Mikulik K, Benada O, Anderova M
Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.
Biochem Biophys Res Commun. 1992 Jan 15;182(1):425-31. doi: 10.1016/s0006-291x(05)80162-7.
Ribulose-1,5-bisphosphate carboxylase was isolated from thermophilic hydrogen-oxidizing Bacillus schlegelii. Molecular mass of the native enzyme is 560,000 and optimal reaction temperature is 70 degrees C. Km value for ribulose 1,5-bisphosphate is 0.27 mM. The carboxylase activity of the enzyme is dependent on Mg2+ with the optimum at 10 mM. The enzyme is an oligomer of L8S8 type with Mr of large subunits and small subunits of 56,000 and 14,000, respectively. Negatively stained enzyme has regular polygonal shape in top view, 12 nm in diameter, with central electron dense patch.
1,5-二磷酸核酮糖羧化酶是从嗜热氢氧化施氏芽孢杆菌中分离得到的。天然酶的分子量为560,000，最佳反应温度为70℃。1,5-二磷酸核酮糖的Km值为0.27 mM。该酶的羧化酶活性依赖于Mg2+，最佳浓度为10 mM。该酶是L8S8型寡聚体，大亚基和小亚基的Mr分别为56,000和14,000。负染后的酶在顶视图中呈规则的多边形，直径为12 nm，中央有电子致密斑。
