity was completely lost by treatment at 60 degrees C for 15 min. The Km values were in the range from 2.38 to 4.55 X 10(-6)M FDP. Metal chelating agents inhibited enzyme activity, but monovalent or bivalent metal ions failed to stimulate the activity. Bivalent metal ions in general were rather inhibitory.
在豌豆根瘤菌、菜豆根瘤菌、三叶草根瘤菌、苜蓿根瘤菌、羽扇豆根瘤菌、日本根瘤菌以及来自花生和田菁的根瘤菌的无细胞提取物中发现了果糖二磷酸醛缩酶。3个代表性菌种中的该酶在0.2M巴比妥缓冲液中pH 8.4时具有最佳活性。在60℃处理15分钟后酶活性完全丧失。米氏常数在2.38至4.55×10⁻⁶M果糖二磷酸的范围内。金属螯合剂抑制酶活性,但单价或二价金属离子未能刺激其活性。一般来说,二价金属离子具有抑制作用。