3-羟基邻氨基苯甲酸向朱红酸的酶促转化。大鼠肝脏朱红酸合酶的部分纯化及性质
nzymic conversion of 3-hydroxyanthranilic acid into cinnabarinic acid. Partial purification and properties of ra-liver cinnabarinate synthase.
作者信息
Rao P V, Vaidyanahan C S
出版信息
Biochem J. 1966 May;99(2):317-22. doi: 10.1042/bj0990317.
Rat-liver cinnabarinate synthase (3-hydroxyanthranilic acid-oxygen oxido-reductase) was partially purified. Stoicheiometric studies indicated the consumption of 3 atoms of oxygen/molecule of cinnabarinic acid formed. There was an initial lag in enzyme activity. The reaction had an optimum pH about 7.2 and an optimum temperature of 37 degrees . The enzyme was highly specific for 3-hydroxyanthranilic acid. The system showed an absolute requirement for Mn(2+) ions. Several bivalent metal ions and metal-chelating agents inhibited the reaction. Thiol inhibitors had no effect on enzyme activity, but reducing agents such as ascorbic acid were potent inhibitors. There was no requirement for any cofactor other than Mn(2+) ions. The probable significance of the reaction in mammals is discussed.
大鼠肝脏朱砂酸合酶（3-羟基邻氨基苯甲酸-氧氧化还原酶）得到了部分纯化。化学计量学研究表明，每形成一分子朱砂酸消耗3个氧原子。酶活性最初有一个延迟期。该反应的最适pH约为7.2，最适温度为37摄氏度。该酶对3-羟基邻氨基苯甲酸具有高度特异性。该系统对Mn(2+)离子有绝对需求。几种二价金属离子和金属螯合剂会抑制该反应。巯基抑制剂对酶活性没有影响，但诸如抗坏血酸等还原剂是强效抑制剂。除了Mn(2+)离子外，不需要任何其他辅因子。文中讨论了该反应在哺乳动物中的可能意义。
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